Neurodevelopmental and Neurocognitive Disorders Essay

Neurodevelopmental and Neurocognitive Disorders Essay
Neurodevelopmental and Neurocognitive Disorders Until the twentieth century, little account was
taken of the special characteristics of psychopathology in children; maladaptive patterns considered
relatively specific to childhood, such as autism, received virtually no attention at all (Butcher &
Hooley, 2014). Today there is more attention paid to children with maladaptive behaviors and
scientific research has been done that demands more attention is paid to specific children's
behaviors, not the behaviors of adult as there are no fair comparisons that allow the diagnosis and
treatments of adult and children's behaviors to be equal. Neurodevelopment disorders in children
result in maladaptive behavior which appears in different life ... Show more content on
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N., Hooley, J. M., Mineka, 2014). The causal factors for ADHD in children have been much
debated. It still remains unclear to what extent the disorder results from environmental or biological
factors (Carr et al., 2006; Hinshaw et al., 2007), and recent researchers believe that biological
factors such as genetic inheritance will turn out to be important precursors to the development of
ADHD (Durston, 2003). But firm conclusions about any biological basis for ADHD must await
further research (Butcher & Hooley, 2014, p. 513). Treatment for ADHD that focuses on controlling
behavior with drugs has been promising. One particular treatment involved the effectiveness of
MTA fading procedures. According to the article, the findings suggest that in contrast to the
hypothesized deterioration in the relative benefit of behavioral modification between nine and 14
months (after completion of fading), the MTA behavior generalization and maintenance procedures
implemented through nine months apparently yield continuing improvement through 14 months,
with preservation of the relative position of behavior compared
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Symptoms And Diagnosis Of Alzheimer 's Disease
Word Count: 1840
It is estimated that currently 5.1 million Americans may have Alzheimer's disease. [1] 60–70% of
dementia cases in the elderly are caused by Alzheimer's. [2] As the population ages a greater
percentage of Americans will be impacted whereas between present time and 2050 it is estimated
that 20 percent of the population will be in an age category that puts them at risk. [1] The disease is
a progressive, degenerative disorder that attacks the neurons resulting in memory loss, language
skills, thinking and behavioral changes. Diagnostic and therapeutic approaches to this disease are
changing due to knowledge that the underlying pathology begins 10–20 years before the symptoms
appear. [3] Therefore new methods are ... Show more content on Helpwriting.net ...
[5] In an Alzheimer's Dementia brain the insoluble A exceeds soluble forms of A by a factor of
about 100–fold. [6] It has been indicated that these plaques can be cleared. [7] Plaques are
composed of insoluble A peptides, mostly 42 amino acids in length (A–42) [8]
Knowledge of the initial deposition of A plaques is important to improve understanding of early
Alzheimer's Dementia pathology. It is suggested that APP mismetabolism and subsequent A
aggregation are the primary events driving pathogenesis. [9] Mutations in the A precursor protein
gene on chromosome 21, lying in or near the Apeptide region, cause early–onset, autosomal
dominant familial forms of Alzheimer's Dementia. [10] The deposition of A is likely important for
signifying the beginning of the pathological cascade even if it may not be the only or main causal
event. However, since all young healthy persons and many older individuals (who do not have
Alzheimer's Dementia) have no evidence of A deposition the conversion of a non–demented
individual with no evidence of A plaques to A deposits in a cerebral distribution suggests a
pathological event.
Biomarkers provide a unique, useful biological measure of the underlying pathology independent of
any clinical signs and neuropsychological characteristics of Alzheimer's Dementia. Identification of
reliable biomarkers is critical

Preventative Methods Of Alzheimer's Disease
Preventative Methods of Alzheimer's disease
Now that the disparity between Alzheimer's disease prevalence in men and women, as well as the
different rates of incidence in different countries has been established, it is now applicable to discuss
what can be done to prevent this disease. There are many ways that researchers believe people can
use to prevent Alzheimer's disease. Studies by researchers have found that cannabinoids could
stimulate the brain cells and slow the progression of the disease. Conversely, some believe that
Alzheimer's is impossible to fight, regardless of the precautions taken. This paper will examine
Alzheimer's disease and also explore in depth on the following topics: the prevalence of Alzheimer's
in males vs. ... Show more content on Helpwriting.net ...
Frank Longo said it best when he stated," We have cured Alzheimer's in mice. Why can't we move
that success to people?" (Time Magazine)
There is research that suggests altering the lifestyle can lower the risk of developing Alzheimer's
disease. There are also two more ways that people can stay healthy and they are: using cannabinoids
and avoiding benzodiazepines. The former is found in marijuana and the latter in anxiety, epilepsy,
and sleep medications. In the benzodiazepine study, the researchers took hundreds of Canadian
participants that were over the age of 66 and grouped them based on whether they had ever used
benzodiazepines. This research was conducted by de Gage, Moride, Ducruet, Kurth, Verdoux,
Tournier, Pariente, and Begaud in 2014. The study on cannabinoids, a significant component found
in marijuana, was done by Bachmeier, Beaulieu–Abdelahad, Mullan, and Paris in 2013. These
studies play an essential role in illustrating how this disease can be prevented. There may not be a
definitive cure for those who are already deeply afflicted with this disease, even in the future.
However, examining studies on cannabinoids and benzodiazepines may help those who are in the
early stages or have no clinical signs of Alzheimer's. In regards to the benzodiazepine study, the
participants who did not ever use benzodiazepines were placed in the control group (de Gage 2014).
The main finding of this study was the fact that benzodiazepine use is correlated to

Is The Amyloid Precursor Protein ( App ) Is Long...
Introduction:
The amyloid precursor protein (APP) is long associated with Alzheimer's disease (AD). It is a
single–pass transmembrane protein and is responsible for producing the neurotoxic Aβ plaque which
accumulates within the brain (O'Brien et al. 2011). This accumulation of Aβ is what characterises
AD. However, in spite of APP's detrimental role in the pathogenesis of AD, it has been recently
shown that APP can act as a neuroprotective molecule following traumatic brain injury (TBI).
Approximately 10 million people worldwide are affected by this disease every year and it is
projected that by 2020, TBI will surpass various diseases and become a major disease of burden
(Hyder et al. 2007). Thus, due to this increase in morbidity and burden, TBI is an urgent medical
and public problem.
APP's protective role in TBI is currently understood to be the product of ɑ–secretase pathway in
soluble amyloid precursor protein ɑ (sAPPɑ) (Corrigan et al. 2013). This pathway was discovered in
the previous year by the same researchers who used APP knockout mice. The knockout mice had
cognitive and motor functions that were severely compromised with impaired neuroreparative
abilities compared to its wild–type counterpart (Corrigan et al. 2012). When the knockout mice were
treated with sAPPɑ, however, their neuroreparative responses were restored.
Furthermore, the protective properties of APP are often correlated with its functions of synaptic
formation and repair and iron transport and

Β-Amyloid Infections: A Case Study
AD is the second most dreaded sickness in the United States, after disease. By 2011, more than five
million Americans have been diagnosed with AD, and the number will climb quickly at the point
when the time of increased birth rates era starts to achieve retirement age. It is evaluated that the
number of Americans with AD will reach around 15 million by 2050. Neglecting to give a cure to
this malady will have enormous effects on human enduring, as well as monetarily and socially (The
Alzheimer's Project, 2009). Consequently, curing AD is of quick essentialness. A number of
medications proposed to ease off or stop the malady are presently in clinical trials as far and wide as
possible. The essential trials of AD – the infection changing medications, are hostile to amyloid
medicines that are attempting to abate its movement ... Show more content on Helpwriting.net ...
A standout amongst the most energizing methodologies of treatment is utilizing β–amyloid
antibodies to assault the malady. Discovering approaches to let down levels of β–amyloid is a key
step towards the curing AD, and hereditary qualities assumes a significant part in this procedure. A
change in the quality Apoe that advances the arrangement the β–amyloid into neuritic plaques is the
initially ensnared in the hereditary qualities of the illness. Understanding the first occasion that
happens, and what happens to a well–working cell to prompt the onset of the sickness is essential
(The Alzheimer's Project, 2009). The larger part of individuals diagnosed with AD have the late–
onset variations. Then again, concentrating on the early–onset cases has been the best hotspot for
exploration in discovering a cure for the

Alzheimer 's Disease Of The Scientific World Essay
In 1906, Alzheimer's disease entered the scientific world. Till this day, it is one of the most studied
neurodegenerative diseases. Researchers have come a long way with scientific outcomes on the
disease, but unfortunately there is no official cure, or a concise reason on how this disease is
generated. The disease has been recognized to being genetic and affecting people in their later years,
roughly around their sixtieth year. Alzheimer's disease affects the person's memory, language,
judgment and even their daily tasks. While the disease continues to dramatically progress, it begins
to affect all regions of the brain, causing the person to lose almost all of their functions. When the
person has reached their final stage, they are no longer able to recognize themselves or their
surroundings and would need full time dependent care. According to the Alzheimer's Association
(alz.org, 2016), the person may have up to eight years max to live after diagnosis.
There are several methods in diagnosing Alzheimer's disease such as: asking the person about their
family medical history, conducting memory tests, carrying out standard medical tests (urine and
blood) and brain scans like CT's, MRI's and PET's (NIH.gov, 2016). The only way the disease can
be verified is after death, because brain tissue can then be studied for a complete diagnosis
(NIH.gov, 2016).
Researching Alzheimer's disease has been a continuous obstacle for all scientists. They have made
miraculous advances in their

Alzheimer's Disease Essay
Alzheimer's disease or AD is an incurable disorder of the brain that results in loss of normal brain
structure and function. In an AD brain, normal brain tissue is slowly replaced by structures called
plaques and neurofibrillary tangles. The plaques represent a naturally occurring sticky protein called
beta amyloid and in an Alzheimer's brain, sufferer's tend to accumulate too much of this protein.
Neurofibrillary tangles represent collapsed tau proteins which, in a normal brain along with
microtubules, form a skeleton that maintains the shape of the nerve cells. In Alzheimer's disease, the
tau proteins break loose from their normal location and form tangles. Without the support of these
molecules, nerve cells collapse and die. As normal ... Show more content on Helpwriting.net ...
There are few people who do not worry about getting AD as they get older. Indeed, the incidence of
AD increases with each successive year of life after age 60. Currently, scientists estimate that "4.5
million people have AD in America alone and 22 million worldwide" (Willett 63). The disease
affects about "five percent of people ages 65 to 74 and nearly half the population of people 85 and
older" ("Alzheimer" 1). Disturbingly, the disease is becoming even more common. Statistics now
show that the number of people with the disease doubles every five years among older people.
Using this as a rule, Dr. Robert Katzman of the University of California "estimates the total could be
45 million worldwide by 2050" (qted in Willett 13).
With these future projections of the incidence of AD, the financial cost of supporting the afflicted
will be exorbitant as well. Lifetime societal costs for an individual afflicted with Alzheimer's disease
are "$174,000 in the United States" (Willett 13). The cost to businesses that "lose productivity of
their employees who must care for their relatives afflicted with AD is 26 billion"(Willett 13).
Economists also state, "the total cost to the United States per year for the care of AD patients is
estimated to be 100 billion" (Willett 13). With these kind of costs financially, it is mandatory that
public health programs be instated to decrease the

The Development And Progression Of Amyloid
As scientists, we are always trying to discover the answers to the how and why questions that comes
up as science progresses. We all know that nothing is ever straight forward and sometimes we end
up with more questions than answers from our obtained results but this is not always a negative. A
major area of interest today is the development and progression of amyloid diseases such as
Alzheimer's' disease, Huntington's disease, and transmissible bovine spongiform encephalopathy.
Despite extensive studies conducted on each one of these diseases, little is really known about their
development and progression because little is known about the mechanism behind amyloid fibril
formation – the common link found in all of these diseases. Over the ... Show more content on
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Previous studies have shown that different proteins contain short identical sequences in their
secondary structures that have completely different functions and folding mechanisms. It has also
been shown that these same sequences can be induced to form an α helix, β strand, or β sheet
structure depending on the context. These findings have suggested that chameleon sequences have a
sense of structural plasticity which can pose a problem for protein secondary structure prediction.
While previous research has only focused on the notion of identical sequences within an α helix in
one protein whereas a different protein has the same identical sequence but instead of an α helix, the
sequence is within a β strand; Guo et al. delve deeper into the notion that there is also the possibility
of these sequences being found within a β sheet or β hairpin conformation. To distinguish between
the two, Guo et al. introduced the terms chameleon–HS and chameleon–HE. Chameleon–HS refers
to the sequences with helix and strand structures whereas chameleon–HE refers to the sequences
with helix and sheet/hairpin structures.
This study used two different data sets, Dataset No.1 and Dataset No.2. Dataset No. 1, used to
search for chameleon sequences, consists of 6962 protein chains generated from the Protein Data
Bank (PDB). Dataset No.

Innate Essay
Innate or learned behavioural responses can be observed in a neural representation of the sensory
world. Naïve animals, which are without prior learning or experience, show an innate response to a
sensory stimulus suggesting that they are mediated by genetically determined neural circuits. Most
sensory stimuli, however, show an experience–dependent response, allowing an organism to
respond appropriately in a variable and uncertain world. Thus, behav–ioural relevance to sensory
cues is mostly acquired through learning. In Drosophila melanogaster, different forms of learning
have been observed in response to a number of sensory stimuli. The mushroom body (MB), in
insects, is responsible for memory formation and retrieval.
When an olfactory ... Show more content on Helpwriting.net ...
Most antennal lobe projection neurons (PNs) extend their dendrites to a single glo¬merulus while
their axons bifurcate to innervate the lateral horn and the MB of the brain. The lateral horn is
thought to mediate innate behaviours, whereas the MB translates olfactory sensory information into
learned behavioural responses. On the activation from an odorant, PN axons synapse onto the
den¬drites of the Kenyon cells (KCs) in the MB calyx. According to anatomical and physiological
studies, each KC is said to receive, on an average, 6.4 inputs from a random combination of
glo¬meruli which indicates that knowledge of a single input to the KC cannot provide information
about all the additional inputs and these connections differ in different flies.
The γ, α′/β′, and α/β lobes of the MB are formed from three classes of KCs that extend their parallel
fibers to these lobes and form synapses with a relatively small number of MB output neurons
(MBONs). The MBONs extend their dendrites into the MB lobes, while their axons are projected to
the neuropils which lie outside the MB. Modulatory input neurons which include the dopaminergic
neurons (DANs) and octo¬paminergic neurons, also innervate the MB lobes. The MBONs and
DANs extend their processes to locations such that they define spatially restricted 'subdomains' in
each lobe.
DANs are modulatory neurons of the MB that are most prevalent.

Amyloid Synthesis Essay
Most of the lesions in the brain of an AD patient are from plaques, which consist of beta amyloid
peptides that are derived from APP (amyloid precursor protein) 7. APP (amyloid precursor protein)
is located on the cell membrane and consists of N extracellular terminal, short C intracellular
terminal, a single hydrophobic transmembrane domain and a metal binding site 16, and there are
two ways for APP cleaving (figure 2): The first one is non–amyloidogenic pathway which is done
by α–secretase to form the soluble sAPPα and the membrane bound C83, and then γ–secretase cut
the residue of the membrane part to get p3 and AICD protein 7,17. The second one is amyloidogenic
pathway in which it starts when β–secretase cut the APP to shorter sAPPβ than sAPPα and C99
terminal then γ–secretase cut the c99 to Aβ: Amyloid β (40–42 amino acids), and ACID protein
(plays an important role in gene transcription of the protein that responsible for degradation of the
beta amyloid monomer) then beta amyloid is normally degraded by zinc metalloproteases (NEP,
IDE ) 7,17 (see figure 2) and then LRP1 protein escorts amyloid beta proteins out of the brain
through BBB24. Whereas when the concentration of the mis–regulated metals

The Chronic and Incurale Disease of Alzheimers Essay
What is Alzheimer's? It is a disease that affects the central nervous system, digestive system, the
neuromuscular system and is generally a disease that is chronic and incurable. 4.7 million people
greater than the age of 65 live with the disease each and every day, which is approximately one
tenth of the population for those over the age of 65. The most common questions are: what are the
risk factors, which vary from person to person, whether or not there are signs and symptoms and has
there been any testing and diagnosis on this disease. Well the first question usually asked by a vast
majority of those in the age range for such a disease is am I at risk for Alzheimer's. First you need to
know the risk factors involved when discussing ... Show more content on Helpwriting.net ...
There are so many signs and symptoms that correlate to the Alzheimer's disease, which include but
are not limited to: having a worsened ability to take in and remember new information, impairments
to reasoning and changes in personal behavior. Usually those who have Alzheimer's will have a hard
time taking in and remembering new information, meaning they will ask repetitive questions or start
conversations that were previously mentioned. A lot of times they will also misplace their personal
belongings and may even forget important appointments or their grand–children's baseball game.
When you have the Alzheimer's disease you may also find out that you get lost very easily on a
commonly traveled route. Finally the question everybody wants an answer to, are there tests that can
be done to find out if I have Alzheimer's and if I do have it is there a diagnosis of this disease?
Before go too far it should be known that there is not a single test for this disease and finding out if
you have it can be a very strenuous procedure. A doctor can do any number of things from taking
down the history of your family to arranging for brain scans to be done. The things that are most
commonly done however are: taking down family history, doing a physical examination and even
doing cognitive testing. Even in recent studies is has been found that using peanut butter can help
diagnose the Alzheimer's disease. The

Gamma Frequency
In this podcast, researchers at MIT look at the ability of high frequency light stimulation to reduce
amyloid plaques and improve memory in Alzheimer's Disease. The phenomenon was focused on the
work of a researcher named Li–Hue Tsai. She focused on the Gamma frequency and its effect on
neuron electrical signaling to process inflammation. Gamma frequency is a rhythm used when you
have complicated or higher thoughts in the brain (a range from 30 bps – 100 bps) = when your brain
is doing something that requires focus, a lot of attention, and your using your working memory, then
a beat known as gamma frequency rises above all the groups of neurons that are in sync on the same
beat, that help us process the world. The gamma frequency is ... Show more content on
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However, in a human, drilling a fiber–optic cable would be very invasive and cause problems. Thus,
they decided to find a different route and this time through the eyes, by shining white light at a high
frequency. Li–Hue and her team, then created a storage closet with shoebox containers of mice,
placed around the edges of a plastic table that had duck–tape strips of LED lights to produce a fast
rhythm (40bps). Essentially this was a flicker room and once they turned off the lights, the room
was glowing with a white LED light also for 1 hour. The amyloid beta levels in the visual cortex and
there was a 50 percent reduction.
With the same approach, this study was followed up by a third study. Same flicker room and light
shining through the eye balls for 1 hour a day for 7 days, using mice with full blown Alzheimer's.
The results were the same. There was nearly a 50 percent reduction in amyloid beta levels.
However, one downfall was that unless the lights were flickered every 24 hours, the levels of
amyloid beta levels increase again.
Next, another group of researchers at MIT challenge that plaques in the brain do not necessarily
relate to loss of memory and cognition. They find a way to pull a memory back in to place from
Alzheimer's. They took some mice that were just starting to lose their memory and put them in a
box with a particular smell, lighting, and texture and feet. In a box of mice in an unfamiliar place, a
light

Alzheimer's Disease Case Study
A fundamental aspect of understanding the Alzheimer's disease (AD) is to establish the crosstalk
between amyloid beta (A) interactions with neuronal cell membrane. Here, we report a novel
structural and mechanistic strategy to unravel the A1–40 interaction with model cell–membranes
using polymethacrylate–copolymer (PMA) encased nanodiscs and macrodiscs. The PMA nanodiscs
remodel both A1–40 monomers and fibers to toxic and non–toxic protomers. The target nanodiscs
isolated the A1–40 intermediates through a symbiotic mechanism of action. While the cationic
PMA triggers the A1–40 binding, the phospholipids remodels the monomers/fibers to protomers.
A controllable modulation of A1–40 aggregation pathways and trapping A1–40 intermediates ...
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Among various proposed cause for the onset of AD [10, 11], the deposition of amyloid– peptides
(A) peptides that are sequentially cleaved from amyloid precursor proteins in the brain has
remained as the fundamental hallmark for pathogenesis [12, 13]. The A peptides are composed of
38 to 43 amino acids and are modulated by the β– and γ–secretase enzyme activities with distinct
cleavage sites [14, 15]. Among these, A and A are the two major isoforms [16,
17] and the latter has been found to aggregate faster and are prominent in the AD brains. The
comparative slow aggregation kinetics of Ahas extended its suitability for the
biophysical and biochemical investigation in solution as well as complex environments containing
cell membranes [18–20]. Moreover, A have shown the capability to form various types of
aggregates, such as oligomers, amorphous aggregates, and immature and mature fibers, depending
on conditions and other molecular interactions [21–23]. The sequential conversion of water soluble
A peptide monomers to intermediate toxic oligomers and large metastable –pleated
amyloids have been proposed to understand the mechanistic approach for AD. The structural
plasticity of unfolded A monomers to adopt transient oligomers also been investigated to
confer their neurotoxicity in vitro [24, 25]. However, the exact mechanism of oligomer conversation
remains challenging and minimizes our

Alzheimer 's Disease ( Ad )
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by β–amyloid plaque
formation caused by aggregation of β–amyloid42 within the brain leading to a progressive decline in
cognitive function and memory loss (2). Hyperphosphorylated tau protein is occasionally found in
brains of AD patients with advanced pathology however, it is not necessarily an indicator of AD but
considered a sign of disease severity (2, 4, Kosik et al, 1986). AD is separated into two
subcategories following the simple sporadic and familial disease classifications, early–onset AD
(EOAD) which develops in individuals between 30 and 60+ years of age and late–onset AD
(LOAD) which develops in individuals 60 years of age or older (2). Familial AD may ... Show more
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β–amyloid aggregation spread from the site of injection to include both hemispheres of the brain
further displaying the potentiation induced by aggregates within the brain homogenates (Stöhr et al,
2012). Under transmission electron microscopy, purified β–amyloid aggregates from transgenic
mice revealed densely bundled fibrils; which were observed to increase levels of GFAP, Aβ(1–40)
and Aβ(1–42) in bigenic mice at 300 days post injection via ELISA and immunoblotting (Stöhr et al,
2012). Crude brain homogenate exhibited approximately 15–20 times less β–amyloid than the
purified homogenates (Stöhr et al, 2012). BLI of bigenic mouse brains injected with purified
homogenate exhibited an early time of detection with signals at 161 + 7 [Tg(APP23)] and 173 + 9
[Tg(CRND8)] days (Stöhr et al, 2012). (FIGURE). Synthetic β–amyloid aggregates, wild–type
Aβ(1–40) and mutant Aβ(AβS26C)2, were used to determine if prior results from purified brain
homogenate could have contained any cofactors which would affect propagation of pathology
(Stöhr et al, 2012). Results from the injection of synthetic fibrils into bigenic mice revealed similar
β–amyloid aggregation, however pathology was less severe than purified brain homogenates from
transgenic models (Stöhr et al, 2012). BLI of synthetic fibrils revealed a decrease in

Alzheimer's Main Features
Examining these three main features of Alzheimer's disease
The brains of people with Alzheimer's disease have an abundance of two abnormal structures –
amyloid plaques and neurofibrillary tangles. These are made of misfolded proteins which can stick
together with other misfolded proteins to form insoluble aggregates. If these aggregates build up,
they can disrupt cellular communication and metabolism. The third main feature of Alzheimer's is
the loss of connections between cells leading to the ill–functioning and death of cells (Institute and
Aging, 2011).
Amyloid plaques
These plaques consisting largely of insoluble deposits of a toxic protein peptide called beta–amyloid
are found in the spaces between the nerve cells in the brain. Beta amyloid

The Methods Of Controlling The Formation Of Beta-Amyloid...
Materials and Methods
Controlling the formation of beta–amyloid plaques by isolating somatic cells from a patient and
creating a stem cell lineage by reverting the isolated cells back to stem cells using the iPS technique.
This will allow the cells then to differentiate into neurons and other brain cells. This would allow for
connections between neurons to re–develop when injected into a patient's brain. One advantages to
using this technique is the production of autologous cells that were reprogrammed from the patient's
own cells. This reduces the chance of rejection that is present in other stem cell infusions. To collect
the somatic cells a mini liposuction procedure will be preformed near the lower abdomen. The
extracted material will ... Show more content on Helpwriting.net ...
The BACE1 gene is directly involved the production beta–amyloid plaques. Beta amyloid is a small
part of a larger protein called APP (amyloid precursor protein). An enzyme cuts the APP in two
places. The first enzyme to act is the BACE1 that generates the production of beta–amyloid. When
BACE2 is activated it is responsible for destroying beta–amyloid by cutting it into pieces. Other
enzymes assist BACE2, but it has been found to be the most efficient due to its ability to perform
this function by two distinct mechanisms [3]. The genetically engineered induced pluripotent stem
cells would first be differentiated into neural lineages prior to injecting them into patients. Direct
injection of iPS cells in vivo can cause the formation of a teratoma. The transfusion would be
conducted in two phases. Each phase will consist of a series of 8 injections of stem cells that have
differentiated into a neural lineage from their own somatic cells. They would then be directly
injected into various areas of the brain that are important for memory and cognition. These areas
include: frontal lobe, parietal lobe, temporal lobe, and occipital lobe. This entire procedure would
first be conducted on mice. After phase II of the experiment, the results would be analyzed to
determine if cognition in mice did in fact improve. If cognition were found to improve after the
injection of the cells, the next step would be to preform a human clinical trial. If approved, the same
procedure

Alzheimer's Disease Compromises Cognitive and Memory Skills
Alzheimer's disease is a progressive neurodegenerative disease of the brain wherein a person
afflicted with the said disease would have compromised cognition and memory skills, and eventual
deterioration of the skill to execute uncomplicated activities. According to experts, most individuals
do not manifest the symptoms for Alzheimer's disease until they are over the age of 60. This disease
affects more than 5.1 million Americans. Alzheimer's disease is named after Dr. Alois Alzheimer
who first discovered deviations from normal tissues of healthy individuals in the brain tissue of a
lady in 1906. The woman, who showed symptoms of erratic behavior, loss of memory, and
problems with communication, died of a then unfamiliar mental disorder. This led Dr. Alzheimer to
investigate the cause of her unusual death. He assessed the brain of the woman and found that there
were many anomalous masses (amyloid plaques) and intertwined bundles of fiber (neurofibrillary
tangles). Scientists today have pinpointed the qualities of Alzheimer's to be a) tangles in the brain
(neurofibrillary tangles), b) plaque in the brain (amyloid plaques), and c) loss of connections among
nerve cells. Experts know little about the true causes of AD (Alzheimer's disease), however they
have proposed the amyloid hypothesis to explain how the disease begins. In people afflicted with
AD, lethal transformations are happening in the brain. A buildup of amyloid plaque (β–amyloid
clumps), caused by the

Amyloid Beta Peptide
Magnetic Resonance Imaging (MRI) is used to show the borders of white and gray matter in the
brain. This can help to differentiate AD from multi infarct dementia and low pressure hydrocephalus
based on the ratios of white and gray matter. A person with AD suffers from a loss of gray matter,
thus making the ratio of gray to white matter smaller than in a person without AD. An exam of the
body fluid and non–neural tissue can be helpful to differentiate between AD and other disorders and
infections that cause changes in the blood and CSF. These tests also help to demonstrate the
functionality of neurotransmitters, metabolites, and enzymes. Although these tests are useful, the
only way to confirm that a patient definitely has AD is by autopsy ... Show more content on
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This specific gene codes for amyloid beta peptides. The amyloid beta peptides are found in the
plaques associated with AD and also in the neurofibrillary tangles. Accumulation of this peptide
may cause AD. There is usually too much accumulation of amyloid beta in the brain and not enough
clearance. The build up then causes the plaques and tangles. It is believed that a missense mutation
in the precursor for this peptide is what causes an imbalance between accumulation and clearance.
Also, when the amyloid beta forms deposits in the neurons, it is believed to stimulate activity of
microglial cells. When these cells are stimulated, it causes the production of more amyloid beta,
accounting for the progression of the disease. This theory is known as the amyloid beta cascade
hypothesis. Although there are many supporters of this theory, there still is not enough evidence to
prove it and there is some evidence against it. Firstly, there is not a mutation in the amyloid gene
that increases the risk of familial AD. Amyloid beta has also been shown to be non toxic, so it alone
can not account for the death of neurons in the brain associated with AD. However, the stimulation
of the microglial cells also results in the production of tau proteins, which when in excess, may be
the cause of neuronal death. Also, the microglial activation might cause the release of other
neurotoxic molecules, such as IL–1b, IL–6, TNFa, nitric oxide, and many other

Informative Speech On The Attention Getter For Alzheimer's...
Student Name: Kayla Stradomski Course # and Section/Time: COMM 101 DAH; Monday, 11:00
a.m. – 1:50 p.m. Topic: Alzheimer's disease General Purpose: To inform Specific Purpose
Statement: To educate my audience on the aspects of Alzheimer's disease. INTRODUCTION
Attention Getter: Can you imagine your life if your memories and cognition slowly started
deteriorating? Well, the Alzheimer's Association's webpage titled Alzheimer's latest facts and figures
last updated in 2018 estimates that that's the reality for 5.7 million Americans. Statement of
Purpose: Today, I want to tell you about three aspects of Alzheimer's disease. Credibility: I became
curious about this disease when my paternal grandmother began losing her memory when I was
younger, ... Show more content on Helpwriting.net ...
They studied this drug over the course of two months by comparing a group of normal mice to two
groups that have been engineered to emulate symptoms of Alzheimer's such as the memory loss and
presences amyloid plaques in the brain among others. One of these groups was treated with the TA
while the other was not. a. According to Li and Hölscher, this study showed positive results. For
example, this graph from the report (show slide #7) shows how the treated mice, marked
APP/PS1+TA, maintained a better memory of a water maze compared to the untreated

Cell Phone Radiation May Help Alzheimer's Disease Essay
Every 71 seconds in this country, someone is diagnosed with Alzheimer's disease and in a startling
new report out today from the Alzheimer's Association, predicts that one out of every eight baby
boomers–– or almost 10 milllion Americans – is expected to develop this disease, (Mckenzie). The
University of South Florida has led a study along with the Alzheimer's Disease Research Center
which has abandoned the idea that cell phone radiation is detrimental to our health. The experiment
studied the effects of cell phones on Alzheimer's. Professor Arendash, started this study by noticing
that the students in the hallway of the university had cell phones plastered to their ears. He set up the
experiment with lab mice, beaming electromagnetic ... Show more content on Helpwriting.net ...
These mice kept strong memories and performed just as well as normal mice which suggests that the
radiation could have protected their memories. Mice, who were transgenic, began the radiation
treatment at five months old when memories had begun to deteriorate. In such cases, the radiation
seemed to stop further memory loss and in some mice, the radiation may have reversed the memory
loss. According to the health physics society, radiation is an energy that comes from a source and
travels through space which may be able to penetrate various materials. In the past few weeks of our
chemistry class I have learned that atoms whom have an unstable nuclei are radioactive, these atoms
give off excess energy which are radiation rays. Radiation varies from gamma, beta, and alpha rays.
Gamma rays have the shortest wavelengths and highest frequencies. Gamma rays are the most
energetic form of light produced by the hottest regions of the universe and emitted by the nucleus of
radioactive atoms. Because of this, gamma rays are used to penetrate tissue property, such as in the
use of CT scans, and radiation therapy. Alpha particles are also ejected by the nuclei of unstable
atoms; however, they are large and consist of two protons and two neutrons. Although alpha
particles have a high mass, they are the most destructive form of radiation with a low penetrating
force; a single piece of paper can block alpha particles. Beta particles are much

Are Amyloid Drug Therapies Still The Best Target For...
Are Amyloid Drug Therapies still the Best Target for Alzheimer's Disease? Denise Bechtold
Professor Ostrander English 1107: 30 November 6, 2017 Are Amyloid Drug Therapies still the Best
Target for Alzheimer's Disease? Have you ever done something dumb, and stated, "I think I've lost
my mind?" Well for an average of 5.5 million people, this is a reality. Parts of their brain literally
have begun to die, and with it, goes their livelihood. Before becoming a home health aide, I had
heard of dementia and Alzheimer's, but I had never seen it first–hand. Over the last two years I have
watched as it has debilitated many people both physically and mentally, and all I can think is:
"When ... Show more content on Helpwriting.net ...
In the early stages of this disease Reagan stated; "I have begun the journey that will lead me into the
sunset of my life." Research has been underway for years and years. One of the more promising
avenues entertains the idea that these amyloid plaque proteins are the cause of changes in the brain.
"The damage occurs when neurons congregate and form protein masses called amyloids that are
water–soluble in normal brains but undergo structural changes and can't be dissolved in Alzheimer's
patients. The masses disrupt nerve cell functions and begin to cause symptoms such as the loss of
short–term memory. The deterioration of the brain is accompanied by a drop–off in the production
of the neurotransmitter acetylcholine, which plays a key role in cognitive functioning" (p.444). I do
believe that these amyloid plaques do play a role in the changes observed. These tangles and plaques
are kind of the tell–tale sign that Alzheimer's is present. The missing piece to the puzzle is, What
gets the ball rolling? What causes these changes to occur? I am confident that if we can find the
answers to these questions, that we can find a cure. Next, I would like to focus on the statistical
analysis and treatment of this disease. As of now, there is no cure to Alzheimer's. There are many
different clinical trials and pharmaceutical drugs being tested. I again searched the Anoka Technical
databases and came across another article

Symptoms And Treatment Of Mild Traumatic Brain Injuries
Introduction
Mild traumatic brain injuries (mTBI) are amongst the most common injuries affecting
approximately 42 million individuals annually (Gardner & Yaffe, 2015). This incidence rate is
inaccurate as many mTBI are not reported (Gardner & Yaffe, 2015). Such injuries are thought to
increase susceptibility to neurodegenerative diseases including Parkinson's disease (PD),
Alzheimer's disease (AD), and amyotrophic lateral sclerosis (ALS) (Gardner & Yaffe, 2015). AD
accounts for up to 80% of all senile dementia and is characterized by cognitive deficits that
progressively manifest into severe cognitive and behavioral impairment (Elder et al., 2010). Such
symptoms are causally associated with amyloid plaques and neurofibrillary tangles ... Show more
A cohort of mice underwent a second mTBI after 24 hours. Mice from both WT and Tg groups were
assessed 2 days, 9 weeks, and 16 weeks after mTBI treatment. Primarily, H&E stain was employed
along with Gomori's iron stain to localize site and severity of mTBI injury. The degree of A
deposition in the somatosensory cortex (SSC), the perihippocampal cortex (PHC), and the
hippocampus (HP) of both hemispheres was determined by 4G8 immunostaining. In addition, GFAP
staining was used to quantify the population of astrocytes at the site of the injury. Furthermore,
Sandwich ELISA was utilized in mice groups 16 weeks after injury to measure A40 and A42 peptide
levels in various brain regions, including the cerebral cortex, the hippocampus, and the cerebellum.
Such tissues were also analyzed for isoprostane levels that are produced by lipid peroxidation.
Isoprostanes were also detected in urine samples at various survival periods. Moreover, mice
underwent Morison water maze (MWM) and composite neuroscore (NS) tests at 16 weeks' post–
injury to examine cognitive and motor functions respectively. Uryu and collegues found a
significant increase in iron deposits and reactive astrocytes in the repetitive mTBI postmortem
sections of Tg mice, when compared to other groups at 16 weeks after the injury. This was not the
case in WT mice. Similarly, there was a significant increase in the A burden within select brain
regions (i.e. SSC, PHC, HP) of single and

Pros And Cons Of Non Professional Nursing Literature
In the nursing field, it is a part of your job to stay abreast with the latest medical research findings
and on top of the latest information concerning your profession. The best way to achieve these goals
is to do your own research. When you do your research you will have to choose between
professional nursing literature and non–professional literature. It is important that you know the
characteristics of both and the pros and cons. For my example of professional nursing literature, I
used the article "Repetitive brain injury & CTE," which was printed in Nursing Made Incredibly
Easy! I used the article "Ahead of the Hit," which appeared in Discover Magazine for an example of
non–professional literature. When you pick up a professional nursing ... Show more content on
Helpwriting.net ...
When articles are written by people without credentials the information in the article can be biased,
have errors and misinterpreted facts. Since a lot of non–professional literature don't have
bibliographies it makes it more difficult for readers to fact–check the author and make sure the
information is correct and the author's source is legitimate. The information in non–professional
literature are mostly for the general public and is written to entertain and inform. This means the
information will less likely if ever pertain strictly to the nursing profession, meaning if you need
information on new nursing regulations or nursing procedures there is a strong possibility you won't
find

Metal Homeostasis System
Normally metals are supplied from the daily nutrients and they are not stored in the body, so its
level is supposed to be regulated by a specific system to prevent it from increasing or decreasing in
the brain and this system is known as metal homeostasis system which is responsible for regulation
the level of the metal in the body with the help of a specific kind of transporters8. These transporters
are divided into two families. One of them is responsible for transporting metals to the cells after
ingestion to help the cell perform its functions by binding to the specific protein there for example
binding to Cu/ZnSOD protein to breaks the free radicals20,21. The other one transports the metal
that binds with glutamatergic neurotransmitter from the presynaptic vesicle to the postsynaptic one
and those metals are responsible for learning, cognition, and memory functions by regulating the
excitation process by either inhibition of NMDA and GABA receptors or enhancing AMPA receptor
in ... Show more content on Helpwriting.net ...
Moreover, the complex studies of the metals (Zn & Cu) with the amyloid protein shows that the
copper coordinates the amyloid beta through four or five coordinating bonds: two imidazole
nitrogens from His–6 and His 13/14, one N–terminal amine nitrogen from Asp1 and a carbonyl
oxygen from Ala–2. And perhaps the fifth bond is from the oxygen of Asp1 (see figure 4c) 40. But
other researchers found that copper binds amyloid via His6, His13, His14, and Tyr10 (Figure 4a).
After the metal binds a beta amyloid (monomeric compound) , the aggregation of β–amyloid starts
after this moment by creating a new coordination bond between imidazole ring of His6 with the
other copper atom from the other copper–amyloid complex to form a dimer compound (see figure 4
b)

To What Extent Is Alzheimer 's Disease Hereditary?
Abstract: This investigation studies the question: To what extent is Alzheimer's disease hereditary?
To come to a conclusion, seven pieces of research were analyzed regarding their implications on the
genetic and environmental factors impacting the etiology of Alzheimer's. Specifically, four genetic
factors were evaluated: the influence of Beta Amyloid Plaques, alcohol dehydrogenase in relation to
mitochondrial function, specific Loci, and a twin study to determine relative heritability. The results
of these studies indicate a high degree of heritability and genetic factors in Alzheimer's disease with
recognition, to a certain extent, of the relative influence of environmental factors. Thus, the impact
of environmental factors was also explored. The influence of epigenetic factors, physical activity,
and environmental enrichment were evaluated through analysis of correlational studies and a lab
experiment. The results of this research generally indicated that environmental factors can play a
role as a preventative measure of developing the disease. There is suggestion that the genetic risk of
developing Alzheimer's can be lessened through environmental enrichment or physical activity.
However, the research lacks definitive evidence that environmental factors can completely diminish
the heritability of the disease across populations. On the other hand, the investigation of the
apolipoprotein genome, the identification of specific loci, the role of alcohol dehydrogenase

Amyloid Cascade Hypothesis
The amyloid cascade hypothesis is the most widely accepted of the AD pathogenesis hypotheses. Its
principle is that the accumulation of Aβ plays a major role in AD pathogenesis, and the disease is
analyzed as a series of abnormalities in the process and secretion of the amyloid precursor protein
(APP), where an inequality between production and clearance of amyloid β is the triggering event
and the most important factor responsible for other abnormalities observed in AD (Hardy et al,
2002; Cummings et al, 2007). Amyloid β is a peptide with high resistance to proteolytic
degradation. It consists of 37–43 amino acids with different isoforms (Deane et al, 2009). Aβ is the
result of sequential cleavage of the amyloid precursor protein (APP), generating ... Show more
Autosomal dominant mutations in APP, PSEN1, or PSEN2 that alter APP processing and the
production or self aggregation of Aβ, promote aggregation and accumulation of Aβ in brain causing
early–onset AD (Bertram et al., 2010).
It has been found that the oligomeric forms of Aβ were more dangerous than its monomers, acting
intracellularly and extracellularly leading to the disruption of several downstream mechanisms, such
as the disruption of intracellular calcium homeostasis (Camandola and Mattson, 2011), and
impairments of axonal transport and mitochondrial functions (Decker et al., 2010; Querfurth and
LaFerla, 2010; Sheng and Cai, 2012). In addition, several lines of evidence suggest that Aβ
regulates neuronal and synaptic activities and that its accumulation in the brain causes aberrant
network activity and synaptic depression (Palop and Mucke, 2010). Impairments of inhibitory
interneurons and aberrant stimulation of glutamate receptors result in excitotoxicity, and play
important upstream roles in this pathogenic cascade. These impairments also lead to a positive
feedback loop, where aberrant neuronal activity augments Aβ production, which in turn leads to
further neuronal damage (Palop and Mucke, 2010; Bero et al., 2011; Verret et al.,

Drug Delivery For Nervous System
INTRODUCTION
Drug delivery to nervous system is still a challenge to the scientists all over the world because of the
vasculature of central nervous system, blood brain barrier (BBB) which acts as the physical barrier
to the passage of therapeutic agents. Though, quite a few delivery systems and strategies have been
developed for delivering drugs to the CNS for various disorders, most of them are invasive and lack
target specificity. Several factors need to take under consideration while designing a drug delivery
system for CNS and optimizing all the factors is a major hurdle. Binding affinity of the drug to the
transporter, enzymatic conversion and solubility of the drug, membrane surface characteristics of
brain capillary, composition of ... Show more content on Helpwriting.net ...
Objective of my proposal is to prepare a delivery system in which the drug will be stable and can
cross the blood brain barrier without any major difficulties and deliver the drug at the target site for
better clinical management of Alzheimer's disease.
PURPOSE OF THE STUDY
Alzheimer's disease (AD) in a deadly chronic neurodegenerative disorders which gets worse with
time. Patients suffer from short term memory loss, disorientation, rapid mood swings, behavioral
problems and ultimately encounter death. This is mainly a genetic disorder; but there are several
hypothesis which are believed to cause this disease such as reduced synthesis of acetylcholine,
deposition of amyloid beta protein and abnormalities in tau protein. In this paper, a polymeric
nanoparticle based delivery system surface attached a dual functional antibody [anti amyloid beta
(Aβ) anti transferrin receptor binding monoclonal antibody] is being proposed. Tacrine has chosen
as the drug for preparing the immunonanoparticles, which is an oral centrally acting
acetylcholinesterase inhibitor. Tacrine was a useful drug in maintaining sufficient concentration of
acetylcholine (ACh) in AD patients but has been discontinued in 2013 due to several reports of
acute liver injury. The precise mechanism of how it causes liver injury is not known, but studies
showed Tacrine increase serum aminotransferase

Assignment ( Hatters ) ( Transthyretin )
B30001 Assignment (Hatters) – Transthyretin
Benjamin Andrikopoulos 759192
Introduction to TTR:
Transthyretin (TTR) is a protein in the blood (serum) and cerebrospinal fluid of humans that
functions in the transport of the thyroid hormone thyroxine (T4) and retinol (also known as Vitamin
A1). [1] It is secreted by the liver into the blood and by the choroid plexus into the cerebrospinal
fluid. [2] Studies have shown that as less than 1% of TTR 's T4–binding sites (T4BS) in the blood
are in use and occupied, new drug designs can be specialised and optimised to bind to these sites,
thus preventing TTR misfolding, dissociation, and aggregation. [4] Amyloid diseases are associated
with the misfolding and dissociation of the TTR tetramer and ... Show more content on
Helpwriting.net ...
Figure 1. Three–dimensional cartoon style structure of transthyretin (TTR) showing two
monomers/one dimer of the dimer–of–dimers quaternary structure (monomers pink and orange) at
the binding interface. Stick style top view of AG10 (blue) highlighting two binding sites per
tetramer and key binding serine and lysine residues S117 and K15 of TTR (green). All monomers of
TTR contain 1 α–helix and an 8–stranded β–sheet with Greek–key topology.
Interaction differences – AG10 vs. tafamidis:
With AG10 binding to TTR, the dimethyl–pyrazole–like ring of AG10 sits deep within the T4BS
cavity, forming two H–bonds to two Ser117 residues of subunits adjacent to each other. The –CH3
pair of the pyrazole ring are positioned into halogen binding pocket 3 (HBP 3), which is considered
a hydrophobic area. [4] The terminal COOH group on the benzene ring allows for van der Waals
interactions with the side chain amino groups of the two Lys15 residues directly on different
monomers at the edge of the T4BS, with the F moiety in the para position fitting into HBP 1. These
interactions close to the binding environment surrounding AG10 are protected in part from the
surrounding solvent, leading to high affinity binding of AG10 to TTR. [4]
Contrasting with tafamidis hydrogen bonding is absent at the base of the binding pocket like with
AG10, but the Cl substituents are instead located in HBP 3, where hydrophobically the subunits are
bridged. [4] This absence of additional

Synaptic Of Alzheimer 's Disease Essay
and synapses to prevent amyloidosis and inhibit further aggregation56. In the CNS, nonneuronal
cell linages like astrocytes have been reported to have an elevated level of HSPs to target misfolded
protein degradation53. However, a major gap in the field is the lack of any such reports about the
extracellular chaperons in the protection of CNS and neuronal structure and function.
Although not fully understood, but it has been reported that different cells have different
susceptibility to proteotoxic stress. The unfolded protein response evoked by cells in response to
proteotoxic stress involves an orchestered functioning of the proteostasis pathways57.
Neuronal cells and cell of the central nervous system bear an increased risk of being burdened by
misfolded protein aggregates under stress or disease conditions. For example, dopaminergic neurons
in the substantia nigra in case of Parkinson's disease, motor neurons in the motor cortex and spinal
cord in amyotrophic lateral sclerosis, cholinergic neurons in the hippocampus and entorhinal cortex
in case of Alzheimer's disease, are those cells with greater susceptibility in comparison to other
cells51. One way of looking at this is to explore the difference in terms of the expression of the
proteostasis components in these cells, and that of the pathological marker proteins like amyloid–β,
α–synuclein, Lewy body, huntingtin and bunnina bodies51. A comparison of deficiencies or
abnormal expression pattern of proteostasis

The Correlation Between Down Syndrome And Alzheimer 's...
The Correlation between Down syndrome and Alzheimer's disease
Anna Lister
Biology Honors, P. 3
Mrs. Creech
25 November 2015
Introduction:
Alzheimer's disease (AD) is a disease that slowly and progressively causes memory impairment. It
will eventually inhibit abilities, such as language, planning, and perception. AD is prevalent in
individuals with Down syndrome (DS), a condition where those affected had acquired three
additional chromosome 21 before birth (emedicinehealth, 2014). Michael Rafii, director of the
Memory Disorders Clinic at UCSD, says that "people with Down syndrome represent the world 's
largest population of individuals predisposed to getting Alzheimer 's disease" (Hamilton, 2014).
There is no cure for either, and scientists are still lacking the knowledge of a complete story.
Beta Amyloid, Plaques, and the Destruction of Nerve Cells:
There is a large supply of amyloid plaques in the cells of people with Alzheimer's disease. Amyloid
plaques are clustered pieces of protein that build up between nerve cells. They speed up the
production of beta amyloid, which are polypeptides of about thirty–six to forty–three amino acids
long (emedicinehealth, 2014; Stanford Medicine, 2013). Amyloid precursor proteins (APP), when
split into specific pieces, are producers of beta amyloid. They are found in tissues and organs, such
as the brain. Amyloid precursor proteins pass through a fatty membrane on the outside of a cell. This
allows them to extend from the

Amyloid Β Precursor Protein Analysis
Amyloid–β Precursor Protein (APP) is a gene that provides instructions for making a protein called
amyloid precursor protein (Andrew, 2009). Amyloid precursor protein is found in several tissues
and organs including the brain and the spinal cord––in other words the central nervous system
(Andrew, 2009). Some studies suggest that in the brain, APP help direct movement of nerve cells
during early development. For instance, APP may be involved in the regulation of synaptogenesis
which is the formation of synapses between neurons in the nervous system (Dawkins, 2014).
Additionally, APP is cut by enzymes that create smaller fragments that are often released outside the
cell. Some fragments that help play a role in AD are soluble amyloid precursor

Amyloid Precursor Protein Essay
Amyloid precursor protein (APP) has many functions and regulations. This protein is involved in
neural development. Many may know it for its involvement in the pathology of Alzheimer disease
as well as other neurodegenerative diseases. However, APP is a developmental gene. This gene
regulates neurons, their differentiation as well as migration. This gene is also involved in neurite
outgrowth and the regulation of synaptic function (1). Despite knowledge of these functions, many
functions of APP is still unclear (2).
Structure:
APP is a member of conserved type 1 membrane proteins which also includes amyloid precursor–
like proteins 1 and 2, APLP1 and APLP2 (human), Appl (fly), and apl–1 (worm). They each contain
a large extracellular ... Show more content on Helpwriting.net ...
Additionally, studies have also demonstrated a role for APPs in regulating stem cells. APP
encourages the differentiation of neural stem cells into astrocytic lineage (2). In human embryonic
stem cells, the over expression of APP or its soluble forms causes fast and strong differentiation
towards a neural fate (1). Another function of this protein that have been found in some studies was
that APP was shown to undergo rapid axonal transport to synaptic sites. Moreover, APP was found
in vesicular sections of dendrites and axons. This suggests a possible role for APP in synaptic
function (1). These functions of APP are shown to be involved in neural development. Therefore,
APP is a complex protein that posses many functions, many of which are still not very well
understood.
Fig 1: Summary of the roles of APP and its metabolites during neural development
As mentioned earlier APP is found to be involved in neural development. The functions discussed
above have shown how. During early development, the expression pattern of APP in neuroblasts and
neurons in the neural tube suggests a role in neurogenesis, including neural proliferation,
differentiation and axonal outgrowth (7). Figure 1 shows neural development from early stages. It
shows how APP and APP metabolites play important roles during the different stages of neural
development. The stages range from neural proliferation to the formation of a functional synapse.
The metabolites that posses

Alzheimer's Amyloid Hypothesis
Alzheimer's disease (AD) is an irreversible progressive neurological disorder affecting memory and
cognitive abilities (Qiu et al., 2009). As Estimated, patients diagnosed with AD may not survive the
disorder within three to nine years since their diagnosis. AD is the leading cause of dementia in
elderly patients, with increased incidence of prevalence with age. Every year, 1275 cases per
100,000 persons aged more than 65 are diagnosed, with a doubling in the incidence every five years
in patients older than 65 (Reitz et al., 2011). AD is a multifactorial disease with a unique pathogenic
protein aggregations, including accumulation of hyper–phosphorylated tau and the accumulation
and misfolding of Amyloid–β (Aβ) (Querfurth and LaFerla, 2010). ... Show more content on
Helpwriting.net ...
The spontaneous self–aggregation of Aβ into multiple coexisting physical forms, including
oligomers (two to six peptides), leads to their coalescence into intermediate assemblies. In addition
to this, β–amyloid can also grow into fibrils, which arrange themselves into β–pleated sheets to form
the insoluble fibers of advanced amyloid plaques. Soluble oligomers and intermediate amyloids are
the most neurotoxic forms of Aβ. In brain–slice preparations, synapses are toxified by dimers and
trimers of Aβ. However, the severity of the cognitive defect in Alzheimer's disease is in correlation
with the levels of oligomers in the brain, not the total burden of Aβ. Neuronal activation rapidly
increases Aβ secretion at the synapse, a process tied to the normal release of vesicles containing

Amyloid Synthesis
Amyloid beta (Aβ) is a short peptide contains 37 to 43 amino acids and is well known for its
hypothesized role in causing pathogenesis of AD, since one of the main hallmarks of AD is the
accumulation of fibrillogenic Aβ in the grey matter of the brain (14–15). Meanwhile, over 90% of
AD patients have cerebral amyloid angiopathy (CAA) which is characterized by the deposition of
Aβ in capillaries, arteries, and arterioles (16–17). CAA causes the degeneration of smooth muscle
cells and leads haemorrhages (17).
Aβ is generated by proteolytic processing from its precursor, the amyloid precursor protein (APP),
which is a type–I oriented membrane protein and its splicing variants include APP695, APP714,
APP751, APP770 (18–21). The isoforms APP751 ... Show more content on Helpwriting.net ...
The processing of APP involves three proteases, α–, β–, and γ–secretases and two processing
pathways, the amyloidogenic pathway and the anti–amyloidogenic pathway as shown in Figure 2
(14, 23). The Aβ is generated in amyloidogenic pathway which is mediated by β–, and γ–secretases
(14). The β– secretase first sheds the ectodomain of APP and generates the APP carboxy–terminal
fragment (βCTF) (14). Then the γ–secretase cuts at the transmembrane region of βCTF and releases
the Aβ into the extracellular fluids like cerebrospinal fluid or plasma (14, 24). In the anti–
amyloidogenic pathway α–secretase first cuts at the middle region of Aβ so a trauncated APP CTF
(αCTF) is generated and after the transmembrane cut of γ–secretase, a truncated Aβ peptide is
released (p3) (Figure 2; 25). The amyloidogenic and anti–amyloidogenic competes with each other
(26–27). In addition, when the γ–secretase cuts at the transmembrane region of APP, the cut site is
not restricted to a single position. The γ–secretase first cuts at

Alzheimer's Hypothesis
Did you know that Alzheimer's disease kills more people than both prostate and breast cancer put
together? This neurodegenerative illness is the sixth leading cause of death in the United States, but
not only does Alzheimer's affect the five million Americans living with it. People caring for those
with the disease gave up around eighteen billion of their own hours this past year to provide the
needed service. What's even more staggering is that these caregivers put in these hours without pay.
Alzheimer's is a serious concern to scientists, but the disease is rooted in the most complex,
confusing part of the human body, the brain. This is a reason why an effective cure for the disease
has been unavailable in the past, but new developments ... Show more content on Helpwriting.net ...
It is a degenerative disease, which means it gets worse over time and as of right now, there is no
way to reverse its negative effects. Scientists are not entirely sure what causes Alzheimer's, but the
widely accepted theory is known as the amyloid hypothesis of Alzheimer's. This hypothesis states
that Alzheimer's is caused by a buildup of plaques in the brain that damage or kill neurons. These
plaques form when sticky proteins called amyloid beta clump together. Amyloid beta proteins are
produced when amyloid precursor protein (APP) is chopped into multiple pieces by Beta–site
Amyloid precursor protein Cleaving Enzyme 1 (BACE1) and an enzyme referred to as gamma–
secretase. The process begins with APP, which sticks out from the membranes of cells, is cut by
BACE1, which makes small pieces called sAPP beta, which are unrelated to the development of
Alzheimer's. The small fragment that still remains in the cell membrane is then chopped by gamma–
secretase, giving off amyloid beta. There are two main types of treatments that are being researched
that scientists believe could slow or even completely eliminate Alzheimer's, antibody therapies and
BACE1

6.3 Amyloid Theory
6.3 Amyloid theory The most commonly supported hypothesis for the cause of AD relates to a
protein expressed in many cells, of unknown function and implicated in familial AD due to
mutations in the gene that code for it(Wisniewski, Wisniewski & Wen 1985). Although its function
is not completely understood, –amyloid precursor protein (APP) is suggested to be critical for
neuron growth(Turner et al. 2003, Vasto et al. 2008, Priller et al. 2006), signalling, and may also
function as an antioxidant(Crouch 2007) and a metalloprotein, modulating copper transport and
metabolism(Turner et al. 2003, Priller et al. 2006, Kong et al. 2007). The parent protein, the 695–
770 amino acid APP, in most cell types undergoes the non–amyloidogenic pathway. Cleavage of the
APP protein can occur at many sites within the cell, including the trans–Golgi network, ... Show
more content on Helpwriting.net ...
The amyloidogenic version of the pathway involves cleavage by –secretase followed by the –
secretase (see figure 6), releasing the 40–43 amino acid amyloid beta (A) peptide, thought to cause
the neurodegenerative disease(Selkoe 2001, Findeis 2007). The enzymatic action of –secretase
leaves a C–terminal fragment known as APP–CTF or
C99, within the membrane and releases APPs into the extracellular space. After A peptide generation
by –secretase from the C99 fragment, the A peptide is extracellularly secreted(Rogaeva et al. 2007).
Most of the A peptides produced are 40 amino acids long, however it is thought in the diseased state
the usual 10% of A peptide production increases, causing havoc within the cell and the surrounding
environment(Vasto et al. 2008). This longer form
(A
42
42
) is more hydrophobic and fibrillates more easily, and is also controversially thought to be more
neurotoxic than the A peptide(Selkoe 2001, Findeis

Benefits Of Using Abdominal Subcutaneous Tissue And...
Ideally biopsies of abdominal subcutaneous tissue and salivary glands should be used for the Congo
red staining test, and it is positive if the sample has apple–green birefringence in appearance under
polarized light. If the sample was inconclusive or negative, then the provider should have the
affected organ biopsied to ensure an accurate diagnosis. The reason one should investigate for
amyloid deposits via more invasive biopsy techniques is due to the higher risk of mortality
associated with misdiagnosis and delayed or lack of treatment. If renal biopsies are warranted,
sufficient amounts of amyloid deposits can be found around the glomerular basement membranes.
Urine testing for paraprotein is not specific enough for the diagnosis of AL, for many gammopathies
present with this in the urine. Once biopsies are positive, then the amyloid deposits should be tested
via immunofluorescence microscopy to obtain valuable information regarding its makeup.
Immunohistochemistry can be used as well, but it is not as successful in providing compositional
information for AL as immunofluorescence. AL should be differentiated from the other forms of
amyloidosis, such as hereditary amyloidosis, inflammatory amyloidosis, and hemodialysis–related
amyloidosis. Randall–type light chain deposition disease (LCDD) should also be included in the
differential (Desport et al., 2012).
To Rule Out Differential Diagnoses Jerzykowska et al. (2014) stressed the importance of ruling out
all other

How Do Pentraxins Help Detect Alzheimer 's Disease? Humans?
Briana Momchilovich
BIO 206
Writing Assignment #3
Detailed focus question: How do pentraxins help detect Alzheimer's disease in humans?
I. At the beginning to have a good understanding of the topic I will explain what the functions or
calcium–binding proteins and the locations of calcium–binding proteins. I am going to do this so the
reader has a better background understanding on the main topic of the paper.
A. Functions of calcium–binding proteins (Swanson el al., 1992).
1. Regulates mostly cellular processes.
a. They are needed for second messenger signals.
2. Calcium–binding proteins bind directly to Ca2+.
a. Regulates the amount of Ca2+ in the cytosol.
3. They have a huge effect on neurons.
a. This has an effect on learning and ... Show more content on Helpwriting.net ...
3. The C–reactive protein is usually produced in the liver of humans.
C. SAP – Serum amyloid P (Swanson el al., 1992).
1. The basic feature of serum amyloid P is it has a high relationship with phospholipids that are
negatively charged.
2. The function of serum amyloid P binds to calcium and it consists of a dimer of pentamer.
a. This allows for defense from pathogens from the body.
3. Serum amyloid P is usually produced in the liver of humans.
III. This last section I will combine all of the ideas that were made above. I will talk about what
Alzheimer's disease is and how C–reactive proteins and serum amyloid P proteins relationship to
Alzheimer's disease.
A. Alzheimer's disease is a very common disease in the older generations (Dominguez–Prieto el al.,
2017).
1. The disease is a progressive disease and it ends up leading to loss of memory.
2. Alzheimer's disease is caused by the increase of beta–amyloid protein.
a. Beta–amyloid protein is what leads to nerve cells dying.
3. Genetic too have a lot to do with Alzheimer's disease also.
a. When a person has a certain gene mutation they are a lot more likely to have Alzheimer's disease.

b. The apoE4 gene is the gene that has the strongest correlation with Alzheimer's disease.
B. C–reactive proteins relationship to Alzheimer's disease (Yarchoan el al., 2013).
1. There is an increase of C–reactive proteins in people that have Alzheimer's disease.

Essay on Alzheimer's: A Look into the Disease
AD: A Look into the Disease
Background problem Despite being known for over one hundred years the cause of Alzheimer's
disease (AD) is still not completely understood. This terminal disease affects about 800,000 people
in the UK and is expected to greatly increase in number of cases in the coming years. AD has
proven to be an elusive disease to understand; yet it is more important than ever to continue
researching AD in attempt to find a cure for the many people and family members that this disease
affects.
Purpose
Since 1907, when Alois Alzheimer characterized AD, many hypotheses and theories have been
developed. However, there has been little progress toward understanding the pathophysiology that
could lead to a cure. ... Show more content on Helpwriting.net ...
Language problems develop where the patient will have difficulty naming simple objects or
maintaining conversation. A person may also wander as the disease develops. The patient will be in
a previously familiar area, but feel completely lost and not know how to get back home. Reasoning
skills including ability to make decisions and judgments are affected. Eventually the disease
progresses to the brainstem affecting vital functions eventually resulting in death. One hypothesis on
the etiology of AD is the Amyloid Cascade Hypothesis. The Amyloid Cascade Hypothesis is based
on the defining characteristics of AD being amyloid plaques and neurofibrillary tangles in the brain.
This hypothesis basically proposes accumulation of amyloid–beta is the first pathological event that
leads to the neurofibrillary tangles and eventually AD. This hypothesis is not universally accepted
because there is no mechanism that proves that amyloid–beta accumulation causes neurofibrillary
tangles. The reason the amyloid–beta cannot be definitively linked to the formation of
neurofibrillary tangles is the lack of evidence to prove whether amyloid–beta is harmful or not.
Recent theories suggest that oligomers of amyloid proteins are the cause of AD. Some other theories
that may lead to or cause AD include: oxidative stress, mitochondrial dysfunction,
Prion/transmission,

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