This document discusses inborn errors of amino acid metabolism. It begins by defining inborn errors of metabolism as inherited metabolic disorders caused by enzymatic defects present from birth. It then discusses several specific inborn errors of amino acid metabolism, including phenylketonuria (PKU), alkaptonuria, tyrosinemia, and albinism. For each, it provides a brief overview of causes, symptoms, diagnosis, and treatment. The document concludes by discussing additional inborn errors of amino acid metabolism such as urea cycle defects, homocystinuria, maple syrup urine disease, hyperprolinemia, nonketotic hyperglycinemia, hyperoxaluria, and glycinuria.
An inherited enzyme deficiency leading to the disruption of normal bodily metabolism.
Accumulation of a toxic substrate.
Impaired formation of a product normally produced by the deficient enzyme.
Galactosemia is a rare, hereditary disorder of carbohydrate metabolism that affects the body's ability to convert galactose (a sugar contained in milk, including human mother's milk) to glucose (a different type of sugar).
An inherited enzyme deficiency leading to the disruption of normal bodily metabolism.
Accumulation of a toxic substrate.
Impaired formation of a product normally produced by the deficient enzyme.
Galactosemia is a rare, hereditary disorder of carbohydrate metabolism that affects the body's ability to convert galactose (a sugar contained in milk, including human mother's milk) to glucose (a different type of sugar).
Alkaptonuria is a rare genetic metabolic disorder characterized by the accumulation of homogentisic acid in the body. Affected individuals lack enough functional levels of an enzyme required to breakdown homogentisic acid. Affected individuals may have dark urine or urine that turns black when exposed to air.
IEM comprise a group of disorders in which a single gene defect causes a clinically significant block in a metabolic pathway resulting either in accumulation of substrate behind the block or deficiency of the product.
Amino acid metabolism disorders are hereditary metabolic disorders. Hereditary disorders occur when parents pass the defective genes that cause these disorders on to their children. Amino acids are the building blocks of proteins and have many functions in the body. Hereditary disorders of amino acid processing (metabolism) can result from defects either in the breakdown of amino acids or in the body’s ability to get amino acids into cells.
MSUD is metabolic genetic error . It happens due to lack of an enzyem that degrades specific amino acids
Homocystinuria is also a metbolic genetic error due to an enzyme defficiency it leads to an accumulation of homocystein and related chemical in the blood
Alkaptonuria is a rare genetic metabolic disorder characterized by the accumulation of homogentisic acid in the body. Affected individuals lack enough functional levels of an enzyme required to breakdown homogentisic acid. Affected individuals may have dark urine or urine that turns black when exposed to air.
IEM comprise a group of disorders in which a single gene defect causes a clinically significant block in a metabolic pathway resulting either in accumulation of substrate behind the block or deficiency of the product.
Amino acid metabolism disorders are hereditary metabolic disorders. Hereditary disorders occur when parents pass the defective genes that cause these disorders on to their children. Amino acids are the building blocks of proteins and have many functions in the body. Hereditary disorders of amino acid processing (metabolism) can result from defects either in the breakdown of amino acids or in the body’s ability to get amino acids into cells.
MSUD is metabolic genetic error . It happens due to lack of an enzyem that degrades specific amino acids
Homocystinuria is also a metbolic genetic error due to an enzyme defficiency it leads to an accumulation of homocystein and related chemical in the blood
AMINO ACID METABOLISM DISORDERS Twenty amino acids, including nine that cannot be synthesized in humans and must be obtained through food, are involved in metabolism. Amino acids are the building blocks of proteins; some also function as or are synthesized into important molecules in the body such as neurotransmitters, hormones, pigments and oxygen-carrying molecules.
Inborn errors of amino acid metabolismRamesh Gupta
Inherited disorders of amino acid metabolism e.g. phenylketonuria, maple syrup urine disease, alkaptonuria, homocystinuria, Hartnup disease etc for medical, biochemistry and biology undergraduates
Disorders of amino acid metabolism
Disorders of renal amino acid transport
Disorders of carbohydrate metabolism and transport
Carbohydrate-deficient protein syndromes
carbohydrate metabolism and transport
Disorders of fatty acid oxidation
Disorders of purine and pyrimidine metabolism
Disorders of lipid and lipoprotein metabolism
Ceroid lipofuscinosis and other lipidoses.
Disorders of serum lipoproteins
Lysosomal disorders
Peroxisomal disorders
Disorders of metal metabolism
Porphyrias
designed for undergraduate level teaching of nitrogen metabolism focusing on amino acid metabolism in biochemistry. this is second in the series of three lectures. ideal for MBBS level teaching
congenital vertebral anomaly. Congenital vertebral anomalies are a collection of malformations of the spine. Most, around 85%, are not clinically significant, but they can cause compression of the spinal cord by deforming the vertebral canal or causing instability. This condition occurs in the womb.
Activation of gene expression by transcription factorsSaad Salih
in eukaryotic cells, environmental stimuli commonly lead to activation of transcription factors and alteration of gene expression levels1. ... For example, the interaction between a transcription factor and DNA can be perturbed by either a change in DNA sequence or a change in the accessibility of the DNA by nucleosomes
Complications of abnormal lipid levels
Generally, a high total cholesterol level (which includes LDL, HDL, and VLDL cholesterol), particularly a high level of LDL (the "bad") cholesterol, increases the risk of atherosclerosis and thus the risk of heart attack or strok
Anatomy and function of the dural venous sinusesSaad Salih
Dural Venous Sinuses
The dural venous sinuses lie between the periosteal and meningeal layers of the dura mater. They are best thought of as collecting pools of blood, which drain the central nervous system, the face, and the scalp. All the dural venous sinuses ultimately drain into the internal jugular vein. Unlike most veins of the body, the dural venous sinuses do not have valves.
There are eleven venous sinuses in total. The straight, superior, and inferior sagittal sinuses are found in the falx cerebri of the dura mater. They converge at the confluence of sinuses (overlying the internal occipital protuberance). The straight sinus is a continuation of the great cerebral vein and the inferior sagittal sinus.
From the confluence, the transverse sinus continues bi-laterally and curves into the sigmoid sinus to meet the opening of the internal jugular vein.
The cavernous sinus drains the ophthalmic veins and can be found on either side of the sella turcica. From here, the blood returns to the internal jugular vein via the superior or inferior petrosal sinuses.
Role of hypothalamus in regulation of body temperatureSaad Salih
Thermoregulation is a process that allows your body to maintain its core internal temperature. All thermoregulation mechanisms are designed to return your body to homeostasis. This is a state of equilibrium.
A healthy internal body temperature falls within a narrow window. The average person has a baseline temperature between 98°F (37°C) and 100°F (37.8°C). Your body has some flexibility with temperature. However, if you get to the extremes of body temperature, it can affect your body’s ability to function. For example, if your body temperature falls to 95°F (35°C) or lower, you have “hypothermia.” This condition can potentially lead to cardiac arrest, brain damage, or even death. If your body temperature rises as high as 107.6°F (42 °C), you can suffer brain damage or even death.
Many factors can affect your body’s temperature, such as spending time in cold or hot weather conditions.
Factors that can raise your internal temperature include:
fever
exercise
digestion
Factors that can lower your internal temperature include:
drug use
alcohol use
metabolic conditions, such as an under-functioning thyroid gland
Your hypothalamus is a section of your brain that controls thermoregulation. When it senses your internal temperature becoming too low or high, it sends signals to your muscles, organs, glands, and nervous system. They respond in a variety of ways to help return your temperature to normal.
Respiratory epithelium, or airway epithelium,[1] is a type of ciliated columnar epithelium found lining most of the respiratory tract as respiratory mucosa,[2] where it serves to moisten and protect the airways. It is not present in the vocal cords of the larynx, or the oropharynx and laryngopharynx, where instead the epithelium is stratified squamous.[3] It also functions as a barrier to potential pathogens and foreign particles, preventing infection and tissue injury by the secretion of mucus and the action of mucociliary clearance.
Contents
1 Structure
1.1 Cells
2 Function
3 Clinical significance
4 References
5 Additional images
micro teaching on communication m.sc nursing.pdfAnurag Sharma
Microteaching is a unique model of practice teaching. It is a viable instrument for the. desired change in the teaching behavior or the behavior potential which, in specified types of real. classroom situations, tends to facilitate the achievement of specified types of objectives.
Ozempic: Preoperative Management of Patients on GLP-1 Receptor Agonists Saeid Safari
Preoperative Management of Patients on GLP-1 Receptor Agonists like Ozempic and Semiglutide
ASA GUIDELINE
NYSORA Guideline
2 Case Reports of Gastric Ultrasound
Tom Selleck Health: A Comprehensive Look at the Iconic Actor’s Wellness Journeygreendigital
Tom Selleck, an enduring figure in Hollywood. has captivated audiences for decades with his rugged charm, iconic moustache. and memorable roles in television and film. From his breakout role as Thomas Magnum in Magnum P.I. to his current portrayal of Frank Reagan in Blue Bloods. Selleck's career has spanned over 50 years. But beyond his professional achievements. fans have often been curious about Tom Selleck Health. especially as he has aged in the public eye.
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Introduction
Many have been interested in Tom Selleck health. not only because of his enduring presence on screen but also because of the challenges. and lifestyle choices he has faced and made over the years. This article delves into the various aspects of Tom Selleck health. exploring his fitness regimen, diet, mental health. and the challenges he has encountered as he ages. We'll look at how he maintains his well-being. the health issues he has faced, and his approach to ageing .
Early Life and Career
Childhood and Athletic Beginnings
Tom Selleck was born on January 29, 1945, in Detroit, Michigan, and grew up in Sherman Oaks, California. From an early age, he was involved in sports, particularly basketball. which played a significant role in his physical development. His athletic pursuits continued into college. where he attended the University of Southern California (USC) on a basketball scholarship. This early involvement in sports laid a strong foundation for his physical health and disciplined lifestyle.
Transition to Acting
Selleck's transition from an athlete to an actor came with its physical demands. His first significant role in "Magnum P.I." required him to perform various stunts and maintain a fit appearance. This role, which he played from 1980 to 1988. necessitated a rigorous fitness routine to meet the show's demands. setting the stage for his long-term commitment to health and wellness.
Fitness Regimen
Workout Routine
Tom Selleck health and fitness regimen has evolved. adapting to his changing roles and age. During his "Magnum, P.I." days. Selleck's workouts were intense and focused on building and maintaining muscle mass. His routine included weightlifting, cardiovascular exercises. and specific training for the stunts he performed on the show.
Selleck adjusted his fitness routine as he aged to suit his body's needs. Today, his workouts focus on maintaining flexibility, strength, and cardiovascular health. He incorporates low-impact exercises such as swimming, walking, and light weightlifting. This balanced approach helps him stay fit without putting undue strain on his joints and muscles.
Importance of Flexibility and Mobility
In recent years, Selleck has emphasized the importance of flexibility and mobility in his fitness regimen. Understanding the natural decline in muscle mass and joint flexibility with age. he includes stretching and yoga in his routine. These practices help prevent injuries, improve posture, and maintain mobilit
Title: Sense of Taste
Presenter: Dr. Faiza, Assistant Professor of Physiology
Qualifications:
MBBS (Best Graduate, AIMC Lahore)
FCPS Physiology
ICMT, CHPE, DHPE (STMU)
MPH (GC University, Faisalabad)
MBA (Virtual University of Pakistan)
Learning Objectives:
Describe the structure and function of taste buds.
Describe the relationship between the taste threshold and taste index of common substances.
Explain the chemical basis and signal transduction of taste perception for each type of primary taste sensation.
Recognize different abnormalities of taste perception and their causes.
Key Topics:
Significance of Taste Sensation:
Differentiation between pleasant and harmful food
Influence on behavior
Selection of food based on metabolic needs
Receptors of Taste:
Taste buds on the tongue
Influence of sense of smell, texture of food, and pain stimulation (e.g., by pepper)
Primary and Secondary Taste Sensations:
Primary taste sensations: Sweet, Sour, Salty, Bitter, Umami
Chemical basis and signal transduction mechanisms for each taste
Taste Threshold and Index:
Taste threshold values for Sweet (sucrose), Salty (NaCl), Sour (HCl), and Bitter (Quinine)
Taste index relationship: Inversely proportional to taste threshold
Taste Blindness:
Inability to taste certain substances, particularly thiourea compounds
Example: Phenylthiocarbamide
Structure and Function of Taste Buds:
Composition: Epithelial cells, Sustentacular/Supporting cells, Taste cells, Basal cells
Features: Taste pores, Taste hairs/microvilli, and Taste nerve fibers
Location of Taste Buds:
Found in papillae of the tongue (Fungiform, Circumvallate, Foliate)
Also present on the palate, tonsillar pillars, epiglottis, and proximal esophagus
Mechanism of Taste Stimulation:
Interaction of taste substances with receptors on microvilli
Signal transduction pathways for Umami, Sweet, Bitter, Sour, and Salty tastes
Taste Sensitivity and Adaptation:
Decrease in sensitivity with age
Rapid adaptation of taste sensation
Role of Saliva in Taste:
Dissolution of tastants to reach receptors
Washing away the stimulus
Taste Preferences and Aversions:
Mechanisms behind taste preference and aversion
Influence of receptors and neural pathways
Impact of Sensory Nerve Damage:
Degeneration of taste buds if the sensory nerve fiber is cut
Abnormalities of Taste Detection:
Conditions: Ageusia, Hypogeusia, Dysgeusia (parageusia)
Causes: Nerve damage, neurological disorders, infections, poor oral hygiene, adverse drug effects, deficiencies, aging, tobacco use, altered neurotransmitter levels
Neurotransmitters and Taste Threshold:
Effects of serotonin (5-HT) and norepinephrine (NE) on taste sensitivity
Supertasters:
25% of the population with heightened sensitivity to taste, especially bitterness
Increased number of fungiform papillae
- Video recording of this lecture in English language: https://youtu.be/lK81BzxMqdo
- Video recording of this lecture in Arabic language: https://youtu.be/Ve4P0COk9OI
- Link to download the book free: https://nephrotube.blogspot.com/p/nephrotube-nephrology-books.html
- Link to NephroTube website: www.NephroTube.com
- Link to NephroTube social media accounts: https://nephrotube.blogspot.com/p/join-nephrotube-on-social-media.html
These lecture slides, by Dr Sidra Arshad, offer a quick overview of physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar leads (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
Title: Sense of Smell
Presenter: Dr. Faiza, Assistant Professor of Physiology
Qualifications:
MBBS (Best Graduate, AIMC Lahore)
FCPS Physiology
ICMT, CHPE, DHPE (STMU)
MPH (GC University, Faisalabad)
MBA (Virtual University of Pakistan)
Learning Objectives:
Describe the primary categories of smells and the concept of odor blindness.
Explain the structure and location of the olfactory membrane and mucosa, including the types and roles of cells involved in olfaction.
Describe the pathway and mechanisms of olfactory signal transmission from the olfactory receptors to the brain.
Illustrate the biochemical cascade triggered by odorant binding to olfactory receptors, including the role of G-proteins and second messengers in generating an action potential.
Identify different types of olfactory disorders such as anosmia, hyposmia, hyperosmia, and dysosmia, including their potential causes.
Key Topics:
Olfactory Genes:
3% of the human genome accounts for olfactory genes.
400 genes for odorant receptors.
Olfactory Membrane:
Located in the superior part of the nasal cavity.
Medially: Folds downward along the superior septum.
Laterally: Folds over the superior turbinate and upper surface of the middle turbinate.
Total surface area: 5-10 square centimeters.
Olfactory Mucosa:
Olfactory Cells: Bipolar nerve cells derived from the CNS (100 million), with 4-25 olfactory cilia per cell.
Sustentacular Cells: Produce mucus and maintain ionic and molecular environment.
Basal Cells: Replace worn-out olfactory cells with an average lifespan of 1-2 months.
Bowman’s Gland: Secretes mucus.
Stimulation of Olfactory Cells:
Odorant dissolves in mucus and attaches to receptors on olfactory cilia.
Involves a cascade effect through G-proteins and second messengers, leading to depolarization and action potential generation in the olfactory nerve.
Quality of a Good Odorant:
Small (3-20 Carbon atoms), volatile, water-soluble, and lipid-soluble.
Facilitated by odorant-binding proteins in mucus.
Membrane Potential and Action Potential:
Resting membrane potential: -55mV.
Action potential frequency in the olfactory nerve increases with odorant strength.
Adaptation Towards the Sense of Smell:
Rapid adaptation within the first second, with further slow adaptation.
Psychological adaptation greater than receptor adaptation, involving feedback inhibition from the central nervous system.
Primary Sensations of Smell:
Camphoraceous, Musky, Floral, Pepperminty, Ethereal, Pungent, Putrid.
Odor Detection Threshold:
Examples: Hydrogen sulfide (0.0005 ppm), Methyl-mercaptan (0.002 ppm).
Some toxic substances are odorless at lethal concentrations.
Characteristics of Smell:
Odor blindness for single substances due to lack of appropriate receptor protein.
Behavioral and emotional influences of smell.
Transmission of Olfactory Signals:
From olfactory cells to glomeruli in the olfactory bulb, involving lateral inhibition.
Primitive, less old, and new olfactory systems with different path
Prix Galien International 2024 Forum ProgramLevi Shapiro
June 20, 2024, Prix Galien International and Jerusalem Ethics Forum in ROME. Detailed agenda including panels:
- ADVANCES IN CARDIOLOGY: A NEW PARADIGM IS COMING
- WOMEN’S HEALTH: FERTILITY PRESERVATION
- WHAT’S NEW IN THE TREATMENT OF INFECTIOUS,
ONCOLOGICAL AND INFLAMMATORY SKIN DISEASES?
- ARTIFICIAL INTELLIGENCE AND ETHICS
- GENE THERAPY
- BEYOND BORDERS: GLOBAL INITIATIVES FOR DEMOCRATIZING LIFE SCIENCE TECHNOLOGIES AND PROMOTING ACCESS TO HEALTHCARE
- ETHICAL CHALLENGES IN LIFE SCIENCES
- Prix Galien International Awards Ceremony
3. Noor Aldin Nabil
Saad Salih Mahdi
Preparation and design
of the seminar
Iminoglycinuria
4. Inborn errors of metabolism (IEM) are a group of inherited metabolic disorders leading to enzymatic
defects in the hum an m etabolism . As its nam e im plies, inborn errors m eans birth defects in newborn
infants which passed down from fam ily and affecting m etabolism . Hence, it is called Inborn errors of
m etabolism or inherited m etabolic disorders. IEM can appear at birth or later in life such as
phenylketonuria, albinism , lactose intolerance, Gaucher disease, Fabry disease etc. IEM refers a condition
where in body’s m etabolism is affected due to genetic disorders. The cause of IEM is m utations in a gene
that code for an enzym e leading to synthesis of defective enzym e activity or deficiency of an enzym e that
affects the norm al function of a m etabolic pathway. The m ain indication of IEM is an excess storage or
accum ulation of specific m etabolites in tissues, organs and blood which further m anifest to health
diseases. In last decades, several hundreds of different IEM have been identified. Most IEM are rare but
som e are life threatening. Although, m ost people do not know what inherited m etabolic disorders are
and m ay never have heard of them .
Therefore, in this presentation you are going to study the basic concept, genetic basis and m etabolic
consequences of inborn errors of m etabolism .
Contents of This presentation
5. 01
Th e Disease
General info about
Disease
02
Diagnosis
Talk about how can
diagnosis
03
Symptoms
Talk about common
symptoms
04
Causes
Talk about causes of
Each disease
05
Treatment
Talk about how can
Treat the disease
06
Chemistry
Talk about chemistry
Correlations
6. Introduction
Inborn errors of amino acid
metabolism are metabolic disorders
which impair the synthesis and
degradation of amino acids.
7. Phenylketonuria
01
(PKU) is an inborn error of metabolism that
results in decreased metabolism of the
amino acid phenylalanine.
10. Figure 1.3 Inherited enzyme defects in catabolic pathway of phenylalanine and Tyrosine and the defective enzyme in indicated by
red summing junctions and the metabolic diseases shaded in the Yellow color (Taken from Principle of Biochemistry, Nelson & Cox,
2004).
11. Alkaptonuria
02
Alkaptonuria is the first inborn errors of
metabolism discovered by Garrod. Estimated
incident of alkaptonuria is about 2-5 per
million live births.
13. Alkaptonuria
C low
low proteins diet are
recommended to control
of the ochronosis
reducing
by reducing the level of
hom ogentisic acid in
tissues
Newborn
Newborn
screening and oral
nitisinone therapy
m ay also helpful
for the treatm ent
of this disease
Treatment
Vitam in C
15. Tyrosinemia
03
Tyrosinemia is also metabolic genetic disorders of
phenylalanine catabolism, occur usually in newborns.
This disorder results due to the absence or deficiency of
enzymes involved in the multiple steps of phenylalanine
and tyrosine catabolism . Untreated tyrosinemia can be
fatal for life .
17. ● Diarrhea
● vom iting
● renal tubular dysfunction
● vitam in D-resistant rickets
● acute interm ittent porphyria
● abdom inal pain
● neuropsychiatric findings
● sensitive to light
● hypertension
● Progressive liver
● renal failure.
● Accum ulation of tyrosine can affect
on eyes, skin
● m ental developm ent
● Persistent keratitis
● hyperkeratosis occur on the fingers,
palm s of hands and soles of feet
● m oderate m ental retardation.
Clinical symptoms
Tyrosinemia I Tyrosinemia II
19. Albinism
04
Albinism is another congenital hereditary disorder of
amino acid metabolism in which biosynthesis of melanin
is defective. Melanin is a color pigment absent in certain
parts of the body such as eyes, patches of skin and
areas of hair. Normally, melanin is polymers of the
amino acid tyrosine which gives color to skin, hair and
eyes
20. Causes
Albinism is caused by the mutation in a
gene coding tyrosine hydroxylase enzyme.
This enzyme converts tyrosine to 3,4-
dihydroxy phenylalanine (DOPA) .
Deficient activity of this enzyme leads to
albinism in which melanin formation is
missing. This condition is referred to
hypomelanosis .
21. Symptoms of the Disease
Albinism can affect eye and skin in infants or people
This condition refers to oculocutaneous albinism (OCA) resulting in
hypopigmentation of the hair, skin and eyes
this disease leads to extremely pale skin, poor vision and white hair
22. About the Disease
Treatm en t
There is no treatment
for albinism
Treatment Diagnosis
Diagnosis is based on
biochemical finding of
hypopigmentation of the
skin and hair. Molecular
genetic testing of OCA
gene is available for the
albinism diagnosis.
require visual rehabilitation
such as wear prescription
lenses for correction of
refractive errors, use hats with
brims and dark glasses or
transition lenses to reduce
discomfort from bright light and
wear protective clothing to
protect skin from sun exposure
24. Urea cycle defects
05
This is an autosomal recessive inherited
genetic disorder that affecting the urea
cycle.
25. About disease
This is an autosomal recessive inherited
genetic disorder that affecting the urea cycle.
The liver is a vital organ which plays a
promising role in detoxification of
nitrogenous wastes by forming the compound
urea through the urea cycle. Urea is a major
disposal byproduct of amino acids. The
disturbance in the normal urea cycle leads to
accumulation of urea causing cellular toxicity .
The estimated incidence of urea cycle defects
is about 1 in 8,000 live births and generally
occurs in the first few days of life.
26. Urea cycle defects
The urea cycle disorders
(UCDs) are caused by
defective or total absence of
catalytic activity of the first five
enzymes involved in the urea
cycle . Errors in this cycle, body
unable to detoxify nitrogen
content leads to abnormal
accumulation of ammonia and
other precursor metabolites.
These enzymes are:
defect in the arginase enzyme resulting argenimia while absence of argininosuccinase and
carbamoyl phosphate synthase-I may also cause argininosuccinic acidemia and carbamoyl
phosphate I deficiency respectively.
27. Treatment
Nutritional modification with
low protein diet may help in
controlling the level of
ammonia in the body
Sodium phenylbutyrate is the primary
medication used to treat urea cycle
disorders. This drug allows an
alternative pathway to disposal of
nitrogen from the body.
If medicine and nutritional
treatment failed, liver
transplantation becomes an
option for UCD’s patient.
28. Urea cycle defects
Clinical symptoms
hyperammonemia condition
resulting in neurologic damage
cerebral edema
lethargy
anorexia, hyper- or hypoventilation
Hypothermia
seizures, neurologic posturing
long term hyperammonemia is toxic
to human beings resulting in mental
retardation
Measurement the elevated level of
ammonia, arginine, arginosuccinate in
plasma and orotic acids in urine are
used to diagnosis of urea cycle
disorders
Diagnosis
31. Homocystinuria
High level of homocysteine
in cells causing lipid
peroxidation
fibrosis
atherogenesis and affecting
muscles cardiovascular
system and nervous
system
Estimation of the level of homocysteine,
total homocysteine, homocysteine-
cysteine mixed disulfide, and methioninein
plasma.
Diagnosis :
Vitamin B6 (Pyridoxine) therapy, betaine, folate and
vitamin B12 supplementation are used to control the
biochemical abnormalities , especially to management
Treatment :
the plasma homocysteine and homocysteine
concentrations and prevent thrombosis.
32. The most common form of
homocystinuria affects at least 1 in
200,000 to 335,000 people
worldwide.
The disorder appears to be more
common in some countries, such
as Ireland (1 in 65,000)
Germany (1 in 17,800)
Norway (1 in 6,400)
Qatar (1 in 1,800)
The rarer forms of homocystinuria
each have a small number of
cases reported in the scientific
literature.
*We have searched about the incidence
of this and other diseases in Iraq, and we
have not found official rates.
Frequency
Homocystinuria
33. Maple syrup urine
disease (MSUD)
07
is an inherited disorder of branched chain
amino acids. Affected people with MSUD
have a defective gene inherited from their
family.
36. Hyperprolinemia
08
is a condition which occurs when the amino acid proline
is not broken down properly by the enzymes proline
oxidase or pyrroline -5-carboxylate dehydrogenase,
causing a buildup of proline in the body
37. Hyperprolinemia
Hyperprolinemia can also occur with other conditions, such as
malnutrition or liver disease. In particular, individuals with
conditions that cause elevated levels of lactic acid in the blood,
such as lactic acidemia, are likely to have elevated proline levels,
because lactic acid inhibits the breakdown of proline
proline
38. NKH
09
Nonketotic hyperglycinemia (NKH) is a genetic condition
that can lead to serious neurological problems, coma,
and death. “Hyperglycinemia ” refers to abnormally high
levels of a molecule, glycine. The word “nonketotic ”
distinguishes NKH from certain other health conditions
that can cause increased glycine.
40. Hyperoxaluria
10
Hyperoxaluria occurs when you have too much oxalate in your
urine. Oxalate is a natural chemical in your body, and it's also
found in certain types of food. But too much oxalate in your urine
can cause serious problems.
Hyperoxaluria can be caused by inherited (genetic) disorders, an
intestinal disease or eating too many oxalate -rich foods. The long -
term health of your kidneys depends on early diagnosis and
prompt treatment of hyperoxaluria.
41. Hyperoxaluria
Symptoms
Severe or sudden back pain
Pain in the area below the
ribs on the back (flank) that
doesn't go away
Blood in the urine
Frequent urge to urinate
Pain when urinating
Chills or fever
type
Primary hyperoxaluria.
Oxalosis
Enteric hyperoxaluria
Hyperoxaluria related to
eating high-oxalate foods
44. Glycinuria
1דּ
Glycinuria , is an autosomal recessive disorder of renal tubular
transport affecting reabsorption of the amino acid glycine, and
the amino acids proline and hydroxyproline. This results in excess
urinary excretion of all three acids ( -uria denotes "in the urine")
Iminoglycinuria is a rare and complex disorder, associated with a
number of genetic mutations that cause defects in both renal and
intestinal transport systems of glycine and amino acids.
45. Glycinuria
Poor appetite
Sleeping longer or more
often
Tiredness
Irritability
Fever
Vomiting
Weak muscle tone (also
known as hypotonia)
Delayed growth
Clinical symptoms
47. “ Th e greatest disease in th e West
today is n ot TB or leprosy; it is
bein g un wan ted, un loved, an d
un cared for. We can cure ph ysical
diseases with m edicin e, but th e
on ly cure for lon elin ess, despair,
an d h opelessn ess is love.”
48. 1. Garrod. Inborn Errors of Metabolism. Oxford University Press. 1923.
2. Martins A. M. Inborn errors of m etabolism : a clinical overview Sao
Paulo Med J/Rev Paul Med. 1999; 117(6):251-65.
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