A comprehensive presentation on Biochemical and clinical aspects of Collagen for MBBS, BDS, B Pharm & Biotechnology students to facilitate self- study.
Collagen is most abundant protein in mammals, the main fibrous component of skin, bone, tendon and cartilage.
Collagen comprises one- third of the total protein, accounts for three-quarters of the dry weight of skin, and is the most prevalent component of the extracellular matrix.
The collagen family consists of 28 members and these are classified by Roman numbers on the basis of their chronology of discovery.
Collagen is most abundant protein in mammals, the main fibrous component of skin, bone, tendon and cartilage.
Collagen comprises one- third of the total protein, accounts for three-quarters of the dry weight of skin, and is the most prevalent component of the extracellular matrix.
The collagen family consists of 28 members and these are classified by Roman numbers on the basis of their chronology of discovery.
Biochemistry of musculoskeletal system. biochemistry of MSS prepared by Fikad...fikaduseyoum1
biochemistry of MSS prepared by Fikadu Seyoum Tola. This ppt essentially discuss about collegen biosnthesis, defect and muscle energy metabolism with its regulations.
Collagen /certified fixed orthodontic courses by Indian dental academy Indian dental academy
Welcome to Indian Dental Academy
The Indian Dental Academy is the Leader in continuing dental education , training dentists in all aspects of dentistry and offering a wide range of dental certified courses in different formats.
Indian dental academy has a unique training program & curriculum that provides students with exceptional clinical skills and enabling them to return to their office with high level confidence and start treating patients
State of the art comprehensive training-Faculty of world wide repute &Very affordable.
Collagen / /certified fixed orthodontic courses by Indian dental academy Indian dental academy
Welcome to Indian Dental Academy
The Indian Dental Academy is the Leader in continuing dental education , training dentists in all aspects of dentistry and offering a wide range of dental certified courses in different formats.
Indian dental academy has a unique training program & curriculum that provides students with exceptional clinical skills and enabling them to return to their office with high level confidence and start treating patients
State of the art comprehensive training-Faculty of world wide repute &Very affordable.
Biotin (vitamin b7) biological functions, clinical indications and its techn...rohini sane
An illustrative presentation on Biotin (Vitamin B7), clinical indications and technological applications for Medical, Dental, Pharmacology & Biotechnology students to facilitate easy- learning.
An illustrative and lucid presentation on Scurvy (deficiency of vitamin C) for Medical, Dental, Pharmacology & Biotechnology students to facilitate easy- learning.
An illustrative presentation on Vitamin C (Ascorbic acid) and Scurvy for Medical, Dental, Pharmacology & Biotechnology students to facilitate easy- learning.
An illustrative presentation on Microscopic examination of Urine for Medical, Dental, Pharmacology and Biotechnology students to facilitate easy- learning and self-study..
Urinalysis for detection of abnormal constituentsrohini sane
An illustrative presentation on Urinalysis for detection of abnormal constituents for medical ,dental , pharmacology and biotechnology students to facilitate easy-learning.
Urinalysis for detection of normal inorganic and organic constituentsrohini sane
An illustrative presentation on urinalysis for detection of normal inorganic and organic constituents for medical, dental , pharmacology and biotechnology students to facilitate easy-learning.
Biochemical kidney function tests with their clinical applicationsrohini sane
An illustrative presentation on Biochemical kidney function tests with their clinical applications for medical ,dental, pharmacology and biotechnology student to facilitate easy-learning.
A comprehensive presentation on Total parenteral nutrition(TPN) to facilitate easy -learning for medical , dental , pharmacology and biotechnology students.
Nutritional management of clinical disordersrohini sane
A lucid presentation Nutritional management of clinical disorders to facilitate easy-learning for medical , dental , pharmacology and biotechnology students.
Nutritional importance of vitamins and mineralsrohini sane
A lucid presentation on Nutritional importance of vitamins and minerals for medical , dental , pharmacology and biotechnology students to facilitate easy-learning.
A lucid presentation on Basal metabolic rate ( BMR) and nutrition for medical ,dental ,pharmacology and biotechnology students to facilitate easy-learning.
Physical activity of the human body and nutritionrohini sane
A lucid presentation on Physical activity of the human body and Nutrition for medical ,dental ,pharmacology and biotechnology students for easy learning.
Couples presenting to the infertility clinic- Do they really have infertility...Sujoy Dasgupta
Dr Sujoy Dasgupta presented the study on "Couples presenting to the infertility clinic- Do they really have infertility? – The unexplored stories of non-consummation" in the 13th Congress of the Asia Pacific Initiative on Reproduction (ASPIRE 2024) at Manila on 24 May, 2024.
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Report Back from SGO 2024: What’s the Latest in Cervical Cancer?bkling
Are you curious about what’s new in cervical cancer research or unsure what the findings mean? Join Dr. Emily Ko, a gynecologic oncologist at Penn Medicine, to learn about the latest updates from the Society of Gynecologic Oncology (SGO) 2024 Annual Meeting on Women’s Cancer. Dr. Ko will discuss what the research presented at the conference means for you and answer your questions about the new developments.
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
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
New Directions in Targeted Therapeutic Approaches for Older Adults With Mantl...i3 Health
i3 Health is pleased to make the speaker slides from this activity available for use as a non-accredited self-study or teaching resource.
This slide deck presented by Dr. Kami Maddocks, Professor-Clinical in the Division of Hematology and
Associate Division Director for Ambulatory Operations
The Ohio State University Comprehensive Cancer Center, will provide insight into new directions in targeted therapeutic approaches for older adults with mantle cell lymphoma.
STATEMENT OF NEED
Mantle cell lymphoma (MCL) is a rare, aggressive B-cell non-Hodgkin lymphoma (NHL) accounting for 5% to 7% of all lymphomas. Its prognosis ranges from indolent disease that does not require treatment for years to very aggressive disease, which is associated with poor survival (Silkenstedt et al, 2021). Typically, MCL is diagnosed at advanced stage and in older patients who cannot tolerate intensive therapy (NCCN, 2022). Although recent advances have slightly increased remission rates, recurrence and relapse remain very common, leading to a median overall survival between 3 and 6 years (LLS, 2021). Though there are several effective options, progress is still needed towards establishing an accepted frontline approach for MCL (Castellino et al, 2022). Treatment selection and management of MCL are complicated by the heterogeneity of prognosis, advanced age and comorbidities of patients, and lack of an established standard approach for treatment, making it vital that clinicians be familiar with the latest research and advances in this area. In this activity chaired by Michael Wang, MD, Professor in the Department of Lymphoma & Myeloma at MD Anderson Cancer Center, expert faculty will discuss prognostic factors informing treatment, the promising results of recent trials in new therapeutic approaches, and the implications of treatment resistance in therapeutic selection for MCL.
Target Audience
Hematology/oncology fellows, attending faculty, and other health care professionals involved in the treatment of patients with mantle cell lymphoma (MCL).
Learning Objectives
1.) Identify clinical and biological prognostic factors that can guide treatment decision making for older adults with MCL
2.) Evaluate emerging data on targeted therapeutic approaches for treatment-naive and relapsed/refractory MCL and their applicability to older adults
3.) Assess mechanisms of resistance to targeted therapies for MCL and their implications for treatment selection
ARTIFICIAL INTELLIGENCE IN HEALTHCARE.pdfAnujkumaranit
Artificial intelligence (AI) refers to the simulation of human intelligence processes by machines, especially computer systems. It encompasses tasks such as learning, reasoning, problem-solving, perception, and language understanding. AI technologies are revolutionizing various fields, from healthcare to finance, by enabling machines to perform tasks that typically require human intelligence.
Ethanol (CH3CH2OH), or beverage alcohol, is a two-carbon alcohol
that is rapidly distributed in the body and brain. Ethanol alters many
neurochemical systems and has rewarding and addictive properties. It
is the oldest recreational drug and likely contributes to more morbidity,
mortality, and public health costs than all illicit drugs combined. The
5th edition of the Diagnostic and Statistical Manual of Mental Disorders
(DSM-5) integrates alcohol abuse and alcohol dependence into a single
disorder called alcohol use disorder (AUD), with mild, moderate,
and severe subclassifications (American Psychiatric Association, 2013).
In the DSM-5, all types of substance abuse and dependence have been
combined into a single substance use disorder (SUD) on a continuum
from mild to severe. A diagnosis of AUD requires that at least two of
the 11 DSM-5 behaviors be present within a 12-month period (mild
AUD: 2–3 criteria; moderate AUD: 4–5 criteria; severe AUD: 6–11 criteria).
The four main behavioral effects of AUD are impaired control over
drinking, negative social consequences, risky use, and altered physiological
effects (tolerance, withdrawal). This chapter presents an overview
of the prevalence and harmful consequences of AUD in the U.S.,
the systemic nature of the disease, neurocircuitry and stages of AUD,
comorbidities, fetal alcohol spectrum disorders, genetic risk factors, and
pharmacotherapies for AUD.
2. Biochemical aspects of Collagen
❖Biochemical aspects of Collagen:
1. Most abundant fibrous protein(major macromolecules) in human body :70 kg
body weight→ 12-14 kg of total protein→5kg of Collagen (1/3 of total protein)
2. Main Component of : connective tissue, skin(70%) ,bone (90%) tendon(85%),
cartilage ,teeth and liver(4%)
3. Synthesized by fibroblast in connective tissue and osteoblasts in bone
4. Made up of small fibrils → tropocollagen( fundamental units ) containing 3
polypeptide chains each of them in left-handed helix with 3 amino acid per turn.
5. rich in Glycine and rare amino acids like hydroxyproline, hydroxylysine
6. Cysteine and Tryptophan absent
7. have a triple helical secondary structure and rich in helix destabilizing amino
acids (Glycine ,Proline and Hydroxyproline). These amino acids prevent the
formation of the usual - helical and - pleated structure. Instead it forms a triple
helical secondary structure.
5. Types of Collagen
❖19 different Types of Collagen , composed of 30 distinct polypeptide
chains encoded by separate genes.
❖ Numbering for Types of Collagen: Roman numerals I, II, III….XIX
❖Structure of collagen types : in principle , all types of collagen are
triple helical structures . The triple helix may occur throughout the
molecule or only a part of the molecule.
❖Each one suited to performed specialized function in tissue
❖e.g. Collagen Type I →skin, Collagen Type II → bone
6. Structure of collagen Type 1
❖ Structure of collagen Type 1:
1. Triple stranded helical structure present throughout the collagen
molecule
2. Shape : rod-like molecule → 1.4 nm diameter and 300 nm length
3. Number of Amino acid residues : 1000 per for each polypeptide
chain (3000 /molecule)
4. Amino acid contribution : 1/3 rd of amino acids are Glycine (every
third amino acid in collagen is Glycine.
5. Repetitive amino acid sequence : (Gly – X –Y )n ,where X and Y
represent other amino acids
6. Proline and hydroxyproline : 100 per for each polypeptide chain
7. Function of Proline and hydroxyproline : confer rigidity to the
collagen molecule
8. Collagen Fibril formation : Triple helical molecule of collagen
assemble to form elongated fibrils . It occurs by a quarter staggered
alignment i.e. each triple helix is displaced longitudinally from its
neighbor collagen molecule by about one-quarter of its length
9. Collagen Fiber formation : Collagen Fibrils assemble to form rod like
fibers .
10. Strength of Collagen Fiber : contributed by covalent cross linking of
formed between Lysine and hydroxylysine and also between Proline
and hydroxyproline.
7. Collagen molecules in Collagen fibers
Triple helical molecule of
collagen assemble to
form elongated fibrils .
Triple stranded helical structure
present throughout the collagen
molecule
Collagen Fibrils
assemble to form
rod like fibers .
Repetitive amino acid sequence (Gly – X –Y )n
Proline and hydroxyproline confer rigidity to the collagen molecule
8. Arrangement of Tropocollagen molecules in collagen fibril
Heads of Tropocollagen molecules 64 nm Cross striations
Sections of Tropocollagen moleculeCollagen Fibril formation :
Triple helical molecule of collagen
assemble to form elongated fibrils .
It occurs by a quarter staggered
alignment i.e. each triple helix
is displaced longitudinally from
its neighbor collagen molecule
by about one-quarter of its length.
9. Tropocollagen molecule
❖Tropocollagen : Subunits of Collagen
• Shape : rod shaped
• Length : 300nm
• Thickness : 1.4 nm
• Molecular weight : 300,000
• Constituent polypeptides: three helically interwind polypeptides
of equal length (each with 1000 amino acid residues)
• Primary structure of collagen : all 3 or two out of three chains
have identical in amino acid sequence. Rich in Glycine (35%)and
Alanine(11%) , Gly-Pro-X or Gly-Hpr-X or
• Repetitive amino acid sequence : (Gly – X –Y )n ,where X and Y
represent other amino acids
• Secondary structure of collagen : Each of three polypeptide
chains of tropocollagen is itself -helix. Proline and
hydroxyproline form bends in polypeptide chains that they are
not compatible with -helix structure.
10. Collagen fibrils
❖Collagen fibril :
• Triple helical molecules are associated into Collagen fibrils.
• It consists of recurring polypeptide subunits called tropocollagen, arranged
head to tail in parallel bundles . The heads of the tropocollagen molecules are
staggered along the length of fibers ,accounting for the characteristic 64 nm
spacing of the cross striations in most collagens .
• A section of tropocollagen molecule shows the backbone of triple helix . Each
of three polypeptide chains of tropocollagen is itself -helix whose pitch and
spacing is determined by the rigid R group of the numerous Proline and
hydroxyproline residue .
• The gap between the end of one triple helix and the beginning of the next
where there is the deposition of hydroxyapatite crystals in bone formation.
11. Constituent amino acids of triple stranded helix Structure of Collagen
• ScvConstituent amino
acids of Collagen
% of total amino acids
Glycine 33
Proline and hydroxy
proline
21
Lysine and hydroxy
Lysine
3
Alanine 11
Arginine 5
Cysteine and
Tryptophan
absent
Scurvy:vitaminCdeficiency→failure ofhydroxylationofProlineandLysineleadstoreducedhydrogen
bonding→weaknessofcollagen→Brittlebonedisease:mutation→replacementofcentralGlycine
13. Forces stabilizing Triple helical secondary structure of Collagen
❖Forces stabilizing Triple helical secondary structure of Collagen:
1. Hydrogen bonds : three left handed helices are bound together by
interchain hydrogen bonds.
2. Lysinonorleucine bond: covalent cross links both within and
between triple helical units further stabilize Collagen fibers.
3. Electrostatic interactions
4. Hydrophobic interactions
14. Covalent cross-links in Collagen fibers
• Strength of Collagen Fiber : contributed by covalent cross linking formed
between Lysine and hydroxylysine and also between Proline and
hydroxyproline.
• Covalent cross links are formed both within and between triple helical units
further stabilize Collagen fibers.
• The degree of covalent cross-linking in Collagen molecule increases with age .
• In Elder individuals : skin, blood vessels (Collagen containing tissue) become
less elastic and more stiff → health complications
15. Skin :Collagen containing tissue
In Elder individuals , skin, blood vessels (Collagen containing tissue) become less elastic and
more stiff → health complications
17. Biosynthesis of collagen
❖Biosynthesis of collagen: collagen is an extracellular protein but synthesized as an
intracellular precursor molecule before becoming a mature collagen fibril.
• Site : fibroblast ,osteoblasts in bones , chondroblasts in cartilage, odontoblasts in teeth
• Cellular location : ribosomes in endoplasmic reticulum (ER)
• Precursor : preprocollagen (a single polypeptide chain) with leader peptide at amino
terminal 20000 MW and carboxy terminal 35000MW.Both are not present in mature
collagen.
• Function of preprocollagen: contains a signal peptide which directs the protein to each
endoplasmic reticulum (ER)
• Synthesis of procollagen : from preprocollagen in (ER) after cleavage of a signal peptide
• Post transcriptional modification of procollagen : hydroxylation, glycosylation and
disulfide formation . Followed by its secretion in extracellular medium by the way of Golgi
complex .
• Synthesis of collagen in extracellular medium : from preprocollagen after action of
aminopeptidase and carboxypeptidase to remove terminal amino acids. This followed by
a spontaneous assembly of polypeptide chains to form triple helical structure (with 1000
amino acids each) of collagen .
19. Structural modification of Collagen during its Synthesis
Procollagen
Tropocollagen
Collagen
Glycosylationloss of peptide potion from N-terminal and C-terminal
Each of the 3 chains is in a left handed
helix with 3 amino acids per turn.
3 Chains are further twisted in right handed way to give
cable like structure.
Hydroxylation of Proline and Lysine by Lysyl hydroxylase
and Proline hydroxylase in presence of vitamin C→
Cross linking of hydroxy proline and hydroxy lysine
Since vitamin C is required for collagen synthesis ,a connective tissue , there is a delay in
wound healing process in vitamin C deficiency.
20. Functions of Collagen
❖Functions of Collagen : triple helical molecules are associated into fibrils. There is
gap between the end of one triple helix and the beginning of the next where there
is deposition of hydroxyapatite crystals in bone formation.
1. Gives tensile strength, support and shape to tissue . To break a collagen fiber of 1
mm in diameter, a load of 10-40 kg is needed. In disease status tensile strength is
reduced.
2. Contributes to proper alignment of cells ,which in turn help in cell proliferation
and their differentiation to different tissue and organs .
3. Collagen which is exposed in blood vessels contributes to thrombus formation.
❖Collagen can be converted to
a. gelatin by boiling by splitting off some amino acids .Gelatin is highly soluble and
easily digestible. It forms gel on cooling and is provided as diet for convalescents
and invalids. But it lacks essential amino acid Tryptophan.
b. a tough hard substance on treatment with tannic acid (tannic process)
21. Genetic aspects of Collagen Synthesis
❖Genetic aspects of Collagen Synthesis :
1. Complex process
2. Involves at least 30 genes in human
3. about 8 post –transcriptional modifications
4. Inherited diseases due to gene mutations linked with collagen synthesis:
a. Ehlers-Danlos syndrome
b. Alport syndrome
c. Osteogenesis imperfecta
d. Epidermolysis bullosa
22. Abnormalities associated with collagen synthesis
Disease Abnormalities associated with collagen synthesis
Ehlers-Danlos
syndrome
Inherited disorders characterized by hyperextensibility of skin and
abnormal tissue fragility
Alport syndrome Defect in formation of type IV collagen fibers found in the basement
membrane of renal glomeruli→ hematuria and renal disease
Osteogenesis
imperfecta
Characterized by abnormal bone fragility due to deceased synthesis of
collagen
Epidermolysis bullosa due to alteration in in the structure of type VII collagen fibers→ skin
breaks and blister formation even with minor trauma
Scurvy Deficiency of vitamin C→ defective post translational modification of
collagen→ bleeding gums ,poor wound healing, subcutaneous
hemorrhage
Lathyrism (disease of
bone deformities )
CausedbyconsumptionofLathyrussativa(kesaridal)containingtoxiccompound
BetaOxalylAminoAlanine(BOAA).BOAAinhibitsenzymeLysyloxidaseand
interfereswiththecrosslinkingoflysineaminoacidresiduesincollagen.
23. Types of Ehlers-Danlos syndrome
❖Types of Ehlers Danlos syndrome :
• Ehlers-Danlos syndrome type V: inherited deficiency of Lysyl oxidase(copper
requiring enzymes)→prevents cross-linking of collagen→ arterio-vascular and
skeletal changes.
• Ehlers-Danlos syndrome type VI: inherited deficiency of Lysyl hydroxylase
→abnormalities of the eye ,severe scoliosis (abnormal vertebral curvature)
and hyperextensibility of skin and joints.
• Ehlers-Danlos syndrome type VII: non-serving of procollagen as a substrate for
the procollagen amino protease →hip dislocation , increased skin elasticity
and short stature.
24. Ehlers-Danlos syndrome : Clinical manifestations
Hyperextensibility of skin and joints
severescoliosis
(abnormalvertebralcurvature)
Ehlers-Danlos syndrome
