Deevska Review Flashcards
Why is vitamin C (ascorbic acid) important for collagen
Required as a cofactors for the enzymes involved in hydroxylation of proline and lysine residues in collagen
What does a deficiency in vit C do?
Lack of proline and lysine hydroxylation lead to impairment of the interchain H bond formation which prevents the formation of a stable triple helix and affects proper cross-linking
What is the effect of vitamin C deficiency on collagen directly
Greatly decrease the tensile strength of the assembled fiber
What disease is caused by vitamin c deficient and what are the symptoms
Scurvy
- easy bruising
- loose teeth an bleeding gums
- poor wound healing
- poor bone development
What is the main difference between the structure of elastin and collagen?
Collagen contains hydroxyproline and hydroxylysine whereas elastin contains scant amounts of this
Extensively interconnected, rubbery network that can stretch and bend in any direction when stressed, giving connective tissue elasticity
Elastin
What is the makeup of elastin
- insoluble protein polymer synthesized from a precursor tropoelastin
- rich in proline and lysine but contains scant amounts od hydroxyproline and hydroxylysine
_________ modifies lysyl side chains in tropoelastin forming a desmosine corsslinking which produces ______
Elastin
What AA are both elastin and collagen abundant in
Proline and glycine
Fibrous proline composed of alpha chains forming triple stranded helix
Collagen
What does collagen have that elastin does not have much of
Contains hydroxyproline and hydroxylysine formed by post translational hydroxylation of proline and lysin residues
Collage requires what as a reducing agent
O2, Fe2+, and vit C
What is the most abundant protein in the human body
Collagen
What types of collagen in cornea
I and VIII
What types of collagen in vitreous
II
Large complexes of heteropolysaccharide chains associated with a small amount of protein
95% carbohydrates
5% protein
Proteoglycans
Protein with a variable but typically small amount of carbohydrate
Glycoproteins
Produce a gel like matrix, form basis of the body’s ground substance, function to form ECM, serves as flexible support for ECM, sieve influencing the movement of materials through the ECM, contributes to the viscous lubricating properties of mucous secretions
Proteoglycans
What are proteoglycan aggregates composed of?
1 proteoglycan monomers
- GAGs
- a core protein
2. Hyaluronic acids
3. Link protein
What is the anchor point for the proteoglycan
Hyaluronic acid
Small protein that stabilizes the association between the core protein and hyaluronic acid in a proteoglycan
Link protein
Part of the proteoglycan monomer that us linked to a serine residue with 100s of monosaccharide chain extending out from it
Core protein
Long unbranched, heteropolysaccharide chains, six different types, always found external to the cytosol in the proteoglycan
GAGs
Characteristics of GAGs
- unbranched
- repeating disaccharide units
Large complexes of NEGATIVELY charged heteropolysaccharide chains
What gives the GAGs their unique function
Negative charge
What kind of charge does a GAG have and why
Negative because carboxyl groups and sulfate groups
What does the negative charge on the GAGs contribute to
- hydraulic absorption and resilience of synovial fluid and vitreous humor of the eye
- lubricating effects of mucous and synovial fluid
Functions of membrane bound glycoproteins
- cell surface recognition by other cells, hormones, viruses
- cell surface antigenicity
- formation of ECM and mucins
non membrane bound glycoproteins
- almost all globular proteins secreted in the plasma are glycoproteins
- many of the lysosomal proteins are glycoproteins
Structure of the carbohydrate chain of a glycoprotein
- short
- no serial repeats
- often branched
- may/may not be negatively charged
- highly variable in amount and comp of carbohydrate
Structure of the linkage between carbohydrate and protein in a glycoproteins
- N-glycosidic link: sugar chain attached to abide group of asparagine
- O-glycosidic link: sugar chain is attached to the hydroxyl group of either serine or threonine
Glycoprotein can contain one of these or both of these
What are the 6 major classes of GAGs
- chondroitin sulfate
- keratin sulfate I and II
- hyaluronic acid
- dermatan sulfate
- heparin
- heparin sulfate
What is the most abundant GAG in the body?
Chondroitin sulfate
Where is chondroitin sulfate (GAGs) found
Cartilage, tendones, ligaments, and aorta
Where is keratin sulfate I and II found
KSI: in coreans
KSII: loose connective tissue proteoglycan aggregates with chondroitin sulfate
What is the only GAG not attached to a core protein?
Hyaluronic acid
What is the only GAG not sulfated?
Hyaluronic acid
Where is hyaluronic acid found
- animal and bacteria
- synovial fluid in joints, vitreous, umbilical cord, loose connective tissue, cartilage
Where is dermatan sulfate found
Skin blood vessels, and heart valves
What is the only GAG that is intercellular
Heparin
Where is heparin found and what does it do
Intracellular component of mast cells that line arteries, especially in liver, lungs, and skin
Serves as an anticoagulant
Where is heparin sulfate found
Basement membrane