Week 5: Connective Tissue 2 - Properties and Extracellular Matrix Flashcards
What types of fibres are in CT?
Collagen, fibres and reticular
What are the morphological characteristics of collagen?
- Thickest fibre
- Each collagen fibre is composed of many collagen fibrils
- Fibrils cause a banding pattern in fibres formed
- Can form networks/ sheets
- Tropocollagen –> collagen bundles
Describe the formation of collagen.
Collagen is a family of proteins that have alpha chain (polypeptide) subunits that interact in various ways to form fibrilar collagens (fibrils –> fibres –> fibre bundles), network or sheet forming collagens in basal laminae, and linking and choring collagens (link fibrillar collagens to each other and ECM)
Formation begins with intracellular synthesis in fibroblasts.
RER:
- Synthesis of procollagen alpha chains with propeptides at each end
- Hydroxylation and attachment of sugars to chains
- Assembly of chains into triple helix procollagen molecule (soluble)
Golgi:
- Packaging of procollagen into secretory vesicles
- Exocytosis of procollagen into extracellular space
Extracellular modification
- Cleavage of terminal proppeptides by procollagen peptidases; soluble procollagen –> insoluble tropocollagen molecules
- Tropocollagen molecules aggregate to form collagen fibrils
- Fibrils reinforced by covalent cross-links between molecules
What are the properties of collagen?
- Extremely tough: resistant to normal shearing and tearing forces
- High tensile strength
- White when abundant, e.g., old scar, fresh tendons
- LM appearance: acidophilic (pink) fibres and fibre bundles
What does the type of collagen depend on?
Amino acid sequence of tropocollagen varies and hence the amount of polymerisation varies.
What is the structure of collagen type I?
Fibrils, fibres and bundles
Where is collagen type I found?
Most CT has collagen type I, e.g., dermis, tendons, ligaments, bone, dentin
What is the function of collagen type I?
Provides resistance to stress and tension; enables flexibility (movement) within tissue.
What is the structure of collagen type II?
Fibrils only
Where is collagen type II found?
Cartilage
What is the function of collagen type II?
Provides resistance to pressure
What is the structure of collagen type III?
Fibrils and fibres
Where is collagen type III found?
Reticular fibres, cellular organs
What is the function of collagen type III?
Provides delicate flexible framework
What is the structure of collagen type IV?
Network sheet
Where is collagen type IV found?
Basal lamina
What is the function of collagen type IV?
Support of delicate structures, filtration
What vitamin deficiency can inhibit collagen production?
Vitamin C
How does a vitamin C deficiency cause scurvy?
Collagen has high levels of proline and lysine amino acids that undergo post-translational modification in RER to hydroxyproline and hydroxylysine.
vitamin C needed for activation of enzymes to modify proline and lysine to hydroxyproline and hydroxylysine.
Lack of vitamin C causes scurvy where there is a reduced amount of collagen that is also less stable
Tissues that have high turnover of collagen (periodontal ligaments) are severely affected, causing loosening of teeth.
Describe the properties of reticular fibres.
- Form a flexible delicate support for cellular organs, e.g., spleen, bone, marrow, lymph nodes
- Special dyes needed to show reticular fibres clearly in LM
- Form an additional layer; reticular lamina below some basal laminae
Describe the general properties of elastic fibres?
- Elasticity
- Taut (i.e., straight and tight) in tissues
- Branch
- Thinnest fibres
Describe the distribution of elastic fibres.
- Large (elastic) arteries, e.g., aorta: passive stretch and recoil, which propels blood onwards and acts as a pressure
- Skin
- Lungs
- Passive stretch and recoil
Describe the composition of elastic fibres.
- Elastin molecules are cross-linked with each other
- When relaxed: random coiled structure
- When stretched: elongated
What is the composition of AGS.
- Carbohydrate and protein components: these complex together
- Glycoproteins: globular protein molecules to which branched chains of monosaccharides are covalently attached, bind components together, influence their interactions
- Proteoglycans: protein core with up to 200 glycosaminoglycans (GAGs, strong negative charge), which attract water to form solvation water