Connective tissue (general) Flashcards
Classifications of CT
- PROPER CT: either loose or dense (depdnding on size of collagen fibers)
- SUPPORTIVE CT: either bone or cartilage (contain viscous, specialised ECM for their mechanical properties)
- SPECIAL CT: either adipose tissue or blood/lymphoid
General functions of CT (6)
- connects tissues for functional and structural integration
- acts as a medium for diffusion and material exchange
- trophic functions
- protects delicate organs
- defense function
- repares tissue damage (scar formation)
General overview of CT proper composition
CELLS:
- Resident cells (formed in CT)
- Migrating cells (formed in other tissue and then migrate into CT)
ECM:
- Fibrillary components (collagen, reticular and elastic fibres)
- Ground substance (H20, glycoproteins, GAGs)
Characteristics of loose proper CT
LOOSE:
-contains less fibers than ground substance
-thin and sparse collagen
-important in the difussion of O2/nutrients/CO2/ waste into and out of blood vessels
-primarily located beneath epithelia
Classificatiosn and characteristics of dense proper CT
DENSE IRREGULAR:
-contains more fibers than ground substance
-contains mainly fibroblasts in terms of cellular components
-abundant collagen arranged in bundles of random orientation
-provides strength
-located in the dermis (in the reticular layer) AND submucosa of hollow organs –> both provide resistance to stretching forces
DENSE REGULAR:
-more fibers than ground substance
-collagen fibers arranged in parallel array and densely packed
-main component of tendons/ligaments.
!! CONTAIN COLLAGEN TYPE ONE
Structure of tendons
-type of dense regular CT
-cord like structures
-attach muscle to bone
-parallel arrangement of collagen fibres
-between fibers are TENDINOCYTES (fibroblasts)
-tendon surrounded by the epitendineum
!!! tendinocytes apper as rows of basophilic nuclei
Collagen levels of organisation of he polymer
- alpha chains (rich in amino acid residues, one in each three chains is glycine, and there is hydroxyproline and proline)
- Tropocollagen: 3 alpha chains wrapped in a helical chain
- Microfibrils: stragerred molecules of tropocollagen joined with covalent cross links
- Fibrils: bundles of microfibrils
- Collagen Fiber: bundles of fibrils
What is collagen periodicity?
Gaps created due to stagerred arrangement of tropocollagen molecules where electrons can pass through in a TEM. Creates alternating electron dense vs light regions
1 Gap = approx 68nm
Collagen synthesis process (7 steps)
INTRACELLULAR PHASE:
1. Protein synthesis of alpha chains on ribosomes of RER (since the protein is secretory)
2. Hydroxylation of lysine in the RER (allows formation of cross links later)
3. Glycosylation starting in RER and completed in Golgi
4. Procollagen is formed (triple helix)
5. Secretion of procollagen via trans Golgi out of cell
EXTRACELLULAR PHASE:
- Cutting of the procollagen globular domain to obtain tropocollagen
- Self assembly of tropocollagen into microfibrils and fibrils into fibers
Collagen maturation definition
-The formation of covalent bonds between tropocollagen molecules when they stagger to form a microfibril
-Prevents degradation of collagen and increases strength
!!! This can only happen if there has been hydroxylation of lysine residues in the RER during collagen synthesis
Overview of the types of collagen (we need to know)
TYPE 1: found in CT of bone, tendon, skin, ligaments, dentin,organ capsules -> provied resistance
TYPE 2: found in Cartilage (hyaline/fibro/elastic), intervertebral discs -> provides resistance
TYPE 3: found in loose CT (organ linings), skin, muscle, blood vessels -> forms reticular fibres to provide scaffolding
TYPE 4: forms basal lamina of ET -> provides support and aids attachment between ET and CT
What are collagen crimps?
-Wavey pattern of arrangement of collagen fibres in tendons and ligaments
Collagen Turnover definition
Dynamic control of the amount of collagen present in each cell by keeping the ratio of collagen synthesis: degradation at an equilibrium
!! all cells have a fixed amount of collagen but not all cells have the SAME fixed amount of collagen
Collagen Turnover process
- Cell receives stimulating factors like growth factors/cytokines
- Release of inactive pro MMPs (matrix metalloproteinases)
- Activation of MMPs via enzymatic cleavage
- Promotes degradation of the ECM
- TIMPs (Tissue inhibitor of metalloproteinase) which block the activation and action of MMPs –> these allow the rate of ECM degradation to be decreased if it gets too high
What determines the classification of type of collagen?
Depends on the specific amino acids of the alpha chain subunits present
what are MMPs?
Matrix metalloproteins: ECM enzymes that degrade collagen
! most important in collagen type 1 cleavage is MMP1
Pathologies associated to faulty collagen turnover (dude to dynamic imbalance)
- EHLERS-DANLOS SYNDROME: causes hyperelasticity of the skin (due to faulty lysyl hydroxylase which prevents cross links from forming due to no hydroxylation)
- OSTEOGENESIS IMPERFECTA: fragile bones due to inability to produce normal Collagen type 1
Reticular fibers structure
-made of collagen type 3
-fibrils are smaller and thinner than collagen 1
-branch out into mesh like networks
-stil exhibit 68nm periodism
-not as efficient in resisting mechanical stress
-play a scaffolding role due to its mesh network
-located in boundary between ET and CT (loose)