ECM Flashcards
Functions of ECM
Structure, Defense and protection, Nutrition, Diffusion of gases, molecules and ions, Cell growth and survival, Cell migration, Lubrication
2 Constituents of ECM
Group Substance and Fibers
Group Substance
GAGs, proteoglycans, water, adhesive glycoproteins
Fibers
collagen, reticular (type III) collagen, elastic
Tissue repair with ECM
very vascular, edema, loose ECM
How does ECM drive the cell cycle
Focal adhesions of cell to ECM regulate cell division, growth and survival
Excessive accumulation of GAGs leads to what
increase in water
Structure of proteoglycans
Core protein is the backbone. Core protein is attached to link protein on hyaluronan. GAGs attach to the core protein and look like bristles
Syndecan
transmembrane proteoglycan. Co-receptor for FGF
What happens when you inactivate gene for perlecan
results in defective skeletal development
3 binding domains on multiadhesive glycoprotein
- Cell adhesion molecule (CAM)
- Collagen fibers
- Proteoglycans
Binding domains of fibronectin
integrins, collagen, heparin, heparan fulfate, hyaluronic acid
Location of fibronectin
connective tissue, blood plasma, embryonic tissue
Binding domains of laminin
integrins, heparan sulfate, collagen IV, entractin
Location of laminin
basal lamina
Binding domains of entactin
laminin, integrins, type IV collagen
location of entactin
basal lamina
binding domains of tenscin
syndecans and fibrorecton
Location of tenascin
embryonic tissue
Binding domains of chondronectin
Type II collagen, chondroitin sulfates, hyaluronic acid, integrins of chondrocytes
Location of chondronectin
cartilage
Binding domains of Ostonectin
Type I collagen, proteoglycans and integrins of bone cells (osteocytes, osteoblasts)
Location of osteonectin
bone
What do antibodies to fibronectin do
Block branching morphogensis in developing mouse salivary glands
Hydroxyproline
Used to calculate concentration of collagen
Collagen can be turned over through what processes
Proteolytic degradation, Phagocytic degradation
Function of Type I collagen
resistance to tension
Function of Type II collagen
resistance to pressure
Function of Type III collagen
maintain structure in expansion organs
Function of Type IV collagen
support of delicate structures and filitration
Function of Type V collagen
anchors basal lamina to lamina reticularis
Tissue Distribution of Type I collagen
dermis, tendon, bone, dentin, cementum, fibrocartilage, organ capsules
Tissue Distribution of Type II collagen
hyaline and elastic cartilage
Tissue Distribution of Type III collagen
spleen, liver, lymph nodes, smooth muscle, skin, lung
Tissue distribution of Type IV collagen
basal lamina
Tissue distribution of Type V collagen
dermis
Synthesizing cells of Type I collagen
fibroblasts, odontoblasts, cementoblasts, osteoblasts, chordroblasts
Synthesizing cells of Type II collagen
chondroblasts
Synthesizing cells of Type III collagen
smooth muscle cells, fibroblasts, reitcular cells
Synthesizing cells of Type IV collagen
endothial cells, epithial cells, Schwann cells, smooth muscle cells
Synthesizing cells of Type V collagen
epidermal cells
Organization of Type I collagen
fibril-forming collagen leading to formation of fibers
Organization of Type II collagen
fibril-forming collagen
Organization of Type III collagen
fibril-forming collagen leading to formation of fibers
Organization of Type IV collagen
network-forming collagen
Organization of Type V collagen
anchoring collagen
Composition of elastic fiber
proelastin, microfibril-associated glycoprotein, fibrillin
Ehlers-Danlos Type IV
Caused by mutation in COLI3A1 gene encoding type III collagen. Leads to varicose veins, aortic rupture, intenstinal rupture
Ehlers-Danlos Type VI
Caused by defective hydroxylation of lysine thereby destabilizing the strenth of collagen. Leads to hyperelasticity of skin, rupture of eyeball
Ehlers-Danlos Type VII
Caused by mutations in the COL1A1 and COL1A2 genes encoding type I collagen. Leads to joint dislocation and hypermobility of joints
Scurvy
Caused by tropocollagen molecules that cannot aggregate into fibrils due to decreased hydroxylation of proline caused by deficency in vitamin C. Results in gum ulceration and hemorrhages
Osteogensis imperfecta
Caused by mutations in COL1A1 leading to reduction in synthesis of type I collagen. Leads to spontaneous fractures, cardiac insufficiency
Strickler syndrome
Caused by mutation in COL2A1 gene encoding type II collagen. Leads to myopia, hypoplasia of mandible, arthritis
Marfan Syndrome
Caused by mutation of fibrillin I gene located on chromosome 15 - defective synthesis of elastic fibers. Leads to aortic aneurysm or rupture, myopia, detached lens, and skeletal defects
Lamina lucida contains
laminin, entractin, integrins, dystoglycans
Lamina densa contains
type IV collagen, fibrorectin, perlecan
Lamina fibroreticularis contains
fibrorectin, types I and III collagen
Collagen VII
anchors lamina densa and lamina fibrorecularis