Extracellular Matrix and Adhesion Flashcards
Functions of ECM (6)
Scaffolding Regulates Cell Survival (Integrins) Differentiation Migration (GAGs) Proliferation Shape
Four major components of ECM
Glucosaminoglycans
Proteoglycans
Fibrous Proteins: Collagen and Elastin
Multidomain Adaptor proteins: Fibronectin & Laminin
Glucosaminoglycans
repeated disaccharides that can attach to serine residues through a tetrasaccharide linker.
Acetylation/Sulfation determines type of GAG
Cross-linking helps with ECM structure
Can bind signals (usually inactive when bound) such as selectins for leukocyte extravasation
Collagen
Most abundant protein in body, main ECM component
Different collagens have different properties
Coiled trimer = pro-collagen, termini removed = tropo collagen
Provide scaffolding
Fibronetin/Laminin
Signaling molecules in ECM, multimers that change ECM properties
Fibronectin: dimer formed by C terminus disulphide bridge. Self association and collagen, cell, and heparin binding domains to maximize cross linking
Laminin: Heterotetramer w/ multiple cross-linking chains/domains
MMPs
Actin protrusions at leading edge coupled with myosin provides movement.
MMPs are zinc-dependent, inactive w/ C terminus attached. Secreted into ECM where C terminus is cleaved and they degrade ECM and activate signals associated with GAGs
Adhesion and Cell Survival
Cells require binding to ECM via integrins in order to survive.
Integrins
transmembrane heterodimers of alpha and beta subunits that recognize specific ECM proteins
Beta unit binds actin intracellularly via adaptor proteins, important in cell motility.
Promote survival and suppress apoptosis when bound to ECM, opposite when not bound to ECM
Cadherins
calcium dependent homodimers that create junctions between cells.
Bind actin intracellularly via beta catenin
CAMs and signaling
Rho associated with CAMs, Beta catenin with cadherins