Lecture 24 - Interactions Between Cells and Their Environment Flashcards
def: a collection of structurally similar cells that cooperate tp perform a specific function
tissue
where did all the proteins outside a cell originally come from?
inside the cell
what are the 3 roles of the ECM?
- helps determine cell shape
- provides physical support for cells
- plays a regulatory role in cell signalling
what are the 3 types of extracellular matrix?
- bone
- cartilage
- connective tissue
def: hard calcified ECM that contains a small number of interspersed cells
bone
def: cells are imbedded in a flexible ECM rich in proteoglycans
cartilage
def: gelatinous ECM surrounding glands and blood vessels
connective tissue
def: structural proteins that provide strength and flexibility
collagens/elastins
def: components of hydrated matrix
proteoglycans
def: adhesive/connective glycoproteins that allow cells to attach to the ECM
fibronectin/laminins
what is the most abundant protein in the human body ?
family of closely related collagens, which form fibres with high tensile strength
collagen is secreted by several types of cells in connective tissues including __________-
fibroblasts
def: mutations in collagen resulting in the excessive looseness of skin and joints
ehlers-danos
def: a temporary collagen disease, because vitamin C is a co-factor in collagen synthesis
scurvy
all collagens occur as a ________, with rigid triple helix of intertwined polypeptides, _______ chains
trimer, alpha
collagens are very rich in:
glycine, proline and lysine
no vitamin C results in what in terms of collagen?
no hydroxyls can be added which means weaker interactions
def: three alpha chains assemble to form a triple helix, with short non-helical sequences at both ends
procollagen
once procollagen is secreted out of the cell, what cleaves it and removes it from both ends of the molecule?
procollagen peptidase
collagen has tensile strength but not enough for some types of tissue, in these cases elasticity is provided by ________
elastins
def: rich in glycine and proline, molecules are cross-linked by covalent bonds between lysine residues
elastins
with time, what happens to elastins?
they’re lost from tissues and skin will wrinkle and joints are less flexible
def: meshed gel-like network of collagen and elastin fibers
proteoglycans
def: large carbohydrates with repeating disaccharide units
glycosaminoglycans (GAGs)
what are the most common types of GAGs?
- chondroitin sulfate
- keratan sulfate
- hyaluronate
the presence of charged sulphate and carboxyl groups attract ______, which bind water, creating a hydrated and gelatinous matrix
cations
most GAGs in the ECM are ___________ _________ ____________ to form proteoglycans
covalently bound to proteins
def: reinforce direct links between the ECM and the plasma membrane
adhesive glycoproteins
what are the most common adhesive glycoproteins?
fibronectins and laminins
what is the structural composition of fibronectin?
consists of 2 very large polypeptide subunits linked near the C-terminus by disulfide bonds
what do the functional units of fibronectin bind?
- numerous components of the ECM
- bind receptors on the cell surface
def: family of proteins with three subunits linked together by disulfide bonds
laminins
what can bind to the binding sites on laminins?
- collagen
- proteoglycans
- other laminins
- receptors on cell surfaces
where are laminins mainly found?
in the basal lamina as a thin sheet of specialized extra cellular material
integrins integrate the _____ and ______ cellular environments
extra- and -intra
what do integrins do outside the cell?
bind to a diverse array of molecules
what do integrins do inside the cell?
interact with dozens of different proteins to influence cellular events