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Untitled - D Ank Unlimited

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lamina propria 438 laminin receptor<br />

lamina propria<br />

The thin connective tissue layer that supports the epithelium<br />

of the gastrointestinal tract. The epithelium and lamina propria<br />

form the mucous membrane. The lamina propria may<br />

be the site of immunologic reactivity in the gastrointestinal<br />

tract, representing an area where lymphocytes, plasma cells,<br />

and mast cells congregate.<br />

laminin<br />

A relatively large (820-kDa) basement membrane glycoprotein<br />

composed of three polypeptide subunits. It belongs<br />

to the integrin receptor family, which includes a 400-kDa<br />

α heavy chain and two 200-kDa light chains designated β 1<br />

and β 2. By electron microscopy the molecule is arranged<br />

in the form of a cross. The domain structures of the α<br />

and β chains resemble one another. There are six primary<br />

domains. Domains I and II have repeat sequences forming<br />

α helices. Domains III and V are composed of cysteine-rich<br />

NH 3 +<br />

Collagen IB<br />

binding site<br />

β1 Chain<br />

(215kD)<br />

– OOC<br />

1<br />

NH 3 +<br />

Laminin.<br />

COO –<br />

α Chain<br />

(400kD)<br />

β2 Chain<br />

(205kD)<br />

COO –<br />

Heparan sulfate<br />

proteoglycan<br />

binding site<br />

NH 3 +<br />

Lamina propria.<br />

repeating sequences. The globular regions are composed<br />

of domains IV and VI. An additional short cysteine-rich<br />

α domain is located between the I and II domains in the<br />

β 1 chain. A relatively large globular segment is linked to<br />

the C terminal of domain I, designated the “foot” in the<br />

α chain. Five “toes” on the foot contain repeat sequences.<br />

Laminins have biological functions and characteristics that<br />

include facilitation of cellular adhesion and linkage to other<br />

basement membrane constituents such as collagen type IV,<br />

heparan, and glycosaminoglycans. Laminins also facilitate<br />

neurite regeneration, an activity associated with the foot<br />

of the molecule. Each form of laminin represents different<br />

gene products, although they possess a high degree of<br />

homology. S laminin describes a form found only in synaptic<br />

and nonmuscle basal lamina. Its is a single 190-kDa<br />

polypeptide (in reduced form) and its weight is >1000 kDa<br />

in the nonreduced form. It is associated with the development<br />

or stabilization of synapses and is homologous to the<br />

β 1 chain of laminin. Laminin facilitates cell attachment and<br />

migration, plays a role in differentiation and metastasis, and<br />

is produced by macrophages, endothelial cells, epithelial<br />

cells, and Schwann cells.<br />

laminin receptor<br />

A membrane protein composed of two disulfide bondlinked<br />

subunits, one relatively large and one relatively<br />

small. Its function appears to be the attachment of cells.<br />

It may share structural similarities with fibronectin and<br />

vitronectin, both of which are also integrins.<br />

Karl Landsteiner.

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