Biology Reference
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Fig. 1. Structure and functions of laminin-1 and it's proteolytic derivatives.
Laminins are heterotrimeric glycoproteins composed of
chains joined in a
coiled-coil to form a cruciform-shaped molecule. The carboxyl-terminal G (globular)
domain of the
α, β,
and
γ
chain extends from the coiled-coil. Roman numerals indicate domains
that are found within each subunit chain. Laminin-1 can support integrin-mediated
adhesion of cells (
α
α
1
β
1,
α
2
β
1,
α
6
β
1,
α
6
β
4,
α
7
β
1), undergo self-polymerization
(polymer), and bind entactin/nidogen (En/Nd),
DG), and heparin.
Note that several domains have overlapping activities. Recombinant G domain (rG)
and recombinant G domain with proximal
α
-dystroglycan (
α
chain coiled-coil (rAiG) have been
purified and shown to have activities similar to those found in native laminin-1 puri-
fied from tissue (5 , 6 , 8) .
α
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