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Cell-interactive and architecture-forming functions are
associated with the short arms of basement membrane laminin-1. To map
and characterize these functions, we expressed recombinant mouse
laminin-1
Volume 270,
Number 16,
Issue of April 21, pp. 9398-9406, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
1
1 Integrin-recognition
Sites within the
-Chain Short Arm of Laminin-1
-chain extending from the N terminus through one third
of domain IIIb. This dumbbell-shaped glycoprotein (r1(VI-IVb)`),
secreted by mammalian cells, was found to possess three activities. 1)
Laminin polymerization was quantitatively inhibited by recombinant
protein, supporting an -chain role for a three-short arm
interaction model of laminin self-assembly. 2) r1(VI-IVb)` bound
to heparin, and the activity was localized to a subfragment
corresponding to domain VI by I-heparin blotting. 3) PC12
rat pheochromocytoma cells adhered to, and rapidly extended branching
neurites on, r
1(VI-IVb)`, with adhesion inhibited by 1 and
1 integrin chain-specific antibodies. The ability of anti-laminin
antibody to block PC12 cell adhesion to laminin was selectively
prevented by absorption with r1(VI-IVb)` or -chain domain VI
fragment. This active integrin-recognition site could furthermore be
distinguished from a second cryptic 11-binding site exposed
by heat treatment of fragment P1`, a short arm fragment lacking
globules. Thus, a polymer-forming, a heparin-binding, and the active
11 integrin-recognition site are all clustered at the end of
the -chain short arm, the latter two resident solely in domain VI.
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