4.1 Article

Laminins in basement membrane assembly

Journal

CELL ADHESION & MIGRATION
Volume 7, Issue 1, Pages 56-63

Publisher

TAYLOR & FRANCIS INC
DOI: 10.4161/cam.21831

Keywords

laminin; collagen IV; nidogen; agrin; perlecan; dystroglycan

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Funding

  1. Wellcome Trust [083942/Z/07/Z]
  2. National Institutes of Health [R37-DK36425]
  3. NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R37DK036425, R01DK036425] Funding Source: NIH RePORTER

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The heterotrimeric laminins are a defining component of all basement membranes and self-assemble into a cell-associated network. The three short arms of the cross-shaped laminin molecule form the network nodes, with a strict requirement for one alpha, one beta and one gamma arm. The globular domain at the end of the long arm binds to cellular receptors, including integrins, alpha-dystroglycan, heparan sulfates and sulfated glycolipids. Collateral anchorage of the laminin network is provided by the proteoglycans perlecan and agrin. A second network is then formed by type IV collagen, which interacts with the laminin network through the heparan sulfate chains of perlecan and agrin and additional linkage by nidogen. This maturation of basement membranes becomes essential at later stages of embryo development.

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