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Laminins in basement membrane assembly

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 α, one β and one γ arm. The globular domain at the end...

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Detalles Bibliográficos
Autores principales: Hohenester, Erhard, Yurchenco, Peter D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3544787/
https://www.ncbi.nlm.nih.gov/pubmed/23076216
http://dx.doi.org/10.4161/cam.21831
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author Hohenester, Erhard
Yurchenco, Peter D.
author_facet Hohenester, Erhard
Yurchenco, Peter D.
author_sort Hohenester, Erhard
collection PubMed
description 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 α, one β and one γ arm. The globular domain at the end of the long arm binds to cellular receptors, including integrins, α-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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spelling pubmed-35447872013-01-18 Laminins in basement membrane assembly Hohenester, Erhard Yurchenco, Peter D. Cell Adh Migr Review 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 α, one β and one γ arm. The globular domain at the end of the long arm binds to cellular receptors, including integrins, α-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. Landes Bioscience 2013-01-01 /pmc/articles/PMC3544787/ /pubmed/23076216 http://dx.doi.org/10.4161/cam.21831 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Review
Hohenester, Erhard
Yurchenco, Peter D.
Laminins in basement membrane assembly
title Laminins in basement membrane assembly
title_full Laminins in basement membrane assembly
title_fullStr Laminins in basement membrane assembly
title_full_unstemmed Laminins in basement membrane assembly
title_short Laminins in basement membrane assembly
title_sort laminins in basement membrane assembly
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3544787/
https://www.ncbi.nlm.nih.gov/pubmed/23076216
http://dx.doi.org/10.4161/cam.21831
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