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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
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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. |
format | Online Article Text |
id | pubmed-3544787 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT hohenestererhard lamininsinbasementmembraneassembly AT yurchencopeterd lamininsinbasementmembraneassembly |