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Laminins.

Durbeej-Hjalt, Madeleine LU (2010) In Cell and Tissue Research1974-01-01+01:00 339. p.259-268
Abstract
Laminins are cell adhesion molecules that comprise a family of glycoproteins found predominantly in basement membranes, which are the thin sheets of extracellular matrix that underlie epithelial and endothelial cells and surround muscle cells, Schwann cells, and fat cells. Many laminins self-assemble to form networks that remain in close association with cells through interactions with cell surface receptors. Laminins are vital for many physiological functions. They are essential for early embryonic development and organogenesis and have crucial functions in several tissues including muscle, nerve, skin, kidney, lung, and the vasculature. A great wealth of data on laminins is available, and an in-depth description is not attempted here. In... (More)
Laminins are cell adhesion molecules that comprise a family of glycoproteins found predominantly in basement membranes, which are the thin sheets of extracellular matrix that underlie epithelial and endothelial cells and surround muscle cells, Schwann cells, and fat cells. Many laminins self-assemble to form networks that remain in close association with cells through interactions with cell surface receptors. Laminins are vital for many physiological functions. They are essential for early embryonic development and organogenesis and have crucial functions in several tissues including muscle, nerve, skin, kidney, lung, and the vasculature. A great wealth of data on laminins is available, and an in-depth description is not attempted here. In this review, I will instead provide a snapshot of laminin structure, tissue distribution, and interactions with other matrix molecules and receptors and briefly describe laminin mutations in mice and humans. Several illuminating and timely reviews are cited that can be consulted for references to original articles and more detailed information concerning laminins. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cell and Tissue Research1974-01-01+01:00
volume
339
pages
259 - 268
publisher
Springer
external identifiers
  • wos:000273953300021
  • pmid:19693542
  • scopus:72449128021
ISSN
1432-0878
DOI
10.1007/s00441-009-0838-2
language
English
LU publication?
yes
id
724009bb-0c2c-4f55-a7b4-da5065b13a1b (old id 1469574)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/19693542?dopt=Abstract
date added to LUP
2009-09-04 14:26:00
date last changed
2018-11-18 04:31:26
@article{724009bb-0c2c-4f55-a7b4-da5065b13a1b,
  abstract     = {Laminins are cell adhesion molecules that comprise a family of glycoproteins found predominantly in basement membranes, which are the thin sheets of extracellular matrix that underlie epithelial and endothelial cells and surround muscle cells, Schwann cells, and fat cells. Many laminins self-assemble to form networks that remain in close association with cells through interactions with cell surface receptors. Laminins are vital for many physiological functions. They are essential for early embryonic development and organogenesis and have crucial functions in several tissues including muscle, nerve, skin, kidney, lung, and the vasculature. A great wealth of data on laminins is available, and an in-depth description is not attempted here. In this review, I will instead provide a snapshot of laminin structure, tissue distribution, and interactions with other matrix molecules and receptors and briefly describe laminin mutations in mice and humans. Several illuminating and timely reviews are cited that can be consulted for references to original articles and more detailed information concerning laminins.},
  author       = {Durbeej-Hjalt, Madeleine},
  issn         = {1432-0878},
  language     = {eng},
  pages        = {259--268},
  publisher    = {Springer},
  series       = {Cell and Tissue Research1974-01-01+01:00},
  title        = {Laminins.},
  url          = {http://dx.doi.org/10.1007/s00441-009-0838-2},
  volume       = {339},
  year         = {2010},
}