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Collagen XVI harbors an integrin alpha 1 beta 1 recognition site in its C-terminal domains

Eble, Johannes A.; Kassner, Anja LU ; Niland, Stephan; Mörgelin, Matthias LU ; Grifka, Joachim and Graessel, Susanne (2006) In Journal of Biological Chemistry 281(35). p.25745-25756
Abstract
Collagen XVI is integrated tissue-dependently into distinct fibrillar aggregates, such as D-banded cartilage fibrils and fibrillin-1-containing microfibrils. In skin, the distribution of collagen XVI overlaps that of the collagen-binding integrins alpha 1 beta 1 and alpha 2 beta 1. Basal layer keratinocytes express integrin alpha 2 beta 1, whereas integrin alpha 1 beta 1 occurs in smooth muscle cells surrounding blood vessels, in hair follicles, and on adipocytes. Cells bearing the integrins alpha 1 beta 1 and alpha 2 beta 1 attach and spread on recombinant collagen XVI. Furthermore, collagen XVI induces the recruitment of these integrins into focal adhesion plaques, a principal step in integrin signaling. Of potential physiological... (More)
Collagen XVI is integrated tissue-dependently into distinct fibrillar aggregates, such as D-banded cartilage fibrils and fibrillin-1-containing microfibrils. In skin, the distribution of collagen XVI overlaps that of the collagen-binding integrins alpha 1 beta 1 and alpha 2 beta 1. Basal layer keratinocytes express integrin alpha 2 beta 1, whereas integrin alpha 1 beta 1 occurs in smooth muscle cells surrounding blood vessels, in hair follicles, and on adipocytes. Cells bearing the integrins alpha 1 beta 1 and alpha 2 beta 1 attach and spread on recombinant collagen XVI. Furthermore, collagen XVI induces the recruitment of these integrins into focal adhesion plaques, a principal step in integrin signaling. Of potential physiological relevance, these integrin-collagen XVI interactions may connect cells with specialized fibrils, thus contributing to the organization of fibrillar and cellular components within connective tissues. In cell-free binding assays, collagen XVI is more avidly bound by alpha 1 beta 1 integrin than by alpha 2 beta 1 integrin. Both integrins interact with collagen XVI via the A domain of their alpha subunits. A tryptic collagen XVI fragment comprising the collagenous domains 1 - 3 is recognized by alpha 1 beta 1 integrin. Electron microscopy of complexes of alpha 1 beta 1 integrin with this tryptic collagen XVI fragment or with full-length collagen XVI revealed a unique alpha 1 beta 1 integrin-binding site within collagen XVI located close to its C-terminal end. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
281
issue
35
pages
25745 - 25756
publisher
ASBMB
external identifiers
  • wos:000240031300077
  • scopus:33748744382
ISSN
1083-351X
DOI
10.1074/jbc.M509942200
language
English
LU publication?
yes
id
e5bf470a-2cab-4854-b3f6-ea3309421bdb (old id 395100)
date added to LUP
2007-10-02 13:53:23
date last changed
2019-09-11 01:38:04
@article{e5bf470a-2cab-4854-b3f6-ea3309421bdb,
  abstract     = {Collagen XVI is integrated tissue-dependently into distinct fibrillar aggregates, such as D-banded cartilage fibrils and fibrillin-1-containing microfibrils. In skin, the distribution of collagen XVI overlaps that of the collagen-binding integrins alpha 1 beta 1 and alpha 2 beta 1. Basal layer keratinocytes express integrin alpha 2 beta 1, whereas integrin alpha 1 beta 1 occurs in smooth muscle cells surrounding blood vessels, in hair follicles, and on adipocytes. Cells bearing the integrins alpha 1 beta 1 and alpha 2 beta 1 attach and spread on recombinant collagen XVI. Furthermore, collagen XVI induces the recruitment of these integrins into focal adhesion plaques, a principal step in integrin signaling. Of potential physiological relevance, these integrin-collagen XVI interactions may connect cells with specialized fibrils, thus contributing to the organization of fibrillar and cellular components within connective tissues. In cell-free binding assays, collagen XVI is more avidly bound by alpha 1 beta 1 integrin than by alpha 2 beta 1 integrin. Both integrins interact with collagen XVI via the A domain of their alpha subunits. A tryptic collagen XVI fragment comprising the collagenous domains 1 - 3 is recognized by alpha 1 beta 1 integrin. Electron microscopy of complexes of alpha 1 beta 1 integrin with this tryptic collagen XVI fragment or with full-length collagen XVI revealed a unique alpha 1 beta 1 integrin-binding site within collagen XVI located close to its C-terminal end.},
  author       = {Eble, Johannes A. and Kassner, Anja and Niland, Stephan and Mörgelin, Matthias and Grifka, Joachim and Graessel, Susanne},
  issn         = {1083-351X},
  language     = {eng},
  number       = {35},
  pages        = {25745--25756},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Collagen XVI harbors an integrin alpha 1 beta 1 recognition site in its C-terminal domains},
  url          = {http://dx.doi.org/10.1074/jbc.M509942200},
  volume       = {281},
  year         = {2006},
}