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

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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; Niland, Stephan; Mörgelin, Matthias; Grifka, Joachim; Graessel, Susanne.

I: Journal of Biological Chemistry, Vol. 281, Nr. 35, 2006, s. 25745-25756.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Harvard

Eble, JA, Kassner, A, Niland, S, Mörgelin, M, Grifka, J & Graessel, S 2006, 'Collagen XVI harbors an integrin alpha 1 beta 1 recognition site in its C-terminal domains', Journal of Biological Chemistry, vol. 281, nr. 35, s. 25745-25756. https://doi.org/10.1074/jbc.M509942200

APA

Eble, J. A., Kassner, A., Niland, S., Mörgelin, M., Grifka, J., & Graessel, S. (2006). Collagen XVI harbors an integrin alpha 1 beta 1 recognition site in its C-terminal domains. Journal of Biological Chemistry, 281(35), 25745-25756. https://doi.org/10.1074/jbc.M509942200

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MLA

Vancouver

Author

Eble, Johannes A. ; Kassner, Anja ; Niland, Stephan ; Mörgelin, Matthias ; Grifka, Joachim ; Graessel, Susanne. / Collagen XVI harbors an integrin alpha 1 beta 1 recognition site in its C-terminal domains. I: Journal of Biological Chemistry. 2006 ; Vol. 281, Nr. 35. s. 25745-25756.

RIS

TY - JOUR

T1 - Collagen XVI harbors an integrin alpha 1 beta 1 recognition site in its C-terminal domains

AU - Eble, Johannes A.

AU - Kassner, Anja

AU - Niland, Stephan

AU - Mörgelin, Matthias

AU - Grifka, Joachim

AU - Graessel, Susanne

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151), Division of Infection Medicine (BMC) (013024020)

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M509942200

DO - 10.1074/jbc.M509942200

M3 - Article

C2 - 16754661

VL - 281

SP - 25745

EP - 25756

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 35

ER -