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

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title = "Collagen XVI harbors an integrin alpha 1 beta 1 recognition site in its C-terminal domains",
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 Anja Kassner and Stephan Niland and Matthias M{\"o}rgelin and Joachim Grifka and Susanne Graessel",
note = "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)",
year = "2006",
doi = "10.1074/jbc.M509942200",
language = "English",
volume = "281",
pages = "25745--25756",
journal = "Journal of Biological Chemistry",
issn = "1083-351X",
publisher = "ASBMB",
number = "35",