A1 Refereed original research article in a scientific journal
Collagen XXIII, Novel Ligand for Integrin alpha(2)beta(1) in the Epidermis
Authors: Veit G, Zwolanek D, Eckes B, Niland S, Kapyla J, Zweers MC, Ishada-Yamamoto A, Krieg T, Heino J, Eble JA, Koch M
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Publication year: 2011
Journal: Journal of Biological Chemistry
Journal name in source: JOURNAL OF BIOLOGICAL CHEMISTRY
Journal acronym: J BIOL CHEM
Number in series: 31
Volume: 286
Issue: 31
First page : 27804
Last page: 27813
Number of pages: 10
ISSN: 0021-9258
DOI: https://doi.org/10.1074/jbc.M111.220046
Abstract
Cellular receptors for collagens belong to the family of beta(1) integrins. In the epidermis, integrin alpha(2)beta(1) is the only collagen-binding integrin present. Its expression is restricted to basal keratinocytes with uniform distribution on the cell surface of those cells. Although alpha(2)beta(1) receptors localized at the basal surface interact with basement membrane proteins collagen IV and laminin 111 and 332, no interaction partners have been reported for these integrin molecules at the lateral and apical membranes of basal keratinocytes. Solid phase binding and surface plasmon resonance spectroscopy demonstrate that collagen XXIII, a member of the transmembrane collagens, directly interacts with integrin alpha(2)beta(1) in an ion-and conformation-dependent manner. The two proteins co-localize on the surface of basal keratinocytes. Furthermore, collagen XXIII is sufficient to induce adhesion and spreading of keratinocytes, a process that is significantly reduced in the absence of functional integrin alpha(2)beta(1).
Cellular receptors for collagens belong to the family of beta(1) integrins. In the epidermis, integrin alpha(2)beta(1) is the only collagen-binding integrin present. Its expression is restricted to basal keratinocytes with uniform distribution on the cell surface of those cells. Although alpha(2)beta(1) receptors localized at the basal surface interact with basement membrane proteins collagen IV and laminin 111 and 332, no interaction partners have been reported for these integrin molecules at the lateral and apical membranes of basal keratinocytes. Solid phase binding and surface plasmon resonance spectroscopy demonstrate that collagen XXIII, a member of the transmembrane collagens, directly interacts with integrin alpha(2)beta(1) in an ion-and conformation-dependent manner. The two proteins co-localize on the surface of basal keratinocytes. Furthermore, collagen XXIII is sufficient to induce adhesion and spreading of keratinocytes, a process that is significantly reduced in the absence of functional integrin alpha(2)beta(1).
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