The recognition sites of the integrins alpha1beta1 and alpha2beta1 within collagen IV are protected against gelatinase A attack in the native protein.

The Journal of Biological Chemistry
J A EbleK Kühn

Abstract

The susceptibility of three different solubilized forms of type IV collagen to gelatinase A cleavage and the concomitant effects on cell and integrin binding have been assessed. Dithiothreitol-solubilized Engelbreth-Holm Swarm (EHS) type IV collagen with disrupted intramolecular disulfide bonds in the CB3[IV] region was cleaved N-terminally to the CB3[IV] region into the two characteristic 100-300-nm fragments at 30 degrees C and was totally degraded at 37 degrees C. This was reflected in the partial or total loss of the alpha1beta1 and alpha2beta1 integrin binding sites within this region. The ability of gelatinase A to cleave EHS type IV collagen preparations with intact interchain disulfide bonds in CB3[IV] only occurred at higher temperatures. Furthermore, no effect on binding of cells or isolated integrins to the gelatinase-treated collagen could be detected after treatment at 37 degrees C. Dimeric collagen IV of human placenta with intact disulfide bonds in the CB3[IV] region was not degraded at all by gelatinase A at 37 degrees C.

References

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Citations

Jul 31, 2003·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·William Hornebeck, François Xavier Maquart
Oct 12, 1999·Matrix Biology : Journal of the International Society for Matrix Biology·A C WheatcroftG S Evans
Sep 20, 2006·Genes & Development·Kevin HotaryStephen J Weiss
Oct 12, 2002·Journal of Cell Science·Nathalie Ortega, Zena Werb
Jan 30, 2014·Cancers·Antonietta Rosella Farina, Andrew Reay Mackay
Oct 14, 2008·Trends in Cell Biology·R Grant Rowe, Stephen J Weiss
May 30, 1998·The Journal of Biological Chemistry·M W OlsonR Fridman
Nov 8, 2006·Protein Science : a Publication of the Protein Society·Susanna MonacoMassimo Coletta

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