Effects of collagenase-cleavage of type I collagen on α2β1 integrin-mediated cell adhesion

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Abstract
In this paper we show that collagenase-3 cleavage of type I collagen has a marked effect on α2β1 integrin-mediated interactions with the collagen fragments generated. Isolated α2β1 integrin and α2 integrin A-domain were found to bind to both native collagen and native fragment and, to a lesser degree, native fragment. Whole integrin and integrin A-domain binding were lost after heat denaturation of the collagen fragments. At physiological temperature, cell adhesion to triple-helical fragment via α2β1 integrin was still possible; however, no α2β1 integrin-mediated adhesion to the fragment was observed. Unwinding of the collagen fragment triple helices by heating to physiological temperatures prior to adsorption to plastic tissue culture plates resulted in total abrogation of HT1080 cell attachment to either fragment. These results provide significant evidence in support of a role for matrixmetalloproteinase cleavage of the extracellular matrix in modifying cell-matrix interactions.