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Exp Cell Res. 1997 Oct 10;236(1):341-5.

Cleavage of beta 4 integrin by matrilysin.

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Department of Pathology, University of Arizona, Tucson 85724, USA.


Overexpression of the matrix metalloproteinase matrilysin and the absence of beta 4 integrin are two features characteristic of human prostate carcinoma. In the following study we demonstrate that the beta 4 integrin, but not the alpha 6 or beta 1 integrin subunits, is cleaved by matrilysin in vitro. A specific fragment of 90 kDa is generated using matrilysin, which is not observed with other proteases. Two putative cleavage sites for matrilysin within the extracellular domain of the beta 4 integrin at residues 107 (isoleucine, prior to the ligand-binding region) and 417 (leucine, prior to cysteine-rich region) are identified by sequence comparisons with known matrilysin substrates. The selective cleavage of the beta 4 integrin by matrilysin may partly explain the loss of beta 4 integrin expression in invasive prostate carcinoma.

[Indexed for MEDLINE]

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