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Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands
Published on: May 30, 2017
60K gelatinase in involuting rat mammary gland is produced as a 90K proenzyme
1Department of Biochemistry, University of Kerala, Kariavattom, Trivandrum, India.
Abstract:
The matrix metalloproteinases appear to play a key role in mammary tissue remodeling during involution. By immunoprecipitation and immunoblot using antibodies against 60K gelatinase which appears during involution a 90K polypeptide has been identified as its inactive proenzyme in the early involuting rat mammary gland. 90K polypeptide was isolated from the second day involuting rat mammary gland by immunoaffinity chromatography. On proteolytic digestion, the inactive 90K polypeptide was converted to active gelatinase. Primary cultures of mammary epithelial cells secreted the 90K polypeptide. These results indicated that the 60K inducible MMP involved in mammary gland involution and remodeling is produced as a 90K proenzyme which is activated by proteolysis in the extracellular sites.

