Premium
Distribution of collagenase and tissue inhibitor of metalloproteinases (TIMP) in colorectal tumours
Author(s) -
Hewitt Robert E.,
Leach Iain H.,
Powe Desmond G.,
Clark Ian M.,
Cawston Tim E.,
Turner David R.
Publication year - 1991
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910490507
Subject(s) - collagenase , matrix metalloproteinase , interstitial collagenase , distribution (mathematics) , medicine , pathology , tissue inhibitor of metalloproteinase , colorectal cancer , oncology , biology , enzyme , cancer , biochemistry , mathematics , mathematical analysis
Increased collagenase activity in colorectal carcinomas has recently been shown to be associated with increased malignant potential. To determine the tissue distribution of collagenase and its specific inhibitor, tissue inhibitor of metalloproteinases (TIMP), we carried out an immunohistochemical study on colorectal carcinomas (n = 20), adenomas (n = 7) and normal mucosa (n = 6). We found increased staining for collagenase in the connective tissue stroma of carcinomas, as compared with adenomas and normal mucosa. Little evidence of epithelial cell staining for collagenase was seen in any tissue. In carcinomas, both stromal fibroblasts and collagen fibres stained strongly and stromal staining was strongest close to neoplastic glands. Vascular staining was more prominent in neoplastic than normal tissues, perhaps reflecting the increased proteolytic activity during tumour angiogenesis. The pattern of TIMP immunostaining was similar to that of collagenase, although basement membrane staining for TIMP was generally more intense. Another difference was that, unlike TIMP, staining for collagenase was often increased at the invasive edge of carcinomas, perhaps reflecting increased collagenase activity at this location.