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Proteinases and sialyltransferase in human breast tumors

✍ Scribed by Joseph Abecassis; Régine Collard; Michel Eber; Jean Pusel; Jean P. Fricker; GÉRard Methlin

Publisher
John Wiley and Sons
Year
1984
Tongue
French
Weight
457 KB
Volume
33
Category
Article
ISSN
0020-7136

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✦ Synopsis

Abstract

Proteolytic and sialyltransferase activities were determined in extracts of 65 human primary breast tumors, 6 lymph node metastases, 6 fibroadenomas and 27 normal tissues. Using proteins and synthetic selective substrates, we observed the presence of collagen‐peptidases, plasminogen activator, cathepsin‐B and cathepsin‐D‐like enzymes, and sialyltransferase. No active or trypsin‐activatable type‐IV collagenase activity was detected. Although individual variations between tumors were large, proteinase and sialyltransferase contents were significantly elevated in malignant breast tissues. Enzyme activities were found to be related to the epithelial volume of the tumor. No significant correlation was found between the proteinase or sialyltransferase activities and the degree of differentiation of the tumor cells, or the degree to which tumors had metastasized to regional lymph nodes. Since large variations of enzyme levels apparently reflect the heterogeneity of epithelial cell densities in tumor samples, proteolytic or sialyltransferase activities cannot therefore be used as a measure of quantitative evaluation of invasive properties in breast cancer.

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