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Increased hyaluronidase levels in breast tumor metastases
Author(s) -
Bertrand Philippe,
Girard Nicole,
Duval Christian,
d'Anjou Joëlle,
Chauzy Claude,
Ménard JeanFrançois,
Delpech Bertrand
Publication year - 1997
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/(sici)1097-0215(19971104)73:3<327::aid-ijc4>3.0.co;2-1
Subject(s) - hyaluronidase , medicine , breast cancer , mammary gland , oncology , biology , cancer , enzyme , biochemistry
Hyaluronidase, a matrix‐degrading enzyme, was assayed in extracts from breast primary tumors and regional metastases using a pool of human sera as a standard. Optimal activities of tumor extracts and serum were found for concentrations of 0.15–0.20 M NaCl in pH 3.8–4.0 buffer. In evaluating contamination by serum due to vascular proliferation, we expressed our results as the ratio of the entire activity (mU/l extract) on serum albumin content of tumors (g/l). Median (interquartile range) activities were 9.02 (6.04–14.34) for primary tumors and 37.36 (24.06–99.63) mU/g albumin for metastases. The difference was significant. Zymographic analysis showed that 3 bands of activity were detected which corresponded to 68, 53 and 49 kDa for tumoral hyaluronidase. The same pattern was observed for cellular extracts of breast cancer cell line CAL51, demonstrating that hyaluronidase detected in tumor extracts had mainly a cellular origin. Our results suggest that hyaluronidase may be involved in the metastatic process. Int. J. Cancer 73:327–331, 1997. © 1997 Wiley‐Liss, Inc.