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Enhanced acid protease activity of lysosomes from papillary thyroid carcinoma
Author(s) -
Sinadinović Jovan,
Cvejic Dubravka,
Savin Svetlana,
Mićić Jovan V.,
JanćićZguricas Marija
Publication year - 1989
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(19890315)63:6<1179::aid-cncr2820630623>3.0.co;2-q
Subject(s) - proteases , thyroid carcinoma , thyroid , protease , thyroglobulin , medicine , papillary carcinoma , carcinoma , endocrinology , in vitro , pathology , enzyme , biochemistry , biology
In vitro lysosomal acid protease activity was studied in human papillary thyroid carcinoma (n = 13). As a control, morphologically normal thyroid tissue from the same patient was used in each individual case of carcinoma. Although a marked variation may be observed between individual cases, each examined papillary thyroid carcinoma showed significantly greater activity of acid proteases, both per unit weight of wet thyroid tissue and per unit of lysosomal proteins, in comparison to the corresponding control (range, 24%‐248%). In conclusion, it is suggested that enhanced proteolytic activity of lysosomal acid proteases in papillary carcinoma is probably a result of disturbance in catabolic degradation of the thyroglobulin molecule in malignantly transformed thyroid tissue.