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Activation of matrix metalloproteinase‐2 is correlated with invasiveness in thymic epithelial tumors
Author(s) -
Kondo Kazuya,
Kinoshita Hidetaka,
Ishikura Hisashi,
Miyoshi Takanori,
Hirose Toshiyuki,
Matsumori Yasumichi,
Monden Yasumasa
Publication year - 2001
Publication title -
journal of surgical oncology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.201
H-Index - 111
eISSN - 1096-9098
pISSN - 0022-4790
DOI - 10.1002/jso.1030
Subject(s) - thymoma , thymic carcinoma , pathology , matrix metalloproteinase , medicine , metastasis , zymography , cancer
Background and Objects Matrix degradation, which is a critical event in the process of tumor invasion and metastasis, is considered to be caused by the action of proteolytic enzymes. Methods We examined the gelatinolytic activity of matrix metalloproteinase (MMP)‐9, and the activity of active and inactive forms of MMP‐2 in five thymi, five noninvasive thymomas, eight invasive thymomas, and five thymic carcinomas by quantitative gelatinolytic zymography. Results The gelatinolytic activity of active MMP‐2 in five thymi was zero. The mean gelatinolytic activity of active MMP‐2 was 0.020 ± 0.015 in noninvasive thymoma, 0.084 ± 0.098 in invasive thymoma and 0.246 ± 0.194 in thymic carcinoma. The gelatinolytic activity of active MMP‐2 correlated with the invasiveness of thymic epithelial tumors (Spearman rank correlation: r ‐value = 0.532). The gelatinolytic activity of active MMP‐2 in three thymoma cases with microscopic capsular invasion was the same as that of noninvasive thymoma. When thymoma cases showing microscopic capsular invasion were classified into the “macroscopically noninvasive thymoma” group, the gelatinolytic activity of active MMP‐2 correlated with the invasiveness of thymic epithelial tumors (Spearman rank correlation: r ‐value = 0.621). Conclusions The gelatinolytic activity of active MMP‐2 significantly correlated with the invasiveness in thymic epithelial tumors. J. Surg. Oncol. 2001;76:169–175. © 2001 Wiley‐Liss, Inc.