NDLI: Walker 256 cancer cells secrete tissue inhibitor of metalloproteinase-free metalloproteinase-9

Content Provider	Springer Nature Link
Author	Pavlaki, Maria Gianpoulou, Eleftheria Niarakis, Anna Ravazoula, Panagiota Aletras, Alexios J.
Copyright Year	2009
Abstract	Walker 256 (W256) cancer cells, developed as ascites in rats, in response to endogenous unidentified stimuli, secrete a gelatinase of apparent molecular mass of 94 kDa, immunologically homologous to the zymogen of matrix metalloproteinase-9 (proMMP-9). After treatment with the activating agent 4-aminophenylmercuric acetate (APMA), affinity-purified W256 gelatinase is converted to a final processed form of 66 kDa in a similar fashion to TIMP-free human proMMP-9. It is demonstrated that although being capable of binding TIMP-1, W256 proMMP-9 is secreted from W256 cells in TIMP-free forms (monomers or oligomers). Moreover, using biochemical and immunological methods, it is established that the W256 cells do not express or secrete TIMP-1 protein, although RT-PCR analysis indicated low-level TIMP-1 mRNA expression. W256 cancer cells displayed high metastatic ability in rats that may be attributed in part to secretion of TIMP-free proMMP-9.
Starting Page	189
Ending Page	199
Page Count	11
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	328
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Springer US
Publisher Date	2009-03-29
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Matrix Metalloproteinases (MMPs) Matrix metalloproteinase-9 (MMP-9) Gelatinase B Tissue inhibitor of metalloproteinase-1 (TIMP-1) Walker 256 carcinosarcoma TIMP-1-free MMP-9 Cardiology Oncology Medical Biochemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

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