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Identification, partial purification and characterization of high-molecular-weight gelatin-degrading metalloproteinases produced by a rat mammary carcinoma cell line

Abstract : BC1 rat mammary carcinoma cells were found to secrete a unique profile of metalloproteinases, distinguished by two gelatin-degrading metalloproteinases of Mr greater than 220.10(3) and Mr much greater than 220.10(3). These enzymes were each partially purified by gel-filtration chromatography, and inhibitor studies showed them to be metalloproteinases. Under conditions where denatured collagen types I, II, and V were completely degraded, native collagen types I, II, IV and V, fibronectin, fibrinogen, C1q, casein, and denatured transferrin were not degraded significantly by these enzymes. The relationship of these enzymes to other extracellular matrix-degrading metalloproteinases and their possible significance in tumour invasion and metastasis is discussed.
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https://hal-univ-rennes1.archives-ouvertes.fr/hal-02445620
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Submitted on : Monday, January 20, 2020 - 12:18:28 PM
Last modification on : Wednesday, August 19, 2020 - 11:17:59 AM

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Wahida Kihal-Talantikite, Séverine Deguen, Cindy Padilla, Muriel Siebert, Cécile Couchoud, et al.. Identification, partial purification and characterization of high-molecular-weight gelatin-degrading metalloproteinases produced by a rat mammary carcinoma cell line. Biochimica et Biophysica Acta (BBA) - General Subjects, Elsevier, 1989, 993 (1), pp.42-47. ⟨10.1016/0304-4165(89)90140-2⟩. ⟨hal-02445620⟩

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