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			PubMed Journals: Eur J Biochem

  Source:		PMID: 9578462


    		Eur J Biochem. 1998 Apr 1;253(1):67-75.
     
			Activation of the precursor of human stromelysin
			2 and its interactions with other matrix
			metalloproteinases.

			Nakamura H(1), Fujii Y, Ohuchi E, Yamamoto
			E, Okada Y.

			Author Information
			(1) Department of Molecular Immunology and
			Pathology, Cancer Research Institute,
			Kanazawa University, Japan.

			Matrix metalloproteinases (MMP) are synthesized
			as inactive zymogens (proMMP) and subsequently
			activated by many factors to degrade the
			extracellular matrix (ECM). In the present
			study, we have examined the intermolecular
			activation mechanisms of proMMP by MMP-10
			(stromelysin 2). ProMMP-10 was purified
			from the culture media of OSC-20 human oral
			squamous carcinoma cells stimulated with
			12-O-tetradecanoylphorbol 13-acetate. The
			final products are partially activated
			(approximately 38% of the full activity)
			during the purification steps and contain
			proMMP-10 of Mr 56,000 with minor protein
			bands of Mr 47,000, 24,000 and 22,000. The
			zymogen is activated by 4-aminophenylmercuric
			acetate and processed to the active forms
			of Mr 47,000 and 24,000. The NH2-terminal sequence
			of the 47,000- and 24,000-Mr species is
			Phe82-Ser-Ser-Phe-Pro-Gly, which is identical
			to that of stromelysin 2. ProMMP-9 (progelatinase
			B) is activated by MMP-10 to its full activity
			and processed to the low-Mr species of Mr
			81,000, 65,000, 57,000 and 55,000, the former
			two of which show proteolytic activity on
			a gelatin zymography. The NH2-terminal sequence
			analysis indicates that the 81,000-, 65,000-
			and 57,000-M, species have the identical
			sequence of Phe88-Gln-Thr-Phe-Glu-Gly, suggesting
			the cleavage of the Arg87-Phe88 peptide
			bond for activation and both NH2-terminal
			and COOH-terminal truncation in the 65,000-
			and 57,000-Mr forms. MMP-10 also activates
			proMMP-7 (promatrilysin) up to about 60%
			of the full activity and generates the same
			active species of Mr 19,000 as that obtained
			by activation with 4-aminophenylmercuric
			acetate. Incubation of proMMP-2 (progelatinase
			A) or proMMP-3 with MMP-10 does not result
			in activation of these proMMP. These results
			indicate that in addition to the previously
			reported activation of proMMP-1 (tissue
			procollagenase) and proMMP-8 (neutrophil
			procollagenase), MMP-10 can also activate
			proMMP-9 and proMMP-7, and suggest the possibility
			that MMP-10 may replace a role of MMP-3
			in the ECM degradation in concert with other
			MMP under various pathological conditions.

			PMID: 9578462 [Indexed for MEDLINE]

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