TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo
Matrix metalloproteinases (MMPs) are synthesized as latent proenzymes. A proteolytic cleavage event involving processing of the cysteine-rich N-terminal propeptide is required for their full activation. Previous in vitro studies indicated that activation of proMMP-2 can occur through formation of a...
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| Veröffentlicht in: | The Journal of biological chemistry 2000-08, Vol.275 (34), p.26411-26415 |
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| container_title | The Journal of biological chemistry |
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| creator | Wang, Z Juttermann, R Soloway, P D |
| description | Matrix metalloproteinases (MMPs) are synthesized as latent proenzymes. A proteolytic cleavage event involving processing of
the cysteine-rich N-terminal propeptide is required for their full activation. Previous in vitro studies indicated that activation of proMMP-2 can occur through formation of a trimolecular complex between MMP-14, TIMP-2,
and proMMP-2 at the cell surface. Using TIMP-2-deficient mice and cells derived from them, TIMP-2 was shown to be required
for efficient proMMP-2 activation both in vivo and in vitro . The requirement for TIMP-2 was not cell-autonomous as exogenously added TIMP-2 could restore activation of proMMP-2 to TIMP-2-deficient
cells. Mutant mice were overtly normal, viable, and fertile on the C57BL/6 background, indicating that both TIMP-2 and activated
proMMP-2 are dispensable for normal development. |
| doi_str_mv | 10.1074/jbc.M001270200 |
| format | Article |
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the cysteine-rich N-terminal propeptide is required for their full activation. Previous in vitro studies indicated that activation of proMMP-2 can occur through formation of a trimolecular complex between MMP-14, TIMP-2,
and proMMP-2 at the cell surface. Using TIMP-2-deficient mice and cells derived from them, TIMP-2 was shown to be required
for efficient proMMP-2 activation both in vivo and in vitro . The requirement for TIMP-2 was not cell-autonomous as exogenously added TIMP-2 could restore activation of proMMP-2 to TIMP-2-deficient
cells. Mutant mice were overtly normal, viable, and fertile on the C57BL/6 background, indicating that both TIMP-2 and activated
proMMP-2 are dispensable for normal development.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M001270200</identifier><identifier>PMID: 10827175</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Cattle ; Enzyme Activation ; Enzyme Precursors - metabolism ; Gelatinases - metabolism ; Matrix Metalloproteinases, Membrane-Associated ; Metalloendopeptidases - metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Tissue Inhibitor of Metalloproteinase-1 - metabolism ; Tissue Inhibitor of Metalloproteinase-2 - deficiency ; Tissue Inhibitor of Metalloproteinase-2 - physiology</subject><ispartof>The Journal of biological chemistry, 2000-08, Vol.275 (34), p.26411-26415</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c481t-34790e51f6090f206e866c0fb9bda70a449d89b763043e224ea2bd139a634d63</citedby><cites>FETCH-LOGICAL-c481t-34790e51f6090f206e866c0fb9bda70a449d89b763043e224ea2bd139a634d63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10827175$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Z</creatorcontrib><creatorcontrib>Juttermann, R</creatorcontrib><creatorcontrib>Soloway, P D</creatorcontrib><title>TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Matrix metalloproteinases (MMPs) are synthesized as latent proenzymes. A proteolytic cleavage event involving processing of
the cysteine-rich N-terminal propeptide is required for their full activation. Previous in vitro studies indicated that activation of proMMP-2 can occur through formation of a trimolecular complex between MMP-14, TIMP-2,
and proMMP-2 at the cell surface. Using TIMP-2-deficient mice and cells derived from them, TIMP-2 was shown to be required
for efficient proMMP-2 activation both in vivo and in vitro . The requirement for TIMP-2 was not cell-autonomous as exogenously added TIMP-2 could restore activation of proMMP-2 to TIMP-2-deficient
cells. Mutant mice were overtly normal, viable, and fertile on the C57BL/6 background, indicating that both TIMP-2 and activated
proMMP-2 are dispensable for normal development.</description><subject>Animals</subject><subject>Cattle</subject><subject>Enzyme Activation</subject><subject>Enzyme Precursors - metabolism</subject><subject>Gelatinases - metabolism</subject><subject>Matrix Metalloproteinases, Membrane-Associated</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Tissue Inhibitor of Metalloproteinase-1 - metabolism</subject><subject>Tissue Inhibitor of Metalloproteinase-2 - deficiency</subject><subject>Tissue Inhibitor of Metalloproteinase-2 - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkMtLAzEQh4MoWqtXj7IH8bZ18tjN5qKI-ChYFCniLWSzSRtpNzXZVvzvjbb4GAhzyDczPz6EjjAMMHB29lrrwQgAEw4EYAv1MFQ0pwV-2UY9AIJzQYpqD-3H-AqpmMC7aC9BhGNe9NDFeDh6zEk2jNmTeVu6YJrM-pBdW-u0M22XXerOrVTnfJt5my2CH30PuDZ7dit_gHasmkVzuOl9NL65Hl_d5fcPt8Ory_tcswp3OWVcgCmwLUGAJVCaqiw12FrUjeKgGBNNJWpeUmDUEMKMInWDqVAlZU1J--h8vXaxrOem0SlYUDO5CG6uwof0ysn_P62byolfSVJWFNLro9PNguDfliZ2cu6iNrOZao1fRskJFhw4T-BgDergYwzG_hzBIL-Uy6Rc_ipPA8d_o_3B144TcLIGpm4yfU-GZe28npq5JLyQlKWMDGP6CR9Qhpc</recordid><startdate>20000825</startdate><enddate>20000825</enddate><creator>Wang, Z</creator><creator>Juttermann, R</creator><creator>Soloway, P D</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000825</creationdate><title>TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo</title><author>Wang, Z ; Juttermann, R ; Soloway, P D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c481t-34790e51f6090f206e866c0fb9bda70a449d89b763043e224ea2bd139a634d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Enzyme Activation</topic><topic>Enzyme Precursors - metabolism</topic><topic>Gelatinases - metabolism</topic><topic>Matrix Metalloproteinases, Membrane-Associated</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Tissue Inhibitor of Metalloproteinase-1 - metabolism</topic><topic>Tissue Inhibitor of Metalloproteinase-2 - deficiency</topic><topic>Tissue Inhibitor of Metalloproteinase-2 - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Z</creatorcontrib><creatorcontrib>Juttermann, R</creatorcontrib><creatorcontrib>Soloway, P D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Z</au><au>Juttermann, R</au><au>Soloway, P D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2000-08-25</date><risdate>2000</risdate><volume>275</volume><issue>34</issue><spage>26411</spage><epage>26415</epage><pages>26411-26415</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Matrix metalloproteinases (MMPs) are synthesized as latent proenzymes. A proteolytic cleavage event involving processing of
the cysteine-rich N-terminal propeptide is required for their full activation. Previous in vitro studies indicated that activation of proMMP-2 can occur through formation of a trimolecular complex between MMP-14, TIMP-2,
and proMMP-2 at the cell surface. Using TIMP-2-deficient mice and cells derived from them, TIMP-2 was shown to be required
for efficient proMMP-2 activation both in vivo and in vitro . The requirement for TIMP-2 was not cell-autonomous as exogenously added TIMP-2 could restore activation of proMMP-2 to TIMP-2-deficient
cells. Mutant mice were overtly normal, viable, and fertile on the C57BL/6 background, indicating that both TIMP-2 and activated
proMMP-2 are dispensable for normal development.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>10827175</pmid><doi>10.1074/jbc.M001270200</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2000-08, Vol.275 (34), p.26411-26415 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2683068 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Animals Cattle Enzyme Activation Enzyme Precursors - metabolism Gelatinases - metabolism Matrix Metalloproteinases, Membrane-Associated Metalloendopeptidases - metabolism Mice Mice, Inbred C57BL Mice, Knockout Tissue Inhibitor of Metalloproteinase-1 - metabolism Tissue Inhibitor of Metalloproteinase-2 - deficiency Tissue Inhibitor of Metalloproteinase-2 - physiology |
| title | TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo |
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