Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro
A high proportion of NG2 in the adult rat spinal cord is saline-soluble and migrates slightly faster than intact NG2 on SDS–PAGE, suggesting that it represents the shed ectodomain of NG2. In the injured cerebral cortex, much of the overall increase in NG2 is due to the saline-soluble (shed), rather...
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| Veröffentlicht in: | Molecular and cellular neuroscience 2005-05, Vol.29 (1), p.82-96 |
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| creator | Asher, Richard A. Morgenstern, Daniel A. Properzi, Francesca Nishiyama, Akiko Levine, Joel M. Fawcett, James W. |
| description | A high proportion of NG2 in the adult rat spinal cord is saline-soluble and migrates slightly faster than intact NG2 on SDS–PAGE, suggesting that it represents the shed ectodomain of NG2. In the injured cerebral cortex, much of the overall increase in NG2 is due to the saline-soluble (shed), rather than the detergent-soluble (intact), form. Hydroxamic acid metalloproteinase inhibitors, but not TIMPs, were able to prevent NG2 shedding in oligodendrocyte precursor cells (OPCs) in vitro
. The generation of another truncated form of NG2 was, however, sensitive to TIMP-2 and TIMP-3. Two observations suggest that NG2 is involved in PDGF signaling in OPCs: the rate of NG2 shedding increased with cell density and NG2 expression was increased in the absence of PDGF. Ectodomain shedding converts NG2 into a diffusible entity able to interact with the growth cone, and we suggest that this release is likely to enhance its axon growth-inhibitory activity. |
| doi_str_mv | 10.1016/j.mcn.2005.02.001 |
| format | Article |
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. The generation of another truncated form of NG2 was, however, sensitive to TIMP-2 and TIMP-3. Two observations suggest that NG2 is involved in PDGF signaling in OPCs: the rate of NG2 shedding increased with cell density and NG2 expression was increased in the absence of PDGF. Ectodomain shedding converts NG2 into a diffusible entity able to interact with the growth cone, and we suggest that this release is likely to enhance its axon growth-inhibitory activity.</description><identifier>ISSN: 1044-7431</identifier><identifier>EISSN: 1095-9327</identifier><identifier>DOI: 10.1016/j.mcn.2005.02.001</identifier><identifier>PMID: 15866049</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Antigens - chemistry ; Antigens - genetics ; Antigens - metabolism ; Axons - enzymology ; Cells, Cultured ; Female ; Growth Cones - enzymology ; In Vitro Techniques ; Metalloendopeptidases - genetics ; Metalloendopeptidases - metabolism ; Oligodendroglia - cytology ; Protein Structure, Tertiary ; Proteoglycans - chemistry ; Proteoglycans - genetics ; Proteoglycans - metabolism ; Rats ; Rats, Sprague-Dawley ; Reverse Transcriptase Polymerase Chain Reaction ; Sodium Chloride ; Solubility ; Spinal Cord - cytology ; Spinal Cord - enzymology ; Stem Cells - cytology ; Stem Cells - ultrastructure ; Tissue Inhibitor of Metalloproteinase-1 - metabolism ; Tissue Inhibitor of Metalloproteinase-2 - metabolism ; Tissue Inhibitor of Metalloproteinase-3 - metabolism</subject><ispartof>Molecular and cellular neuroscience, 2005-05, Vol.29 (1), p.82-96</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-34d12a40a085e82ba75454d52b804f2443bc65015131c06c3ef3a1a2ead1c5963</citedby><cites>FETCH-LOGICAL-c382t-34d12a40a085e82ba75454d52b804f2443bc65015131c06c3ef3a1a2ead1c5963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.mcn.2005.02.001$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15866049$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Asher, Richard A.</creatorcontrib><creatorcontrib>Morgenstern, Daniel A.</creatorcontrib><creatorcontrib>Properzi, Francesca</creatorcontrib><creatorcontrib>Nishiyama, Akiko</creatorcontrib><creatorcontrib>Levine, Joel M.</creatorcontrib><creatorcontrib>Fawcett, James W.</creatorcontrib><title>Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro</title><title>Molecular and cellular neuroscience</title><addtitle>Mol Cell Neurosci</addtitle><description>A high proportion of NG2 in the adult rat spinal cord is saline-soluble and migrates slightly faster than intact NG2 on SDS–PAGE, suggesting that it represents the shed ectodomain of NG2. In the injured cerebral cortex, much of the overall increase in NG2 is due to the saline-soluble (shed), rather than the detergent-soluble (intact), form. Hydroxamic acid metalloproteinase inhibitors, but not TIMPs, were able to prevent NG2 shedding in oligodendrocyte precursor cells (OPCs) in vitro
. The generation of another truncated form of NG2 was, however, sensitive to TIMP-2 and TIMP-3. Two observations suggest that NG2 is involved in PDGF signaling in OPCs: the rate of NG2 shedding increased with cell density and NG2 expression was increased in the absence of PDGF. Ectodomain shedding converts NG2 into a diffusible entity able to interact with the growth cone, and we suggest that this release is likely to enhance its axon growth-inhibitory activity.</description><subject>Animals</subject><subject>Antigens - chemistry</subject><subject>Antigens - genetics</subject><subject>Antigens - metabolism</subject><subject>Axons - enzymology</subject><subject>Cells, Cultured</subject><subject>Female</subject><subject>Growth Cones - enzymology</subject><subject>In Vitro Techniques</subject><subject>Metalloendopeptidases - genetics</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Oligodendroglia - cytology</subject><subject>Protein Structure, Tertiary</subject><subject>Proteoglycans - chemistry</subject><subject>Proteoglycans - genetics</subject><subject>Proteoglycans - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Sodium Chloride</subject><subject>Solubility</subject><subject>Spinal Cord - cytology</subject><subject>Spinal Cord - enzymology</subject><subject>Stem Cells - cytology</subject><subject>Stem Cells - ultrastructure</subject><subject>Tissue Inhibitor of Metalloproteinase-1 - metabolism</subject><subject>Tissue Inhibitor of Metalloproteinase-2 - metabolism</subject><subject>Tissue Inhibitor of Metalloproteinase-3 - metabolism</subject><issn>1044-7431</issn><issn>1095-9327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctuFDEQRS1ERELCB7BBXrHrpvzqh1ihCAJSRDbJ2nLb1YlH3fZgexKFr8eTGYkdrGzL5x6V6hLynkHLgHWfNu1qQ8sBVAu8BWCvyBmDUTWj4P3r_V3KppeCnZK3OW-ggnwUb8gpU0PXgRzPyO_bp0gzbk0yBemKxSxL3KZY0AeTkRpb_KMvHjM1CWnCvI0h-2lBOsdEywPS_IDO-XBPTXC0Ri3mvH_G-eX75xWnL8J4vzxbE6gPtBpTvCAns1kyvjue5-Tu29fby-_N9c3Vj8sv140VAy-NkI5xI8HAoHDgk-mVVNIpPg0gZy6lmGyngCkmmIXOCpyFYYajccyqsRPn5OPBW6f4tcNc9OqzxWUxAeMu667vh3Ho-H9B1gvR19VWkB1Am2LOCWe9TX416Vkz0Ptm9EbXZvS-GQ1c12Zq5sNRvptWdH8Txyoq8PkAYN3Fo8eks_UYLDqf0Bbtov-H_g9ZI5_H</recordid><startdate>20050501</startdate><enddate>20050501</enddate><creator>Asher, Richard A.</creator><creator>Morgenstern, Daniel A.</creator><creator>Properzi, Francesca</creator><creator>Nishiyama, Akiko</creator><creator>Levine, Joel M.</creator><creator>Fawcett, James W.</creator><general>Elsevier Inc</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>20050501</creationdate><title>Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro</title><author>Asher, Richard A. ; Morgenstern, Daniel A. ; Properzi, Francesca ; Nishiyama, Akiko ; Levine, Joel M. ; Fawcett, James W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-34d12a40a085e82ba75454d52b804f2443bc65015131c06c3ef3a1a2ead1c5963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Antigens - chemistry</topic><topic>Antigens - genetics</topic><topic>Antigens - metabolism</topic><topic>Axons - enzymology</topic><topic>Cells, Cultured</topic><topic>Female</topic><topic>Growth Cones - enzymology</topic><topic>In Vitro Techniques</topic><topic>Metalloendopeptidases - genetics</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Oligodendroglia - cytology</topic><topic>Protein Structure, Tertiary</topic><topic>Proteoglycans - chemistry</topic><topic>Proteoglycans - genetics</topic><topic>Proteoglycans - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Sodium Chloride</topic><topic>Solubility</topic><topic>Spinal Cord - cytology</topic><topic>Spinal Cord - enzymology</topic><topic>Stem Cells - cytology</topic><topic>Stem Cells - ultrastructure</topic><topic>Tissue Inhibitor of Metalloproteinase-1 - metabolism</topic><topic>Tissue Inhibitor of Metalloproteinase-2 - metabolism</topic><topic>Tissue Inhibitor of Metalloproteinase-3 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Asher, Richard A.</creatorcontrib><creatorcontrib>Morgenstern, Daniel A.</creatorcontrib><creatorcontrib>Properzi, Francesca</creatorcontrib><creatorcontrib>Nishiyama, Akiko</creatorcontrib><creatorcontrib>Levine, Joel M.</creatorcontrib><creatorcontrib>Fawcett, James W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Asher, Richard A.</au><au>Morgenstern, Daniel A.</au><au>Properzi, Francesca</au><au>Nishiyama, Akiko</au><au>Levine, Joel M.</au><au>Fawcett, James W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro</atitle><jtitle>Molecular and cellular neuroscience</jtitle><addtitle>Mol Cell Neurosci</addtitle><date>2005-05-01</date><risdate>2005</risdate><volume>29</volume><issue>1</issue><spage>82</spage><epage>96</epage><pages>82-96</pages><issn>1044-7431</issn><eissn>1095-9327</eissn><abstract>A high proportion of NG2 in the adult rat spinal cord is saline-soluble and migrates slightly faster than intact NG2 on SDS–PAGE, suggesting that it represents the shed ectodomain of NG2. In the injured cerebral cortex, much of the overall increase in NG2 is due to the saline-soluble (shed), rather than the detergent-soluble (intact), form. Hydroxamic acid metalloproteinase inhibitors, but not TIMPs, were able to prevent NG2 shedding in oligodendrocyte precursor cells (OPCs) in vitro
. The generation of another truncated form of NG2 was, however, sensitive to TIMP-2 and TIMP-3. Two observations suggest that NG2 is involved in PDGF signaling in OPCs: the rate of NG2 shedding increased with cell density and NG2 expression was increased in the absence of PDGF. Ectodomain shedding converts NG2 into a diffusible entity able to interact with the growth cone, and we suggest that this release is likely to enhance its axon growth-inhibitory activity.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15866049</pmid><doi>10.1016/j.mcn.2005.02.001</doi><tpages>15</tpages></addata></record> |
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| subjects | Animals Antigens - chemistry Antigens - genetics Antigens - metabolism Axons - enzymology Cells, Cultured Female Growth Cones - enzymology In Vitro Techniques Metalloendopeptidases - genetics Metalloendopeptidases - metabolism Oligodendroglia - cytology Protein Structure, Tertiary Proteoglycans - chemistry Proteoglycans - genetics Proteoglycans - metabolism Rats Rats, Sprague-Dawley Reverse Transcriptase Polymerase Chain Reaction Sodium Chloride Solubility Spinal Cord - cytology Spinal Cord - enzymology Stem Cells - cytology Stem Cells - ultrastructure Tissue Inhibitor of Metalloproteinase-1 - metabolism Tissue Inhibitor of Metalloproteinase-2 - metabolism Tissue Inhibitor of Metalloproteinase-3 - metabolism |
| title | Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro |
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