Growth Stimulation of Human Keratinocytes by Tissue Inhibitor of Metalloproteinases
Human recombinant tissue inhibitor of metalloproteinases (rTIMP) at 0.2-4.6 μM was found to stimulate the growth of normal human keratinocytes, in primary cultures on a plastic support, and to markedly increase their growth on a tridimensional culture system, the skin equivalent, as shown by histolo...
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| Veröffentlicht in: | Journal of investigative dermatology 1991-10, Vol.97 (4), p.679-685 |
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| creator | Bertaux, Brigitte Hornebeck, William Eisen, Arthur Z Dubertret, Louis |
| description | Human recombinant tissue inhibitor of metalloproteinases (rTIMP) at 0.2-4.6 μM was found to stimulate the growth of normal human keratinocytes, in primary cultures on a plastic support, and to markedly increase their growth on a tridimensional culture system, the skin equivalent, as shown by histology, DNA measurements, and planimetry. In contrast rTIMP had no effect on the growth of normal human fibroblasts.
The growth of keratinocytes on extracellular matrix components produced by keratinocytes cultured in the presence or absence of rTIMP was similar, suggesting that rTIMP does bit stimulate keratinocyte growth by modifying either the quantity or the composition of the extracellular matrix deposited.
rTIMP was labeled with 125iodine in order to study its interaction with keratinocytes in culture. Binding of (125I) rTIMP to keratinocytes was found to be temperature and time dependent. Under steady-state was identified with KD of 8.7nM and 135,000 sites/cell. Such findings are in keeping with the known potentiating effect of TIMP on erythroid precursors, and indicate that this protein has at least two distinct activities. |
| doi_str_mv | 10.1111/1523-1747.ep12483956 |
| format | Article |
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The growth of keratinocytes on extracellular matrix components produced by keratinocytes cultured in the presence or absence of rTIMP was similar, suggesting that rTIMP does bit stimulate keratinocyte growth by modifying either the quantity or the composition of the extracellular matrix deposited.
rTIMP was labeled with 125iodine in order to study its interaction with keratinocytes in culture. Binding of (125I) rTIMP to keratinocytes was found to be temperature and time dependent. Under steady-state was identified with KD of 8.7nM and 135,000 sites/cell. Such findings are in keeping with the known potentiating effect of TIMP on erythroid precursors, and indicate that this protein has at least two distinct activities.</description><identifier>ISSN: 0022-202X</identifier><identifier>EISSN: 1523-1747</identifier><identifier>DOI: 10.1111/1523-1747.ep12483956</identifier><identifier>PMID: 1940438</identifier><identifier>CODEN: JIDEAE</identifier><language>eng</language><publisher>Danvers, MA: Elsevier Inc</publisher><subject>Binding Sites ; Biological and medical sciences ; Cell Division - drug effects ; Cell physiology ; Cells, Cultured ; Extracellular Matrix Proteins - biosynthesis ; Fibroblasts - drug effects ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - metabolism ; Glycoproteins - pharmacology ; Humans ; Keratinocytes - drug effects ; Keratinocytes - metabolism ; Metalloendopeptidases - antagonists & inhibitors ; Molecular and cellular biology ; Recombinant Proteins - metabolism ; Recombinant Proteins - pharmacology ; Responses to growth factors, tumor promotors, other factors ; Tissue Inhibitor of Metalloproteinases</subject><ispartof>Journal of investigative dermatology, 1991-10, Vol.97 (4), p.679-685</ispartof><rights>1991 The Society for Investigative Dermatology, Inc</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-92e798d00e5a4ae0b816354db69d01e1bcbc62362602c92c93744a6237a1dcf23</citedby><cites>FETCH-LOGICAL-c452t-92e798d00e5a4ae0b816354db69d01e1bcbc62362602c92c93744a6237a1dcf23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5091736$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1940438$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bertaux, Brigitte</creatorcontrib><creatorcontrib>Hornebeck, William</creatorcontrib><creatorcontrib>Eisen, Arthur Z</creatorcontrib><creatorcontrib>Dubertret, Louis</creatorcontrib><title>Growth Stimulation of Human Keratinocytes by Tissue Inhibitor of Metalloproteinases</title><title>Journal of investigative dermatology</title><addtitle>J Invest Dermatol</addtitle><description>Human recombinant tissue inhibitor of metalloproteinases (rTIMP) at 0.2-4.6 μM was found to stimulate the growth of normal human keratinocytes, in primary cultures on a plastic support, and to markedly increase their growth on a tridimensional culture system, the skin equivalent, as shown by histology, DNA measurements, and planimetry. In contrast rTIMP had no effect on the growth of normal human fibroblasts.
The growth of keratinocytes on extracellular matrix components produced by keratinocytes cultured in the presence or absence of rTIMP was similar, suggesting that rTIMP does bit stimulate keratinocyte growth by modifying either the quantity or the composition of the extracellular matrix deposited.
rTIMP was labeled with 125iodine in order to study its interaction with keratinocytes in culture. Binding of (125I) rTIMP to keratinocytes was found to be temperature and time dependent. Under steady-state was identified with KD of 8.7nM and 135,000 sites/cell. Such findings are in keeping with the known potentiating effect of TIMP on erythroid precursors, and indicate that this protein has at least two distinct activities.</description><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cell Division - drug effects</subject><subject>Cell physiology</subject><subject>Cells, Cultured</subject><subject>Extracellular Matrix Proteins - biosynthesis</subject><subject>Fibroblasts - drug effects</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - metabolism</subject><subject>Glycoproteins - pharmacology</subject><subject>Humans</subject><subject>Keratinocytes - drug effects</subject><subject>Keratinocytes - metabolism</subject><subject>Metalloendopeptidases - antagonists & inhibitors</subject><subject>Molecular and cellular biology</subject><subject>Recombinant Proteins - metabolism</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Responses to growth factors, tumor promotors, other factors</subject><subject>Tissue Inhibitor of Metalloproteinases</subject><issn>0022-202X</issn><issn>1523-1747</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9LxDAQxYMouq5-A4UexFvXJE3T9iKI-A9XPKjgLaTpFCNtsiapst_elC7rzSEw8ObNm_BD6ITgBYl1QXKapaRgxQJWhLIyq3K-g2ZbeRfNMKY0pZi-H6BD7z8xJpzl5T7aJxXDLCtn6OXO2Z_wkbwE3Q-dDNqaxLbJ_dBLkzyCi4qxah3AJ_U6edXeD5A8mA9d62DdaH2CILvOrpwNoI304I_QXis7D8ebPkdvtzev1_fp8vnu4fpqmSqW05BWFIqqbDCGXDIJuC4Jz3LW1LxqMAFSq1pxmnHKMVVVfFnBmIxKIUmjWprN0fmUG29_DeCD6LVX0HXSgB28KCjLGeckGtlkVM5676AVK6d76daCYDGyFCM0MUITfyzj2ukmf6h7aP6WJnhxfraZS69k1zpplPZbW44rUmRjzOVkg8jiW4MTXmkwChrtQAXRWP3_P34BpYWQow</recordid><startdate>19911001</startdate><enddate>19911001</enddate><creator>Bertaux, Brigitte</creator><creator>Hornebeck, William</creator><creator>Eisen, Arthur Z</creator><creator>Dubertret, Louis</creator><general>Elsevier Inc</general><general>Nature Publishing</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><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></search><sort><creationdate>19911001</creationdate><title>Growth Stimulation of Human Keratinocytes by Tissue Inhibitor of Metalloproteinases</title><author>Bertaux, Brigitte ; Hornebeck, William ; Eisen, Arthur Z ; Dubertret, Louis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-92e798d00e5a4ae0b816354db69d01e1bcbc62362602c92c93744a6237a1dcf23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cell Division - drug effects</topic><topic>Cell physiology</topic><topic>Cells, Cultured</topic><topic>Extracellular Matrix Proteins - biosynthesis</topic><topic>Fibroblasts - drug effects</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - metabolism</topic><topic>Glycoproteins - pharmacology</topic><topic>Humans</topic><topic>Keratinocytes - drug effects</topic><topic>Keratinocytes - metabolism</topic><topic>Metalloendopeptidases - antagonists & inhibitors</topic><topic>Molecular and cellular biology</topic><topic>Recombinant Proteins - metabolism</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Responses to growth factors, tumor promotors, other factors</topic><topic>Tissue Inhibitor of Metalloproteinases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bertaux, Brigitte</creatorcontrib><creatorcontrib>Hornebeck, William</creatorcontrib><creatorcontrib>Eisen, Arthur Z</creatorcontrib><creatorcontrib>Dubertret, Louis</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><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><jtitle>Journal of investigative dermatology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bertaux, Brigitte</au><au>Hornebeck, William</au><au>Eisen, Arthur Z</au><au>Dubertret, Louis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Growth Stimulation of Human Keratinocytes by Tissue Inhibitor of Metalloproteinases</atitle><jtitle>Journal of investigative dermatology</jtitle><addtitle>J Invest Dermatol</addtitle><date>1991-10-01</date><risdate>1991</risdate><volume>97</volume><issue>4</issue><spage>679</spage><epage>685</epage><pages>679-685</pages><issn>0022-202X</issn><eissn>1523-1747</eissn><coden>JIDEAE</coden><abstract>Human recombinant tissue inhibitor of metalloproteinases (rTIMP) at 0.2-4.6 μM was found to stimulate the growth of normal human keratinocytes, in primary cultures on a plastic support, and to markedly increase their growth on a tridimensional culture system, the skin equivalent, as shown by histology, DNA measurements, and planimetry. In contrast rTIMP had no effect on the growth of normal human fibroblasts.
The growth of keratinocytes on extracellular matrix components produced by keratinocytes cultured in the presence or absence of rTIMP was similar, suggesting that rTIMP does bit stimulate keratinocyte growth by modifying either the quantity or the composition of the extracellular matrix deposited.
rTIMP was labeled with 125iodine in order to study its interaction with keratinocytes in culture. Binding of (125I) rTIMP to keratinocytes was found to be temperature and time dependent. Under steady-state was identified with KD of 8.7nM and 135,000 sites/cell. Such findings are in keeping with the known potentiating effect of TIMP on erythroid precursors, and indicate that this protein has at least two distinct activities.</abstract><cop>Danvers, MA</cop><pub>Elsevier Inc</pub><pmid>1940438</pmid><doi>10.1111/1523-1747.ep12483956</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of investigative dermatology, 1991-10, Vol.97 (4), p.679-685 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Binding Sites Biological and medical sciences Cell Division - drug effects Cell physiology Cells, Cultured Extracellular Matrix Proteins - biosynthesis Fibroblasts - drug effects Fundamental and applied biological sciences. Psychology Glycoproteins - metabolism Glycoproteins - pharmacology Humans Keratinocytes - drug effects Keratinocytes - metabolism Metalloendopeptidases - antagonists & inhibitors Molecular and cellular biology Recombinant Proteins - metabolism Recombinant Proteins - pharmacology Responses to growth factors, tumor promotors, other factors Tissue Inhibitor of Metalloproteinases |
| title | Growth Stimulation of Human Keratinocytes by Tissue Inhibitor of Metalloproteinases |
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