Proteinases in cutaneous wound healing
Cutaneous wound healing is a complex and highly coordinated process where a number of different cell types participate to renew the damaged tissue under the strict regulation of soluble and insoluble factors. One of the most versatile processes involved in wound repair is proteolysis. During cell mi...
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description | Cutaneous wound healing is a complex and highly coordinated process where a number of different cell types participate to renew the damaged tissue under the strict regulation of soluble and insoluble factors. One of the most versatile processes involved in wound repair is proteolysis. During cell migration, proteins of extracellular matrix are cleaved, often creating biologically active cleavage products, and proteolysis of cellular contacts leads to increased cell motility and division. Moreover, proteases activate various growth factors and other proteases in wound and regulate growth factor signaling by shedding growth factor receptors on cell surface. Normally, proteolysis is strictly controlled, and changes in protease activity are associated with alterations in wound closure and scar formation. Here, we present the current view on the role of metalloproteinases and the plasmin-plasminogen system in normal and aberrant cutaneous wound repair and discuss their role as potential therapeutic targets for chronic ulcers or fibrotic scars. |
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One of the most versatile processes involved in wound repair is proteolysis. During cell migration, proteins of extracellular matrix are cleaved, often creating biologically active cleavage products, and proteolysis of cellular contacts leads to increased cell motility and division. Moreover, proteases activate various growth factors and other proteases in wound and regulate growth factor signaling by shedding growth factor receptors on cell surface. Normally, proteolysis is strictly controlled, and changes in protease activity are associated with alterations in wound closure and scar formation. Here, we present the current view on the role of metalloproteinases and the plasmin-plasminogen system in normal and aberrant cutaneous wound repair and discuss their role as potential therapeutic targets for chronic ulcers or fibrotic scars.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-008-8388-4</identifier><identifier>PMID: 18810321</identifier><language>eng</language><publisher>Basel: Basel : Birkhäuser-Verlag</publisher><subject>ADAM ; ADAM Proteins - metabolism ; ADAMTS ; Animals ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cell adhesion & migration ; Cell Biology ; Cicatrix - metabolism ; Cicatrix - pathology ; Fibrinolysin - metabolism ; fibrosis ; Growth factors ; Humans ; Life Sciences ; Matrix Metalloproteinases - metabolism ; MMP ; Models, Biological ; Peptide Hydrolases - metabolism ; plasminogen ; Proteins ; Review ; skin ; Skin - injuries ; Skin - metabolism ; Tissue Inhibitor of Metalloproteinases - metabolism ; wound ; Wound healing ; Wound Healing - physiology</subject><ispartof>Cellular and molecular life sciences : CMLS, 2009-01, Vol.66 (2), p.203-224</ispartof><rights>Birkhäuser Verlag, Basel 2008</rights><rights>Birkhäuser Verlag, Basel 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c449t-5019bc7fc259754c589f03521522c86bd3a0bddbeb4b1b5be0904ec637ee07803</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11131559/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11131559/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41488,42557,51319,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18810321$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Toriseva, M</creatorcontrib><creatorcontrib>Kähäri, V.-M</creatorcontrib><title>Proteinases in cutaneous wound healing</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>Cutaneous wound healing is a complex and highly coordinated process where a number of different cell types participate to renew the damaged tissue under the strict regulation of soluble and insoluble factors. One of the most versatile processes involved in wound repair is proteolysis. During cell migration, proteins of extracellular matrix are cleaved, often creating biologically active cleavage products, and proteolysis of cellular contacts leads to increased cell motility and division. Moreover, proteases activate various growth factors and other proteases in wound and regulate growth factor signaling by shedding growth factor receptors on cell surface. Normally, proteolysis is strictly controlled, and changes in protease activity are associated with alterations in wound closure and scar formation. Here, we present the current view on the role of metalloproteinases and the plasmin-plasminogen system in normal and aberrant cutaneous wound repair and discuss their role as potential therapeutic targets for chronic ulcers or fibrotic scars.</description><subject>ADAM</subject><subject>ADAM Proteins - metabolism</subject><subject>ADAMTS</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell adhesion & migration</subject><subject>Cell Biology</subject><subject>Cicatrix - metabolism</subject><subject>Cicatrix - pathology</subject><subject>Fibrinolysin - metabolism</subject><subject>fibrosis</subject><subject>Growth factors</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Matrix Metalloproteinases - metabolism</subject><subject>MMP</subject><subject>Models, Biological</subject><subject>Peptide Hydrolases - metabolism</subject><subject>plasminogen</subject><subject>Proteins</subject><subject>Review</subject><subject>skin</subject><subject>Skin - injuries</subject><subject>Skin - metabolism</subject><subject>Tissue Inhibitor of Metalloproteinases - metabolism</subject><subject>wound</subject><subject>Wound healing</subject><subject>Wound Healing - physiology</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kc1L5TAUxYM4-P0HuNGHC3cd702aj65EZNQBQUEFdyFJ02elL9GkVea_nz76UGcWrhK4v3NyTw4h-wg_EUCeZABAVQCoQjGlinKNbGFJoahA4vrqLhR93CTbOT-PMFdUbJBNVAqBUdwix7cp9r4NJvs8a8PMDb0JPg559h6HUM-evOnaMN8lPxrTZb-3OnfIw8Wv-_Or4vrm8vf52XXhyrLqCw5YWScbR3kleem4qhpgnCKn1Clha2bA1rX1trRoufVQQemdYNJ7kArYDjmdfF8Gu_C186FPptMvqV2Y9EdH0-p_J6F90vP4phGRIefV6HC8ckjxdfC514s2O991UywthJJIJRvBo__A5zikMKbTUiBIJugSwglyKeacfPOxCoJedqCnDvTYgV52oMtRc_A1w6di9ekjQCcgj6Mw9-nz5e9cDydRY6I289Rm_XBHAdmyVCkFZ38BVeyaLQ</recordid><startdate>20090101</startdate><enddate>20090101</enddate><creator>Toriseva, M</creator><creator>Kähäri, V.-M</creator><general>Basel : Birkhäuser-Verlag</general><general>Birkhäuser-Verlag</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090101</creationdate><title>Proteinases in cutaneous wound healing</title><author>Toriseva, M ; Kähäri, V.-M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c449t-5019bc7fc259754c589f03521522c86bd3a0bddbeb4b1b5be0904ec637ee07803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>ADAM</topic><topic>ADAM Proteins - 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Mol. Life Sci</stitle><addtitle>Cell Mol Life Sci</addtitle><date>2009-01-01</date><risdate>2009</risdate><volume>66</volume><issue>2</issue><spage>203</spage><epage>224</epage><pages>203-224</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>Cutaneous wound healing is a complex and highly coordinated process where a number of different cell types participate to renew the damaged tissue under the strict regulation of soluble and insoluble factors. One of the most versatile processes involved in wound repair is proteolysis. During cell migration, proteins of extracellular matrix are cleaved, often creating biologically active cleavage products, and proteolysis of cellular contacts leads to increased cell motility and division. Moreover, proteases activate various growth factors and other proteases in wound and regulate growth factor signaling by shedding growth factor receptors on cell surface. Normally, proteolysis is strictly controlled, and changes in protease activity are associated with alterations in wound closure and scar formation. Here, we present the current view on the role of metalloproteinases and the plasmin-plasminogen system in normal and aberrant cutaneous wound repair and discuss their role as potential therapeutic targets for chronic ulcers or fibrotic scars.</abstract><cop>Basel</cop><pub>Basel : Birkhäuser-Verlag</pub><pmid>18810321</pmid><doi>10.1007/s00018-008-8388-4</doi><tpages>22</tpages></addata></record> |
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subjects | ADAM ADAM Proteins - metabolism ADAMTS Animals Biochemistry Biomedical and Life Sciences Biomedicine Cell adhesion & migration Cell Biology Cicatrix - metabolism Cicatrix - pathology Fibrinolysin - metabolism fibrosis Growth factors Humans Life Sciences Matrix Metalloproteinases - metabolism MMP Models, Biological Peptide Hydrolases - metabolism plasminogen Proteins Review skin Skin - injuries Skin - metabolism Tissue Inhibitor of Metalloproteinases - metabolism wound Wound healing Wound Healing - physiology |
title | Proteinases in cutaneous wound healing |
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