Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions
Decorin, a prototype small leucine-rich proteoglycan, regulates a vast array of cellular processes including collagen fibrillogenesis, wound repair, angiostasis, tumor growth, and autophagy. This functional versatility arises from a wide array of decorin/protein interactions also including interacti...
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Veröffentlicht in: | Matrix biology 2016-09, Vol.55, p.7-21 |
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description | Decorin, a prototype small leucine-rich proteoglycan, regulates a vast array of cellular processes including collagen fibrillogenesis, wound repair, angiostasis, tumor growth, and autophagy. This functional versatility arises from a wide array of decorin/protein interactions also including interactions with its single glycosaminoglycan side chain. The decorin-binding partners encompass numerous categories ranging from extracellular matrix molecules to cell surface receptors to growth factors and enzymes. Despite the diversity of the decorin interacting network, two main roles emerge as prominent themes in decorin function: maintenance of cellular structure and outside-in signaling, culminating in anti-tumorigenic effects. Here we present contemporary knowledge regarding the decorin interacting network and discuss in detail the biological relevance of these pleiotropic interactions, some of which could be targeted by therapeutic interventions.
•Decorin embraces a variety of binding partners branding it as a multi-purpose small, leucine-rich proteoglycan.•Structural integrity and cellular signaling are two prominent themes found in the decorin interactome.•Decorin anti-tumorigenic effects result from multiple concurrent interactions with receptor tyrosine kinases.•Emerging functions include angiostasis and autophagic induction. |
doi_str_mv | 10.1016/j.matbio.2016.09.009 |
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•Decorin embraces a variety of binding partners branding it as a multi-purpose small, leucine-rich proteoglycan.•Structural integrity and cellular signaling are two prominent themes found in the decorin interactome.•Decorin anti-tumorigenic effects result from multiple concurrent interactions with receptor tyrosine kinases.•Emerging functions include angiostasis and autophagic induction.</description><identifier>ISSN: 0945-053X</identifier><identifier>EISSN: 1569-1802</identifier><identifier>DOI: 10.1016/j.matbio.2016.09.009</identifier><identifier>PMID: 27693454</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Angiogenesis ; Animals ; Autophagy ; Binding sites ; Binding-partners ; Cell surface ; Cells ; Collagen ; Collagen - physiology ; Decorin ; Decorin - physiology ; Extracellular matrix ; Extracellular Matrix - physiology ; Fibrillogenesis ; Glycosaminoglycans - physiology ; Growth factors ; Humans ; Leucine ; Matrix ; Molecules ; Phagocytosis ; Protein arrays ; Protein interaction ; Protein Interaction Maps ; Proteins ; Proteoglycan ; Proteoglycans - physiology ; Signal Transduction ; Tumorigenesis ; Wound healing</subject><ispartof>Matrix biology, 2016-09, Vol.55, p.7-21</ispartof><rights>2016</rights><rights>Copyright © 2016. Published by Elsevier B.V.</rights><rights>Copyright Elsevier Science Ltd. Sep 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c491t-e7502a288657168bf30ba8a8b78cf178306af1df92cb37e8722bce521933fad3</citedby><cites>FETCH-LOGICAL-c491t-e7502a288657168bf30ba8a8b78cf178306af1df92cb37e8722bce521933fad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0945053X16302268$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27693454$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gubbiotti, Maria A.</creatorcontrib><creatorcontrib>Vallet, Sylvain D.</creatorcontrib><creatorcontrib>Ricard-Blum, Sylvie</creatorcontrib><creatorcontrib>Iozzo, Renato V.</creatorcontrib><title>Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions</title><title>Matrix biology</title><addtitle>Matrix Biol</addtitle><description>Decorin, a prototype small leucine-rich proteoglycan, regulates a vast array of cellular processes including collagen fibrillogenesis, wound repair, angiostasis, tumor growth, and autophagy. This functional versatility arises from a wide array of decorin/protein interactions also including interactions with its single glycosaminoglycan side chain. The decorin-binding partners encompass numerous categories ranging from extracellular matrix molecules to cell surface receptors to growth factors and enzymes. Despite the diversity of the decorin interacting network, two main roles emerge as prominent themes in decorin function: maintenance of cellular structure and outside-in signaling, culminating in anti-tumorigenic effects. Here we present contemporary knowledge regarding the decorin interacting network and discuss in detail the biological relevance of these pleiotropic interactions, some of which could be targeted by therapeutic interventions.
•Decorin embraces a variety of binding partners branding it as a multi-purpose small, leucine-rich proteoglycan.•Structural integrity and cellular signaling are two prominent themes found in the decorin interactome.•Decorin anti-tumorigenic effects result from multiple concurrent interactions with receptor tyrosine kinases.•Emerging functions include angiostasis and autophagic induction.</description><subject>Angiogenesis</subject><subject>Animals</subject><subject>Autophagy</subject><subject>Binding sites</subject><subject>Binding-partners</subject><subject>Cell surface</subject><subject>Cells</subject><subject>Collagen</subject><subject>Collagen - physiology</subject><subject>Decorin</subject><subject>Decorin - physiology</subject><subject>Extracellular matrix</subject><subject>Extracellular Matrix - physiology</subject><subject>Fibrillogenesis</subject><subject>Glycosaminoglycans - physiology</subject><subject>Growth factors</subject><subject>Humans</subject><subject>Leucine</subject><subject>Matrix</subject><subject>Molecules</subject><subject>Phagocytosis</subject><subject>Protein arrays</subject><subject>Protein interaction</subject><subject>Protein Interaction Maps</subject><subject>Proteins</subject><subject>Proteoglycan</subject><subject>Proteoglycans - physiology</subject><subject>Signal Transduction</subject><subject>Tumorigenesis</subject><subject>Wound healing</subject><issn>0945-053X</issn><issn>1569-1802</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUuPFCEUhYnROO3oPzCGxI2bKnkUBbgwmYzPZBI3s3BHKOrWNG0VtEC1mX8vnR7Hx8IVueE7B-45CD2npKWE9q937WLL4GPL6tQS3RKiH6ANFb1uqCLsIdoQ3YmGCP71DD3JeUcI6TqpHqMzJnvNO9FtUHwHLiYfsA8FknXFhxscoPyI6dsbfIFdXPYJthCyPwC2wc632WccJzyehM3gw3gU7W0qAVKu0IjLFnzChzra4mfA0xqqdQz5KXo02TnDs7vzHF1_eH99-am5-vLx8-XFVeM6TUsDUhBmmVK9kLRXw8TJYJVVg1RuolJx0tuJjpNmbuASlGRscCAY1ZxPduTn6O3Jdr8OC4wOQkl2NvvkF5tuTbTe_H0T_NbcxIOpuSihdDV4dWeQ4vcVcjGLzw7m2QaIazZUccE7TXRf0Zf_oLu4pppUNoxIKaQQVFaqO1EuxZwTTPefocQcCzU7cyrUHAs1RJtaaJW9-HORe9GvBn9vCjXNg4dksvMQHIw-gStmjP7_L_wEwAu2vQ</recordid><startdate>201609</startdate><enddate>201609</enddate><creator>Gubbiotti, Maria A.</creator><creator>Vallet, Sylvain D.</creator><creator>Ricard-Blum, Sylvie</creator><creator>Iozzo, Renato V.</creator><general>Elsevier B.V</general><general>Elsevier Science Ltd</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>201609</creationdate><title>Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions</title><author>Gubbiotti, Maria A. ; Vallet, Sylvain D. ; Ricard-Blum, Sylvie ; Iozzo, Renato V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-e7502a288657168bf30ba8a8b78cf178306af1df92cb37e8722bce521933fad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Angiogenesis</topic><topic>Animals</topic><topic>Autophagy</topic><topic>Binding sites</topic><topic>Binding-partners</topic><topic>Cell surface</topic><topic>Cells</topic><topic>Collagen</topic><topic>Collagen - physiology</topic><topic>Decorin</topic><topic>Decorin - physiology</topic><topic>Extracellular matrix</topic><topic>Extracellular Matrix - physiology</topic><topic>Fibrillogenesis</topic><topic>Glycosaminoglycans - physiology</topic><topic>Growth factors</topic><topic>Humans</topic><topic>Leucine</topic><topic>Matrix</topic><topic>Molecules</topic><topic>Phagocytosis</topic><topic>Protein arrays</topic><topic>Protein interaction</topic><topic>Protein Interaction Maps</topic><topic>Proteins</topic><topic>Proteoglycan</topic><topic>Proteoglycans - physiology</topic><topic>Signal Transduction</topic><topic>Tumorigenesis</topic><topic>Wound healing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gubbiotti, Maria A.</creatorcontrib><creatorcontrib>Vallet, Sylvain D.</creatorcontrib><creatorcontrib>Ricard-Blum, Sylvie</creatorcontrib><creatorcontrib>Iozzo, Renato V.</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>Matrix biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gubbiotti, Maria A.</au><au>Vallet, Sylvain D.</au><au>Ricard-Blum, Sylvie</au><au>Iozzo, Renato V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions</atitle><jtitle>Matrix biology</jtitle><addtitle>Matrix Biol</addtitle><date>2016-09</date><risdate>2016</risdate><volume>55</volume><spage>7</spage><epage>21</epage><pages>7-21</pages><issn>0945-053X</issn><eissn>1569-1802</eissn><abstract>Decorin, a prototype small leucine-rich proteoglycan, regulates a vast array of cellular processes including collagen fibrillogenesis, wound repair, angiostasis, tumor growth, and autophagy. This functional versatility arises from a wide array of decorin/protein interactions also including interactions with its single glycosaminoglycan side chain. The decorin-binding partners encompass numerous categories ranging from extracellular matrix molecules to cell surface receptors to growth factors and enzymes. Despite the diversity of the decorin interacting network, two main roles emerge as prominent themes in decorin function: maintenance of cellular structure and outside-in signaling, culminating in anti-tumorigenic effects. Here we present contemporary knowledge regarding the decorin interacting network and discuss in detail the biological relevance of these pleiotropic interactions, some of which could be targeted by therapeutic interventions.
•Decorin embraces a variety of binding partners branding it as a multi-purpose small, leucine-rich proteoglycan.•Structural integrity and cellular signaling are two prominent themes found in the decorin interactome.•Decorin anti-tumorigenic effects result from multiple concurrent interactions with receptor tyrosine kinases.•Emerging functions include angiostasis and autophagic induction.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>27693454</pmid><doi>10.1016/j.matbio.2016.09.009</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Angiogenesis Animals Autophagy Binding sites Binding-partners Cell surface Cells Collagen Collagen - physiology Decorin Decorin - physiology Extracellular matrix Extracellular Matrix - physiology Fibrillogenesis Glycosaminoglycans - physiology Growth factors Humans Leucine Matrix Molecules Phagocytosis Protein arrays Protein interaction Protein Interaction Maps Proteins Proteoglycan Proteoglycans - physiology Signal Transduction Tumorigenesis Wound healing |
title | Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions |
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