Wound healing activity of a collagen-derived cryptic peptide
Wound healing involves a well-controlled series of interactions among cells and several mediators leading to the restoration of damaged tissue. Degradation of the extracellular matrix (ECM) protein collagen during remodelling of wound tissue leads to the release of bioactive peptides that can possib...
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| Veröffentlicht in: | Amino acids 2015-02, Vol.47 (2), p.317-328 |
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| creator | Banerjee, Pradipta Suguna, Lonchin Shanthi, C |
| description | Wound healing involves a well-controlled series of interactions among cells and several mediators leading to the restoration of damaged tissue. Degradation of the extracellular matrix (ECM) protein collagen during remodelling of wound tissue leads to the release of bioactive peptides that can possibly influence the healing process. The RGD-containing, antioxidative collagen peptide E1 isolated in an earlier work was screened in this study for its ability to influence multiple steps of the wound healing process. E1 was assayed for and found to be chemotactic. Excision and incision wounds were created on separate groups of rats and E1 was administered topically. The wound tissues were isolated on the 4th and 8th days post-wound and subjected to biochemical and biophysical analysis. A significant decrease in lipid peroxides in the treatment group confirmed the in vivo antioxidant capacity of E1. The treatment group also displayed significant increase in total protein, collagen and amino sugar synthesis indicating faster ECM formation. The significantly increased rate of wound contraction and reepithelialisation along with higher tensile strength of the wound tissue corroborated the results of biochemical analysis. The results confirm the significant role played by collagen peptides in accelerating the healing process and justify their possible use as a pharmaceutical agent. |
| doi_str_mv | 10.1007/s00726-014-1860-6 |
| format | Article |
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Degradation of the extracellular matrix (ECM) protein collagen during remodelling of wound tissue leads to the release of bioactive peptides that can possibly influence the healing process. The RGD-containing, antioxidative collagen peptide E1 isolated in an earlier work was screened in this study for its ability to influence multiple steps of the wound healing process. E1 was assayed for and found to be chemotactic. Excision and incision wounds were created on separate groups of rats and E1 was administered topically. The wound tissues were isolated on the 4th and 8th days post-wound and subjected to biochemical and biophysical analysis. A significant decrease in lipid peroxides in the treatment group confirmed the in vivo antioxidant capacity of E1. The treatment group also displayed significant increase in total protein, collagen and amino sugar synthesis indicating faster ECM formation. The significantly increased rate of wound contraction and reepithelialisation along with higher tensile strength of the wound tissue corroborated the results of biochemical analysis. The results confirm the significant role played by collagen peptides in accelerating the healing process and justify their possible use as a pharmaceutical agent.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-014-1860-6</identifier><identifier>PMID: 25385312</identifier><language>eng</language><publisher>Vienna: Springer-Verlag</publisher><subject>amino sugars ; Analytical Chemistry ; Animals ; antioxidant activity ; Biochemical Engineering ; Biochemistry ; Biocompatibility ; Biomedical and Life Sciences ; chemotaxis ; collagen ; Collagen - chemistry ; Collagens ; Electrochemical machining ; excision ; extracellular matrix ; Healing ; Life Sciences ; Male ; Neurobiology ; Original Article ; Peptides ; Peptides - chemistry ; Peptides - pharmacology ; peroxides ; protein content ; Proteins ; Proteomics ; Rats ; Rats, Wistar ; Restoration ; tensile strength ; tissue ; tissue repair ; tissues ; Wound healing ; Wound Healing - drug effects ; wounds ; Wounds, Penetrating - drug therapy ; Wounds, Penetrating - metabolism ; Wounds, Penetrating - pathology</subject><ispartof>Amino acids, 2015-02, Vol.47 (2), p.317-328</ispartof><rights>Springer-Verlag Wien 2014</rights><rights>Springer-Verlag Wien 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-e06de47373f2cf9cf1fc984750d95978762abaa66b95ac10c749a0bd6384c8d03</citedby><cites>FETCH-LOGICAL-c499t-e06de47373f2cf9cf1fc984750d95978762abaa66b95ac10c749a0bd6384c8d03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00726-014-1860-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00726-014-1860-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27928,27929,41492,42561,51323</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25385312$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Banerjee, Pradipta</creatorcontrib><creatorcontrib>Suguna, Lonchin</creatorcontrib><creatorcontrib>Shanthi, C</creatorcontrib><title>Wound healing activity of a collagen-derived cryptic peptide</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>Wound healing involves a well-controlled series of interactions among cells and several mediators leading to the restoration of damaged tissue. Degradation of the extracellular matrix (ECM) protein collagen during remodelling of wound tissue leads to the release of bioactive peptides that can possibly influence the healing process. The RGD-containing, antioxidative collagen peptide E1 isolated in an earlier work was screened in this study for its ability to influence multiple steps of the wound healing process. E1 was assayed for and found to be chemotactic. Excision and incision wounds were created on separate groups of rats and E1 was administered topically. The wound tissues were isolated on the 4th and 8th days post-wound and subjected to biochemical and biophysical analysis. A significant decrease in lipid peroxides in the treatment group confirmed the in vivo antioxidant capacity of E1. The treatment group also displayed significant increase in total protein, collagen and amino sugar synthesis indicating faster ECM formation. The significantly increased rate of wound contraction and reepithelialisation along with higher tensile strength of the wound tissue corroborated the results of biochemical analysis. The results confirm the significant role played by collagen peptides in accelerating the healing process and justify their possible use as a pharmaceutical agent.</description><subject>amino sugars</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>antioxidant activity</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biocompatibility</subject><subject>Biomedical and Life Sciences</subject><subject>chemotaxis</subject><subject>collagen</subject><subject>Collagen - chemistry</subject><subject>Collagens</subject><subject>Electrochemical machining</subject><subject>excision</subject><subject>extracellular matrix</subject><subject>Healing</subject><subject>Life Sciences</subject><subject>Male</subject><subject>Neurobiology</subject><subject>Original Article</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>peroxides</subject><subject>protein content</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Restoration</subject><subject>tensile strength</subject><subject>tissue</subject><subject>tissue repair</subject><subject>tissues</subject><subject>Wound healing</subject><subject>Wound Healing - drug effects</subject><subject>wounds</subject><subject>Wounds, Penetrating - drug therapy</subject><subject>Wounds, Penetrating - metabolism</subject><subject>Wounds, Penetrating - pathology</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkUtrGzEUhUVpiJ3HD-imHcgmG6X36jUSdBNC0hYCWaQhSyFLGneCPeNIMwH_-8iMW0oXIRvdhb5z7pEOIZ8QLhCg_prLwRQFFBS1Aqo-kDkKrilDYz6SORhuqBASZ-Qo5ycAZBrVIZkxybXkyObk22M_dqH6Hd2q7ZaV80P70g7bqm8qV_l-tXLL2NEQU_sSQ-XTdjO0vtrEMkI8IQeNW-V4up_H5OHm-tfVD3p79_3n1eUt9cKYgUZQIYqa17xhvjG-wcYbLWoJwUhT61oxt3BOqYWRziP4WhgHi6C4Fl4H4MfkfPLdpP55jHmw6zb7WMJ1sR-zRaWMVgJAvgOVTCAiNwU9-w996sfUlYcUqsRFqWC3GyfKpz7nFBu7Se3apa1FsLsW7NSCLS3YXQtWFc3nvfO4WMfwV_Hn2wvAJiCXq24Z0z-r33D9Moka11u3TG22D_cMsKQErIVk_BWm3Zjv</recordid><startdate>20150201</startdate><enddate>20150201</enddate><creator>Banerjee, Pradipta</creator><creator>Suguna, Lonchin</creator><creator>Shanthi, C</creator><general>Springer-Verlag</general><general>Springer Vienna</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>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>20150201</creationdate><title>Wound healing activity of a collagen-derived cryptic peptide</title><author>Banerjee, Pradipta ; Suguna, Lonchin ; Shanthi, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-e06de47373f2cf9cf1fc984750d95978762abaa66b95ac10c749a0bd6384c8d03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>amino sugars</topic><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>antioxidant activity</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biocompatibility</topic><topic>Biomedical and Life Sciences</topic><topic>chemotaxis</topic><topic>collagen</topic><topic>Collagen - chemistry</topic><topic>Collagens</topic><topic>Electrochemical machining</topic><topic>excision</topic><topic>extracellular matrix</topic><topic>Healing</topic><topic>Life Sciences</topic><topic>Male</topic><topic>Neurobiology</topic><topic>Original Article</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>peroxides</topic><topic>protein content</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Restoration</topic><topic>tensile strength</topic><topic>tissue</topic><topic>tissue repair</topic><topic>tissues</topic><topic>Wound healing</topic><topic>Wound Healing - drug effects</topic><topic>wounds</topic><topic>Wounds, Penetrating - drug therapy</topic><topic>Wounds, Penetrating - metabolism</topic><topic>Wounds, Penetrating - pathology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Banerjee, Pradipta</creatorcontrib><creatorcontrib>Suguna, Lonchin</creatorcontrib><creatorcontrib>Shanthi, C</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Banerjee, Pradipta</au><au>Suguna, Lonchin</au><au>Shanthi, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Wound healing activity of a collagen-derived cryptic peptide</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2015-02-01</date><risdate>2015</risdate><volume>47</volume><issue>2</issue><spage>317</spage><epage>328</epage><pages>317-328</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>Wound healing involves a well-controlled series of interactions among cells and several mediators leading to the restoration of damaged tissue. Degradation of the extracellular matrix (ECM) protein collagen during remodelling of wound tissue leads to the release of bioactive peptides that can possibly influence the healing process. The RGD-containing, antioxidative collagen peptide E1 isolated in an earlier work was screened in this study for its ability to influence multiple steps of the wound healing process. E1 was assayed for and found to be chemotactic. Excision and incision wounds were created on separate groups of rats and E1 was administered topically. The wound tissues were isolated on the 4th and 8th days post-wound and subjected to biochemical and biophysical analysis. A significant decrease in lipid peroxides in the treatment group confirmed the in vivo antioxidant capacity of E1. The treatment group also displayed significant increase in total protein, collagen and amino sugar synthesis indicating faster ECM formation. The significantly increased rate of wound contraction and reepithelialisation along with higher tensile strength of the wound tissue corroborated the results of biochemical analysis. The results confirm the significant role played by collagen peptides in accelerating the healing process and justify their possible use as a pharmaceutical agent.</abstract><cop>Vienna</cop><pub>Springer-Verlag</pub><pmid>25385312</pmid><doi>10.1007/s00726-014-1860-6</doi><tpages>12</tpages></addata></record> |
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| subjects | amino sugars Analytical Chemistry Animals antioxidant activity Biochemical Engineering Biochemistry Biocompatibility Biomedical and Life Sciences chemotaxis collagen Collagen - chemistry Collagens Electrochemical machining excision extracellular matrix Healing Life Sciences Male Neurobiology Original Article Peptides Peptides - chemistry Peptides - pharmacology peroxides protein content Proteins Proteomics Rats Rats, Wistar Restoration tensile strength tissue tissue repair tissues Wound healing Wound Healing - drug effects wounds Wounds, Penetrating - drug therapy Wounds, Penetrating - metabolism Wounds, Penetrating - pathology |
| title | Wound healing activity of a collagen-derived cryptic peptide |
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