Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV: Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV
Hemorphins are endogenous peptides belonging to the family of “atypical” opioid peptides released from sequentially hydrolyzed hemoglobin. In this paper, we report an inhibitory effect of these peptides on dipeptidyl peptidase IV (DPPIV) activity, known to be involved in regulatory functions such as...
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| Veröffentlicht in: | Biochimie 2004, Vol.86 (1), p.31-37 |
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| creator | Cohen, M Fruitier-Arnaudin, I Piot, J.M |
| description | Hemorphins are endogenous peptides belonging to the family of “atypical” opioid peptides released from sequentially hydrolyzed hemoglobin. In this paper, we report an inhibitory effect of these peptides on dipeptidyl peptidase IV (DPPIV) activity, known to be involved in regulatory functions such as the activation or inactivation of peptides. The structure activity research revealed that hemorphins N-terminus sequence influences nature of the interaction between hemorphins and DPPIV. Kinetic studies conducted with purified DPPIV demonstrated that hemorphin-7 (H7) constitutes a good substrate (
K
cat/
K
m of 137 mM
–1 s
–1) for this enzyme but could also act as a selective competitive inhibitor by substrate binding site competition. These blood-derived peptides could represent endogenous regulators of this enzyme activity. |
| doi_str_mv | 10.1016/j.biochi.2003.11.001 |
| format | Article |
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K
cat/
K
m of 137 mM
–1 s
–1) for this enzyme but could also act as a selective competitive inhibitor by substrate binding site competition. These blood-derived peptides could represent endogenous regulators of this enzyme activity.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2003.11.001</identifier><identifier>PMID: 14987798</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>Animals ; Dipeptidyl Peptidase 4 - chemistry ; Dipeptidyl Peptidase 4 - metabolism ; Dipeptidyl peptidase IV, DPPIV ; Enzyme Activation - drug effects ; Enzyme Inhibitors - metabolism ; Enzyme Inhibitors - pharmacology ; Hemoglobins - chemistry ; Hemoglobins - metabolism ; Hemoglobins - pharmacology ; Hemorphin ; Inhibition study ; Kidney - enzymology ; Kinetic study ; Male ; Microsomes - enzymology ; Peptide Fragments - metabolism ; Peptide Fragments - pharmacology ; Peptide hydrolysis ; Protein Binding ; Rats ; Rats, Wistar ; Substrate Specificity</subject><ispartof>Biochimie, 2004, Vol.86 (1), p.31-37</ispartof><rights>2003 Éditions scientifiques et médicales Elsevier SAS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.biochi.2003.11.001$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,4012,27910,27911,27912,45982</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14987798$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cohen, M</creatorcontrib><creatorcontrib>Fruitier-Arnaudin, I</creatorcontrib><creatorcontrib>Piot, J.M</creatorcontrib><title>Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV: Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Hemorphins are endogenous peptides belonging to the family of “atypical” opioid peptides released from sequentially hydrolyzed hemoglobin. In this paper, we report an inhibitory effect of these peptides on dipeptidyl peptidase IV (DPPIV) activity, known to be involved in regulatory functions such as the activation or inactivation of peptides. The structure activity research revealed that hemorphins N-terminus sequence influences nature of the interaction between hemorphins and DPPIV. Kinetic studies conducted with purified DPPIV demonstrated that hemorphin-7 (H7) constitutes a good substrate (
K
cat/
K
m of 137 mM
–1 s
–1) for this enzyme but could also act as a selective competitive inhibitor by substrate binding site competition. These blood-derived peptides could represent endogenous regulators of this enzyme activity.</description><subject>Animals</subject><subject>Dipeptidyl Peptidase 4 - chemistry</subject><subject>Dipeptidyl Peptidase 4 - metabolism</subject><subject>Dipeptidyl peptidase IV, DPPIV</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Hemoglobins - chemistry</subject><subject>Hemoglobins - metabolism</subject><subject>Hemoglobins - pharmacology</subject><subject>Hemorphin</subject><subject>Inhibition study</subject><subject>Kidney - enzymology</subject><subject>Kinetic study</subject><subject>Male</subject><subject>Microsomes - enzymology</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Fragments - pharmacology</subject><subject>Peptide hydrolysis</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Substrate Specificity</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkcFu1DAURS0EokPhDxDyil3S59iTOF0goULpSBV0Ad1advyieJTEwXZA_Rj-tR6lqKt3n3V0fe1LyHsGJQNWXxxL43w3uLIC4CVjJQB7QXas5rKomeQvyQ44QNGCFGfkTYxHANhD1b4mZ0y0smlauSP_bnDyYRncHC9pXE1MQSeMVM_2wgfq5sEZl3yI1PfUugWX5OzDSDehI9LD_SV9NqHfi4RhcvMaacTfK84dZpd-3JSfaRpOBxnSXXJ5N5j-Is50ePbIl9Mvd3eH-7fkVa_HiO-e5jn5df3159VNcfvj2-Hq822BVV2lQggDrBG1bEC2ewmQtTFgBGslaw3ypuvrltveCltLI7SWQkDT9Lba1xJ7fk4-br5L8DlzTGpyscNx1DP6NaqG1ZKB5Bn88ASuZkKrluAmHR7U_w_NwKcNwBz3j8OgYudOT7cuYJeU9U4xUKcG1VFtDapTg4oxlRvkj3XxkbI</recordid><startdate>2004</startdate><enddate>2004</enddate><creator>Cohen, M</creator><creator>Fruitier-Arnaudin, I</creator><creator>Piot, J.M</creator><general>Elsevier Masson SAS</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>2004</creationdate><title>Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV: Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV</title><author>Cohen, M ; Fruitier-Arnaudin, I ; Piot, J.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e262t-44b01746870895800746bb0b419819be37cf693dfd4d68b4aa844077fd2568ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Dipeptidyl Peptidase 4 - chemistry</topic><topic>Dipeptidyl Peptidase 4 - metabolism</topic><topic>Dipeptidyl peptidase IV, DPPIV</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzyme Inhibitors - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Hemoglobins - chemistry</topic><topic>Hemoglobins - metabolism</topic><topic>Hemoglobins - pharmacology</topic><topic>Hemorphin</topic><topic>Inhibition study</topic><topic>Kidney - enzymology</topic><topic>Kinetic study</topic><topic>Male</topic><topic>Microsomes - enzymology</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Fragments - pharmacology</topic><topic>Peptide hydrolysis</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cohen, M</creatorcontrib><creatorcontrib>Fruitier-Arnaudin, I</creatorcontrib><creatorcontrib>Piot, J.M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cohen, M</au><au>Fruitier-Arnaudin, I</au><au>Piot, J.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV: Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2004</date><risdate>2004</risdate><volume>86</volume><issue>1</issue><spage>31</spage><epage>37</epage><pages>31-37</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>Hemorphins are endogenous peptides belonging to the family of “atypical” opioid peptides released from sequentially hydrolyzed hemoglobin. In this paper, we report an inhibitory effect of these peptides on dipeptidyl peptidase IV (DPPIV) activity, known to be involved in regulatory functions such as the activation or inactivation of peptides. The structure activity research revealed that hemorphins N-terminus sequence influences nature of the interaction between hemorphins and DPPIV. Kinetic studies conducted with purified DPPIV demonstrated that hemorphin-7 (H7) constitutes a good substrate (
K
cat/
K
m of 137 mM
–1 s
–1) for this enzyme but could also act as a selective competitive inhibitor by substrate binding site competition. These blood-derived peptides could represent endogenous regulators of this enzyme activity.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>14987798</pmid><doi>10.1016/j.biochi.2003.11.001</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-9084 |
| ispartof | Biochimie, 2004, Vol.86 (1), p.31-37 |
| issn | 0300-9084 1638-6183 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Dipeptidyl Peptidase 4 - chemistry Dipeptidyl Peptidase 4 - metabolism Dipeptidyl peptidase IV, DPPIV Enzyme Activation - drug effects Enzyme Inhibitors - metabolism Enzyme Inhibitors - pharmacology Hemoglobins - chemistry Hemoglobins - metabolism Hemoglobins - pharmacology Hemorphin Inhibition study Kidney - enzymology Kinetic study Male Microsomes - enzymology Peptide Fragments - metabolism Peptide Fragments - pharmacology Peptide hydrolysis Protein Binding Rats Rats, Wistar Substrate Specificity |
| title | Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV: Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV |
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