Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides
Dipeptidyl peptidase IV (DPPIV, EC 3.4.14.5) is a serine type protease with an important modulatory activity on a number of chemokines, neuropeptides and peptide hormones. It is also known as CD26 or adenosine deaminase (ADA; EC 3.5.4.4) binding protein. DPPIV has been demonstrated on the plasmamemb...
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| Veröffentlicht in: | European journal of biochemistry 2000-09, Vol.267 (17), p.5608-5613 |
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| container_title | European journal of biochemistry |
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| creator | Durinx, C Lambeir, A M Bosmans, E Falmagne, J B Berghmans, R Haemers, A Scharpé, S De Meester, I |
| description | Dipeptidyl peptidase IV (DPPIV, EC 3.4.14.5) is a serine type protease with an important modulatory activity on a number of chemokines, neuropeptides and peptide hormones. It is also known as CD26 or adenosine deaminase (ADA; EC 3.5.4.4) binding protein. DPPIV has been demonstrated on the plasmamembranes of T cells and activated natural killer or B cells as well as on a number of endothelial and differentiated epithelial cells. A soluble form of CD26/DPPIV has been described in serum. Over the past few years, several related enzymes with similar dipeptidyl peptidase activity have been discovered, raising questions on the molecular origin(s) of serum dipeptidyl peptidase activity. Among them attractin, the human orthologue of the mouse mahogany protein, was postulated to be responsible for the majority of the DPPIV-like activity in serum. Using ADA-affinity chromatography, it is shown here that 95% of the serum dipeptidyl peptidase activity is associated with a protein with ADA-binding properties. The natural protein was purified in milligram quantities, allowing molecular characterization (N-terminal sequence, glycosylation type, CD-spectrum, pH and thermal stability) and comparison with CD26/DPPIV from other sources. The purified serum enzyme was confirmed as CD26. |
| doi_str_mv | 10.1046/j.1432-1327.2000.01634.x |
| format | Article |
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It is also known as CD26 or adenosine deaminase (ADA; EC 3.5.4.4) binding protein. DPPIV has been demonstrated on the plasmamembranes of T cells and activated natural killer or B cells as well as on a number of endothelial and differentiated epithelial cells. A soluble form of CD26/DPPIV has been described in serum. Over the past few years, several related enzymes with similar dipeptidyl peptidase activity have been discovered, raising questions on the molecular origin(s) of serum dipeptidyl peptidase activity. Among them attractin, the human orthologue of the mouse mahogany protein, was postulated to be responsible for the majority of the DPPIV-like activity in serum. Using ADA-affinity chromatography, it is shown here that 95% of the serum dipeptidyl peptidase activity is associated with a protein with ADA-binding properties. The natural protein was purified in milligram quantities, allowing molecular characterization (N-terminal sequence, glycosylation type, CD-spectrum, pH and thermal stability) and comparison with CD26/DPPIV from other sources. The purified serum enzyme was confirmed as CD26.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1046/j.1432-1327.2000.01634.x</identifier><identifier>PMID: 10951221</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Chromatography, Affinity ; Chromatography, Gel ; Circular Dichroism ; Dipeptides - chemistry ; Dipeptides - metabolism ; Dipeptidyl Peptidase 4 - blood ; Dipeptidyl Peptidase 4 - chemistry ; Dipeptidyl Peptidase 4 - isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Humans ; Molecular Sequence Data ; Proline - chemistry ; Recombinant Proteins - blood ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Semen - enzymology</subject><ispartof>European journal of biochemistry, 2000-09, Vol.267 (17), p.5608-5613</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c256t-a63b3af67c627d797900e43ef70f6a8e59ff9ce6d7eaff3db1669ecc7e97cd7f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10951221$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Durinx, C</creatorcontrib><creatorcontrib>Lambeir, A M</creatorcontrib><creatorcontrib>Bosmans, E</creatorcontrib><creatorcontrib>Falmagne, J B</creatorcontrib><creatorcontrib>Berghmans, R</creatorcontrib><creatorcontrib>Haemers, A</creatorcontrib><creatorcontrib>Scharpé, S</creatorcontrib><creatorcontrib>De Meester, I</creatorcontrib><title>Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Dipeptidyl peptidase IV (DPPIV, EC 3.4.14.5) is a serine type protease with an important modulatory activity on a number of chemokines, neuropeptides and peptide hormones. It is also known as CD26 or adenosine deaminase (ADA; EC 3.5.4.4) binding protein. DPPIV has been demonstrated on the plasmamembranes of T cells and activated natural killer or B cells as well as on a number of endothelial and differentiated epithelial cells. A soluble form of CD26/DPPIV has been described in serum. Over the past few years, several related enzymes with similar dipeptidyl peptidase activity have been discovered, raising questions on the molecular origin(s) of serum dipeptidyl peptidase activity. Among them attractin, the human orthologue of the mouse mahogany protein, was postulated to be responsible for the majority of the DPPIV-like activity in serum. Using ADA-affinity chromatography, it is shown here that 95% of the serum dipeptidyl peptidase activity is associated with a protein with ADA-binding properties. The natural protein was purified in milligram quantities, allowing molecular characterization (N-terminal sequence, glycosylation type, CD-spectrum, pH and thermal stability) and comparison with CD26/DPPIV from other sources. The purified serum enzyme was confirmed as CD26.</description><subject>Amino Acid Sequence</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>Circular Dichroism</subject><subject>Dipeptides - chemistry</subject><subject>Dipeptides - metabolism</subject><subject>Dipeptidyl Peptidase 4 - blood</subject><subject>Dipeptidyl Peptidase 4 - chemistry</subject><subject>Dipeptidyl Peptidase 4 - isolation & purification</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Proline - chemistry</subject><subject>Recombinant Proteins - blood</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Semen - enzymology</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkctu2zAQRYmiReO4_YWCq-wk8yGTZnaBmxeQoFmkRXcERQ0RGrSpklJg91_6r5EiI-giKw44585dHIQwJSUllVhsSlpxVlDOZMkIISWhglfl_gOaTQvC-Uc0I4RWBVNLcYJOc94MoFBCfkYnlKglZYzO0L_7GMD2wSRsn0wytoPk_5rOxx2ODje-hbbzzSHgaTAZ8AD5Z98dsN_hDKnfnuMcQ18HwOvvTCzeDd3-wj7jBLmNu-xH1sWEuycY_gKMxFD3u3hI8a0U8hf0yZmQ4evxnaOfV5eP65vi7sf17frirrBsKbrCCF5z44S0gslGKqkIgYqDk8QJs4Klck5ZEI0E4xxvaiqEAmslKGkb6fgcnU132xT_9JA7vfXZQghmB7HPWjKqFFVyAFcTaFPMOYHTbfJbkw6aEj2q0Rs9GtCjGj2q0a9q9H6Ifjt29PUWmv-Ckwv-Andij0s</recordid><startdate>20000901</startdate><enddate>20000901</enddate><creator>Durinx, C</creator><creator>Lambeir, A M</creator><creator>Bosmans, E</creator><creator>Falmagne, J B</creator><creator>Berghmans, R</creator><creator>Haemers, A</creator><creator>Scharpé, S</creator><creator>De Meester, I</creator><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>20000901</creationdate><title>Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides</title><author>Durinx, C ; 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It is also known as CD26 or adenosine deaminase (ADA; EC 3.5.4.4) binding protein. DPPIV has been demonstrated on the plasmamembranes of T cells and activated natural killer or B cells as well as on a number of endothelial and differentiated epithelial cells. A soluble form of CD26/DPPIV has been described in serum. Over the past few years, several related enzymes with similar dipeptidyl peptidase activity have been discovered, raising questions on the molecular origin(s) of serum dipeptidyl peptidase activity. Among them attractin, the human orthologue of the mouse mahogany protein, was postulated to be responsible for the majority of the DPPIV-like activity in serum. Using ADA-affinity chromatography, it is shown here that 95% of the serum dipeptidyl peptidase activity is associated with a protein with ADA-binding properties. 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| ispartof | European journal of biochemistry, 2000-09, Vol.267 (17), p.5608-5613 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Chromatography, Affinity Chromatography, Gel Circular Dichroism Dipeptides - chemistry Dipeptides - metabolism Dipeptidyl Peptidase 4 - blood Dipeptidyl Peptidase 4 - chemistry Dipeptidyl Peptidase 4 - isolation & purification Electrophoresis, Polyacrylamide Gel Humans Molecular Sequence Data Proline - chemistry Recombinant Proteins - blood Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Semen - enzymology |
| title | Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides |
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