Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I
Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that catalyzes the sequential removal of dipeptides from the amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA libraries. The deduced amino acid sequence codes f...
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| Veröffentlicht in: | The Journal of biological chemistry 1997-04, Vol.272 (16), p.10695-10703 |
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| container_title | The Journal of biological chemistry |
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| creator | Pham, C T Armstrong, R J Zimonjic, D B Popescu, N C Payan, D G Ley, T J |
| description | Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that catalyzes the sequential removal of dipeptides from the
amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA
libraries. The deduced amino acid sequence codes for a protein of 462 amino acid residues; comparison of this deduced sequence
with that of rat and human DPPI revealed 90.1% and 77.8% identity, respectively. Using DPPI cDNA, we obtained two BAC (Bacterial
Artificial Chromosome) clones that contained the murine DPPI locus. The DPPI gene consists of seven exons and 6 introns, and
spans approximately 20 kilobases. Using fluorescence in situ chromosome hybridization, we localized murine DPPI to chromosome 7D3-E1.1. We determined that DPPI protein is widely distributed
in mouse tissues, although its relative abundance varies from tissue to tissue. In contrast to previous reports, we show here
that DPPI mRNA and protein levels and enzymatic activity are unchanged during in vitro T cell activation, implying that this enzyme is not rate-limiting for granzyme processing. |
| doi_str_mv | 10.1074/jbc.272.16.10695 |
| format | Article |
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amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA
libraries. The deduced amino acid sequence codes for a protein of 462 amino acid residues; comparison of this deduced sequence
with that of rat and human DPPI revealed 90.1% and 77.8% identity, respectively. Using DPPI cDNA, we obtained two BAC (Bacterial
Artificial Chromosome) clones that contained the murine DPPI locus. The DPPI gene consists of seven exons and 6 introns, and
spans approximately 20 kilobases. Using fluorescence in situ chromosome hybridization, we localized murine DPPI to chromosome 7D3-E1.1. We determined that DPPI protein is widely distributed
in mouse tissues, although its relative abundance varies from tissue to tissue. In contrast to previous reports, we show here
that DPPI mRNA and protein levels and enzymatic activity are unchanged during in vitro T cell activation, implying that this enzyme is not rate-limiting for granzyme processing.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.272.16.10695</identifier><identifier>PMID: 9099719</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Cathepsin C ; Cathepsins - chemistry ; Chromosome Mapping ; Cloning, Molecular ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - biosynthesis ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics ; DNA, Complementary ; Exons ; Gene Library ; Humans ; In Situ Hybridization, Fluorescence ; Introns ; Karyotyping ; Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Rats ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Restriction Mapping ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; Spleen - enzymology ; T-Lymphocytes - enzymology ; T-Lymphocytes - immunology ; Thymus Gland - enzymology</subject><ispartof>The Journal of biological chemistry, 1997-04, Vol.272 (16), p.10695-10703</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-9a0d1e21341d1f54250bf57d03ba60c75dc2544b4fcc336db04f3748f5fe689a3</citedby><cites>FETCH-LOGICAL-c462t-9a0d1e21341d1f54250bf57d03ba60c75dc2544b4fcc336db04f3748f5fe689a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9099719$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pham, C T</creatorcontrib><creatorcontrib>Armstrong, R J</creatorcontrib><creatorcontrib>Zimonjic, D B</creatorcontrib><creatorcontrib>Popescu, N C</creatorcontrib><creatorcontrib>Payan, D G</creatorcontrib><creatorcontrib>Ley, T J</creatorcontrib><title>Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that catalyzes the sequential removal of dipeptides from the
amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA
libraries. The deduced amino acid sequence codes for a protein of 462 amino acid residues; comparison of this deduced sequence
with that of rat and human DPPI revealed 90.1% and 77.8% identity, respectively. Using DPPI cDNA, we obtained two BAC (Bacterial
Artificial Chromosome) clones that contained the murine DPPI locus. The DPPI gene consists of seven exons and 6 introns, and
spans approximately 20 kilobases. Using fluorescence in situ chromosome hybridization, we localized murine DPPI to chromosome 7D3-E1.1. We determined that DPPI protein is widely distributed
in mouse tissues, although its relative abundance varies from tissue to tissue. In contrast to previous reports, we show here
that DPPI mRNA and protein levels and enzymatic activity are unchanged during in vitro T cell activation, implying that this enzyme is not rate-limiting for granzyme processing.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cathepsin C</subject><subject>Cathepsins - chemistry</subject><subject>Chromosome Mapping</subject><subject>Cloning, Molecular</subject><subject>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - biosynthesis</subject><subject>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry</subject><subject>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics</subject><subject>DNA, Complementary</subject><subject>Exons</subject><subject>Gene Library</subject><subject>Humans</subject><subject>In Situ Hybridization, Fluorescence</subject><subject>Introns</subject><subject>Karyotyping</subject><subject>Lymphocyte Activation</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Rats</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spleen - enzymology</subject><subject>T-Lymphocytes - enzymology</subject><subject>T-Lymphocytes - immunology</subject><subject>Thymus Gland - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1PGzEQxa0KRMPHvZdKPiBO2dT22t71sQopRUpEDyBxQLK8Xps48q63dlZA_3pcEiFxYi4zT-_NO_wA-IbRDKOK_tg0ekYqMsM8ay7YFzDBqC6LkuH7AzBBiOBCEFZ_BccpbVAeKvAROBJIiAqLCXhYBW_06FWEcx961z9O4XwdQxdS6JSHy6CVd__U1oV-ClXfwsXzEE1KWcNg4WqMrjfw0g1m2Lr2xcM_b4dKBl6fgkOrfDJn-30C7n4tbue_i-XN1fX857LQlJNtIRRqsSG4pLjFllHCUGNZ1aKyURzpirWaMEobarUuS942iNqyorVl1vBaqPIEXOx6hxj-jiZtZeeSNt6r3oQxyaoWnLKafxrETFQZGclBtAvqGFKKxsohuk7FF4mR_E9eZvIyk5eYyzfy-eX7vntsOtO-P-xRZ_9856_d4_rJRSMbF_TadB9rXgGJd4sK</recordid><startdate>19970418</startdate><enddate>19970418</enddate><creator>Pham, C T</creator><creator>Armstrong, R J</creator><creator>Zimonjic, D B</creator><creator>Popescu, N C</creator><creator>Payan, D G</creator><creator>Ley, T J</creator><general>American Society for Biochemistry and Molecular Biology</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19970418</creationdate><title>Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I</title><author>Pham, C T ; Armstrong, R J ; Zimonjic, D B ; Popescu, N C ; Payan, D G ; Ley, T J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-9a0d1e21341d1f54250bf57d03ba60c75dc2544b4fcc336db04f3748f5fe689a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cathepsin C</topic><topic>Cathepsins - chemistry</topic><topic>Chromosome Mapping</topic><topic>Cloning, Molecular</topic><topic>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - biosynthesis</topic><topic>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry</topic><topic>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics</topic><topic>DNA, Complementary</topic><topic>Exons</topic><topic>Gene Library</topic><topic>Humans</topic><topic>In Situ Hybridization, Fluorescence</topic><topic>Introns</topic><topic>Karyotyping</topic><topic>Lymphocyte Activation</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Rats</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spleen - enzymology</topic><topic>T-Lymphocytes - enzymology</topic><topic>T-Lymphocytes - immunology</topic><topic>Thymus Gland - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pham, C T</creatorcontrib><creatorcontrib>Armstrong, R J</creatorcontrib><creatorcontrib>Zimonjic, D B</creatorcontrib><creatorcontrib>Popescu, N C</creatorcontrib><creatorcontrib>Payan, D G</creatorcontrib><creatorcontrib>Ley, T J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pham, C T</au><au>Armstrong, R J</au><au>Zimonjic, D B</au><au>Popescu, N C</au><au>Payan, D G</au><au>Ley, T J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1997-04-18</date><risdate>1997</risdate><volume>272</volume><issue>16</issue><spage>10695</spage><epage>10703</epage><pages>10695-10703</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that catalyzes the sequential removal of dipeptides from the
amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA
libraries. The deduced amino acid sequence codes for a protein of 462 amino acid residues; comparison of this deduced sequence
with that of rat and human DPPI revealed 90.1% and 77.8% identity, respectively. Using DPPI cDNA, we obtained two BAC (Bacterial
Artificial Chromosome) clones that contained the murine DPPI locus. The DPPI gene consists of seven exons and 6 introns, and
spans approximately 20 kilobases. Using fluorescence in situ chromosome hybridization, we localized murine DPPI to chromosome 7D3-E1.1. We determined that DPPI protein is widely distributed
in mouse tissues, although its relative abundance varies from tissue to tissue. In contrast to previous reports, we show here
that DPPI mRNA and protein levels and enzymatic activity are unchanged during in vitro T cell activation, implying that this enzyme is not rate-limiting for granzyme processing.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9099719</pmid><doi>10.1074/jbc.272.16.10695</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1997-04, Vol.272 (16), p.10695-10703 |
| issn | 0021-9258 1083-351X |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Cathepsin C Cathepsins - chemistry Chromosome Mapping Cloning, Molecular Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - biosynthesis Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - genetics DNA, Complementary Exons Gene Library Humans In Situ Hybridization, Fluorescence Introns Karyotyping Lymphocyte Activation Mice Molecular Sequence Data Rats Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Restriction Mapping RNA, Messenger - metabolism Sequence Homology, Amino Acid Spleen - enzymology T-Lymphocytes - enzymology T-Lymphocytes - immunology Thymus Gland - enzymology |
| title | Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I |
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