Identification of a New Member of the Tryptase Family of Mouse and Human Mast Cell Proteases Which Possesses a Novel COOH-terminal Hydrophobic Extension
Mapping of the tryptase locus on chromosome 17 revealed a novel gene 2.3 kilobase 3′ of the mouse mast cell protease (mMCP) 6 gene. This 3.7-kilobase gene encodes the first example of a protease in the tryptase family that contains a membrane-spanning segment located at its COOH terminus. Comparativ...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-10, Vol.274 (43), p.30784-30793 |
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| container_title | The Journal of biological chemistry |
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| creator | Wong, Guang W. Tang, Yinzi Feyfant, Eric Šali, Andrej Li, Lixin Li, Yong Huang, Chifu Friend, Daniel S. Krilis, Steven A. Stevens, Richard L. |
| description | Mapping of the tryptase locus on chromosome 17 revealed a novel gene 2.3 kilobase 3′ of the mouse mast cell protease (mMCP) 6 gene. This 3.7-kilobase gene encodes the first example of a protease in the tryptase family that contains a membrane-spanning segment located at its COOH terminus. Comparative structural studies indicated that the putative transmembrane tryptase (TMT) possesses a unique substrate-binding cleft. As assessed by RNA blot analyses, mTMT is expressed in mice in both strain- and tissue-dependent manners. Thus, different transcriptional and/or post-transcriptional mechanisms are used to control the expression of mTMT in vivo. Analysis of the corresponding tryptase locus in the human genome resulted in the isolation and characterization of the hTMT gene. ThehTMT transcript is expressed in numerous tissues and is also translated. Analysis of the tryptase family of genes in mice and humans now indicates that a primordial serine protease gene duplicated early and often during the evolution of mammals to generate a panel of homologous tryptases in each species that differ in their tissue expression, substrate specificities, and physical properties. |
| doi_str_mv | 10.1074/jbc.274.43.30784 |
| format | Article |
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This 3.7-kilobase gene encodes the first example of a protease in the tryptase family that contains a membrane-spanning segment located at its COOH terminus. Comparative structural studies indicated that the putative transmembrane tryptase (TMT) possesses a unique substrate-binding cleft. As assessed by RNA blot analyses, mTMT is expressed in mice in both strain- and tissue-dependent manners. Thus, different transcriptional and/or post-transcriptional mechanisms are used to control the expression of mTMT in vivo. Analysis of the corresponding tryptase locus in the human genome resulted in the isolation and characterization of the hTMT gene. ThehTMT transcript is expressed in numerous tissues and is also translated. Analysis of the tryptase family of genes in mice and humans now indicates that a primordial serine protease gene duplicated early and often during the evolution of mammals to generate a panel of homologous tryptases in each species that differ in their tissue expression, substrate specificities, and physical properties.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.43.30784</identifier><identifier>PMID: 10521469</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Cell Membrane - enzymology ; chromosome 17 ; Chromosome Mapping ; Chymases ; Cloning, Molecular ; Female ; Genome, Human ; hTMT gene ; Humans ; Kinetics ; Male ; Mast Cells - enzymology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; mMCP6 gene ; Molecular Sequence Data ; mTMT gene ; Organ Specificity ; Protein Biosynthesis ; Recombinant Proteins - chemistry ; Restriction Mapping ; Sequence Alignment ; Sequence Homology, Amino Acid ; Serine Endopeptidases - chemistry ; Serine Endopeptidases - genetics ; serine proteinase ; Transcription, Genetic ; Tryptases</subject><ispartof>The Journal of biological chemistry, 1999-10, Vol.274 (43), p.30784-30793</ispartof><rights>1999 © 1999 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c448t-dd89ee4d793a3409964e0a4199fba8d1d245604e32366cf8334eab4b37b1bb503</citedby><cites>FETCH-LOGICAL-c448t-dd89ee4d793a3409964e0a4199fba8d1d245604e32366cf8334eab4b37b1bb503</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/10521469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wong, Guang W.</creatorcontrib><creatorcontrib>Tang, Yinzi</creatorcontrib><creatorcontrib>Feyfant, Eric</creatorcontrib><creatorcontrib>Šali, Andrej</creatorcontrib><creatorcontrib>Li, Lixin</creatorcontrib><creatorcontrib>Li, Yong</creatorcontrib><creatorcontrib>Huang, Chifu</creatorcontrib><creatorcontrib>Friend, Daniel S.</creatorcontrib><creatorcontrib>Krilis, Steven A.</creatorcontrib><creatorcontrib>Stevens, Richard L.</creatorcontrib><title>Identification of a New Member of the Tryptase Family of Mouse and Human Mast Cell Proteases Which Possesses a Novel COOH-terminal Hydrophobic Extension</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Mapping of the tryptase locus on chromosome 17 revealed a novel gene 2.3 kilobase 3′ of the mouse mast cell protease (mMCP) 6 gene. This 3.7-kilobase gene encodes the first example of a protease in the tryptase family that contains a membrane-spanning segment located at its COOH terminus. Comparative structural studies indicated that the putative transmembrane tryptase (TMT) possesses a unique substrate-binding cleft. As assessed by RNA blot analyses, mTMT is expressed in mice in both strain- and tissue-dependent manners. Thus, different transcriptional and/or post-transcriptional mechanisms are used to control the expression of mTMT in vivo. Analysis of the corresponding tryptase locus in the human genome resulted in the isolation and characterization of the hTMT gene. ThehTMT transcript is expressed in numerous tissues and is also translated. Analysis of the tryptase family of genes in mice and humans now indicates that a primordial serine protease gene duplicated early and often during the evolution of mammals to generate a panel of homologous tryptases in each species that differ in their tissue expression, substrate specificities, and physical properties.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cell Membrane - enzymology</subject><subject>chromosome 17</subject><subject>Chromosome Mapping</subject><subject>Chymases</subject><subject>Cloning, Molecular</subject><subject>Female</subject><subject>Genome, Human</subject><subject>hTMT gene</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Male</subject><subject>Mast Cells - enzymology</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Mice, Inbred C57BL</subject><subject>mMCP6 gene</subject><subject>Molecular Sequence Data</subject><subject>mTMT gene</subject><subject>Organ Specificity</subject><subject>Protein Biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Restriction Mapping</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - genetics</subject><subject>serine proteinase</subject><subject>Transcription, Genetic</subject><subject>Tryptases</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvEzEUhS1ERUNhzwp5gbqbYI89D7NDUUsqNU0XRbCz_LjDuJoZB9tpyT_h5-IwXSAkhDfWsb57dI8PQm8oWVLS8Pf32izLhi85WzLStPwZWlDSsoJV9OtztCCkpIUoq_YUvYzxnuTDBX2BTimpSsprsUA_ryxMyXXOqOT8hH2HFb6BR7yBUUM46tQDvguHXVIR8KUa3XA4Pm_8Pms1Wbzej2rCGxUTXsEw4NvgE2Q44i-9Mz2-9TGLo87W_gEGvNpu10WCMLpJDXh9sMHveq-dwRc_Ekwxb_IKnXRqiPD66T5Dny8v7lbr4nr76Wr18bownLepsLYVANw2ginGiRA1B6I4FaLTqrXUlryqCQdWsro2XcsYB6W5Zo2mWleEnaHz2XcX_Pc9xCRHF02OoSbICWVDWl42TftfkDa8amvBMkhm0IQcPEAnd8GNKhwkJfJYm8y1yVyb5Ez-ri2PvH3y3usR7B8Dc08ZeDcDvfvWP7oAUjtvehj_9vkwY5B_7MFBkNE4mAzYPGKStN79e4lfoy2zkw</recordid><startdate>19991022</startdate><enddate>19991022</enddate><creator>Wong, Guang W.</creator><creator>Tang, Yinzi</creator><creator>Feyfant, Eric</creator><creator>Šali, Andrej</creator><creator>Li, Lixin</creator><creator>Li, Yong</creator><creator>Huang, Chifu</creator><creator>Friend, Daniel S.</creator><creator>Krilis, Steven A.</creator><creator>Stevens, Richard L.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19991022</creationdate><title>Identification of a New Member of the Tryptase Family of Mouse and Human Mast Cell Proteases Which Possesses a Novel COOH-terminal Hydrophobic Extension</title><author>Wong, Guang W. ; Tang, Yinzi ; Feyfant, Eric ; Šali, Andrej ; Li, Lixin ; Li, Yong ; Huang, Chifu ; Friend, Daniel S. ; Krilis, Steven A. ; Stevens, Richard L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c448t-dd89ee4d793a3409964e0a4199fba8d1d245604e32366cf8334eab4b37b1bb503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cell Membrane - enzymology</topic><topic>chromosome 17</topic><topic>Chromosome Mapping</topic><topic>Chymases</topic><topic>Cloning, Molecular</topic><topic>Female</topic><topic>Genome, Human</topic><topic>hTMT gene</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Male</topic><topic>Mast Cells - enzymology</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Mice, Inbred C57BL</topic><topic>mMCP6 gene</topic><topic>Molecular Sequence Data</topic><topic>mTMT gene</topic><topic>Organ Specificity</topic><topic>Protein Biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Restriction Mapping</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Endopeptidases - genetics</topic><topic>serine proteinase</topic><topic>Transcription, Genetic</topic><topic>Tryptases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wong, Guang W.</creatorcontrib><creatorcontrib>Tang, Yinzi</creatorcontrib><creatorcontrib>Feyfant, Eric</creatorcontrib><creatorcontrib>Šali, Andrej</creatorcontrib><creatorcontrib>Li, Lixin</creatorcontrib><creatorcontrib>Li, Yong</creatorcontrib><creatorcontrib>Huang, Chifu</creatorcontrib><creatorcontrib>Friend, Daniel S.</creatorcontrib><creatorcontrib>Krilis, Steven A.</creatorcontrib><creatorcontrib>Stevens, Richard L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wong, Guang W.</au><au>Tang, Yinzi</au><au>Feyfant, Eric</au><au>Šali, Andrej</au><au>Li, Lixin</au><au>Li, Yong</au><au>Huang, Chifu</au><au>Friend, Daniel S.</au><au>Krilis, Steven A.</au><au>Stevens, Richard L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a New Member of the Tryptase Family of Mouse and Human Mast Cell Proteases Which Possesses a Novel COOH-terminal Hydrophobic Extension</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-10-22</date><risdate>1999</risdate><volume>274</volume><issue>43</issue><spage>30784</spage><epage>30793</epage><pages>30784-30793</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Mapping of the tryptase locus on chromosome 17 revealed a novel gene 2.3 kilobase 3′ of the mouse mast cell protease (mMCP) 6 gene. This 3.7-kilobase gene encodes the first example of a protease in the tryptase family that contains a membrane-spanning segment located at its COOH terminus. Comparative structural studies indicated that the putative transmembrane tryptase (TMT) possesses a unique substrate-binding cleft. As assessed by RNA blot analyses, mTMT is expressed in mice in both strain- and tissue-dependent manners. Thus, different transcriptional and/or post-transcriptional mechanisms are used to control the expression of mTMT in vivo. Analysis of the corresponding tryptase locus in the human genome resulted in the isolation and characterization of the hTMT gene. ThehTMT transcript is expressed in numerous tissues and is also translated. Analysis of the tryptase family of genes in mice and humans now indicates that a primordial serine protease gene duplicated early and often during the evolution of mammals to generate a panel of homologous tryptases in each species that differ in their tissue expression, substrate specificities, and physical properties.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10521469</pmid><doi>10.1074/jbc.274.43.30784</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Base Sequence Cell Membrane - enzymology chromosome 17 Chromosome Mapping Chymases Cloning, Molecular Female Genome, Human hTMT gene Humans Kinetics Male Mast Cells - enzymology Mice Mice, Inbred BALB C Mice, Inbred C57BL mMCP6 gene Molecular Sequence Data mTMT gene Organ Specificity Protein Biosynthesis Recombinant Proteins - chemistry Restriction Mapping Sequence Alignment Sequence Homology, Amino Acid Serine Endopeptidases - chemistry Serine Endopeptidases - genetics serine proteinase Transcription, Genetic Tryptases |
| title | Identification of a New Member of the Tryptase Family of Mouse and Human Mast Cell Proteases Which Possesses a Novel COOH-terminal Hydrophobic Extension |
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