Cloning of the cDNA and gene for mouse mast cell protease 4. Demonstration of its late transcription in mast cell subclasses and analysis of its homology to subclass-specific neutral proteases of the mouse and rat
Based on the amino-terminal amino acid sequence of the mature form of mouse mast cell protease 4 (MMCP-4), previously identified in peritoneal connective tissue mast cells (CTMC) and Kirsten sarcoma virus-immortalized mast cells (KiSV-MC), a 26-mer oligonucleotide probe was constructed and used to c...
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| Veröffentlicht in: | The Journal of biological chemistry 1991-01, Vol.266 (3), p.1934-1941 |
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| container_issue | 3 |
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| container_title | The Journal of biological chemistry |
| container_volume | 266 |
| creator | SERAFIN, W. E SULLIVAN, T. P CONDER, G. A EBRAHIMI, A MARCHAM, P JOHNSON, S. S AUSTEN, K. F REYNOLDS, D. S |
| description | Based on the amino-terminal amino acid sequence of the mature form of mouse mast cell protease 4 (MMCP-4), previously identified
in peritoneal connective tissue mast cells (CTMC) and Kirsten sarcoma virus-immortalized mast cells (KiSV-MC), a 26-mer oligonucleotide
probe was constructed and used to clone cDNAs for MMCP-4 from a KiSV-MC1 cDNA library. MMCP-4 is the first secretory granule
serine protease of CTMC to be molecularly cloned. Using a cDNA probe derived from the 3'-untranslated portion of the MMCP-4
cDNA, the gene for MMCP-4 and a second highly related gene (mouse mast cell protease-like, MMCP-L) were cloned from a BALB/c
mouse genomic DNA library and sequenced entirely, including approximately 2 kilobases of the 5'-flanking region. MMCP-4 and
MMCP-L have five exons of identical length, four introns of nearly identical length, and approximately 900 base pairs of 5'-flanking
DNA with sequence similarity by dot matrix analysis. By RNA blot analysis with gene-specific probes for MMCP-4 (bases 497-633
of the cDNA) and MMCP-L (bases 502-638 of the cDNA), mRNA for MMCP-4 was present in KiSV-MC5, CTMC, and the intestine of a
mouse infected with the parasite Nippostrongylus brasiliensis markedly enriched for mucosal mast cells (MMC); MMCP-L mRNA
was detected only in the intestine of the N. brasiliensis-infected mouse. MMCP-4 mRNA was not expressed in normal mouse intestine
or in interleukin 3-dependent bone marrow-derived mast cells, which can serve as precursors to both MMC and CTMC. This finding
suggests that MMCP-4 is transcribed relatively late in the development of both the CTMC and MMC subclasses and underscores
the fact that mouse bone-marrow-derived mast cells are immature mast cells, rather than tissue culture equivalents of the
MMC subclass. |
| doi_str_mv | 10.1016/S0021-9258(18)52383-8 |
| format | Article |
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in peritoneal connective tissue mast cells (CTMC) and Kirsten sarcoma virus-immortalized mast cells (KiSV-MC), a 26-mer oligonucleotide
probe was constructed and used to clone cDNAs for MMCP-4 from a KiSV-MC1 cDNA library. MMCP-4 is the first secretory granule
serine protease of CTMC to be molecularly cloned. Using a cDNA probe derived from the 3'-untranslated portion of the MMCP-4
cDNA, the gene for MMCP-4 and a second highly related gene (mouse mast cell protease-like, MMCP-L) were cloned from a BALB/c
mouse genomic DNA library and sequenced entirely, including approximately 2 kilobases of the 5'-flanking region. MMCP-4 and
MMCP-L have five exons of identical length, four introns of nearly identical length, and approximately 900 base pairs of 5'-flanking
DNA with sequence similarity by dot matrix analysis. By RNA blot analysis with gene-specific probes for MMCP-4 (bases 497-633
of the cDNA) and MMCP-L (bases 502-638 of the cDNA), mRNA for MMCP-4 was present in KiSV-MC5, CTMC, and the intestine of a
mouse infected with the parasite Nippostrongylus brasiliensis markedly enriched for mucosal mast cells (MMC); MMCP-L mRNA
was detected only in the intestine of the N. brasiliensis-infected mouse. MMCP-4 mRNA was not expressed in normal mouse intestine
or in interleukin 3-dependent bone marrow-derived mast cells, which can serve as precursors to both MMC and CTMC. This finding
suggests that MMCP-4 is transcribed relatively late in the development of both the CTMC and MMC subclasses and underscores
the fact that mouse bone-marrow-derived mast cells are immature mast cells, rather than tissue culture equivalents of the
MMC subclass.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)52383-8</identifier><identifier>PMID: 1988455</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Blotting, Northern ; Cloning, Molecular ; DNA - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Genes ; mast cells ; Mast Cells - enzymology ; Mice ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Oligonucleotides - chemistry ; Rats ; RNA, Messenger - genetics ; Serine Endopeptidases - genetics ; Transcription, Genetic</subject><ispartof>The Journal of biological chemistry, 1991-01, Vol.266 (3), p.1934-1941</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-ef93c11517303fb018d830efe00bfc579c143b6752b0011a2f4f015239e5f8df3</citedby><cites>FETCH-LOGICAL-c439t-ef93c11517303fb018d830efe00bfc579c143b6752b0011a2f4f015239e5f8df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19640186$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1988455$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SERAFIN, W. E</creatorcontrib><creatorcontrib>SULLIVAN, T. P</creatorcontrib><creatorcontrib>CONDER, G. A</creatorcontrib><creatorcontrib>EBRAHIMI, A</creatorcontrib><creatorcontrib>MARCHAM, P</creatorcontrib><creatorcontrib>JOHNSON, S. S</creatorcontrib><creatorcontrib>AUSTEN, K. F</creatorcontrib><creatorcontrib>REYNOLDS, D. S</creatorcontrib><title>Cloning of the cDNA and gene for mouse mast cell protease 4. Demonstration of its late transcription in mast cell subclasses and analysis of its homology to subclass-specific neutral proteases of the mouse and rat</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Based on the amino-terminal amino acid sequence of the mature form of mouse mast cell protease 4 (MMCP-4), previously identified
in peritoneal connective tissue mast cells (CTMC) and Kirsten sarcoma virus-immortalized mast cells (KiSV-MC), a 26-mer oligonucleotide
probe was constructed and used to clone cDNAs for MMCP-4 from a KiSV-MC1 cDNA library. MMCP-4 is the first secretory granule
serine protease of CTMC to be molecularly cloned. Using a cDNA probe derived from the 3'-untranslated portion of the MMCP-4
cDNA, the gene for MMCP-4 and a second highly related gene (mouse mast cell protease-like, MMCP-L) were cloned from a BALB/c
mouse genomic DNA library and sequenced entirely, including approximately 2 kilobases of the 5'-flanking region. MMCP-4 and
MMCP-L have five exons of identical length, four introns of nearly identical length, and approximately 900 base pairs of 5'-flanking
DNA with sequence similarity by dot matrix analysis. By RNA blot analysis with gene-specific probes for MMCP-4 (bases 497-633
of the cDNA) and MMCP-L (bases 502-638 of the cDNA), mRNA for MMCP-4 was present in KiSV-MC5, CTMC, and the intestine of a
mouse infected with the parasite Nippostrongylus brasiliensis markedly enriched for mucosal mast cells (MMC); MMCP-L mRNA
was detected only in the intestine of the N. brasiliensis-infected mouse. MMCP-4 mRNA was not expressed in normal mouse intestine
or in interleukin 3-dependent bone marrow-derived mast cells, which can serve as precursors to both MMC and CTMC. This finding
suggests that MMCP-4 is transcribed relatively late in the development of both the CTMC and MMC subclasses and underscores
the fact that mouse bone-marrow-derived mast cells are immature mast cells, rather than tissue culture equivalents of the
MMC subclass.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Cloning, Molecular</subject><subject>DNA - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Genes</subject><subject>mast cells</subject><subject>Mast Cells - enzymology</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Oligonucleotides - chemistry</subject><subject>Rats</subject><subject>RNA, Messenger - genetics</subject><subject>Serine Endopeptidases - genetics</subject><subject>Transcription, Genetic</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcuO1DAQRSMEGpqBTxjJQgLBIoMrjtPOctTDSxrBApDYWY673DFK7CaVCPWH8j84nZ7HDm9suU7duvbNsgvgl8CheveN8wLyupDqDai3shBK5OpRtgKeDkLCz8fZ6g55mj0j-sXTKms4y86gVqqUcpX93XQx-LBj0bGxRWavv1wxE7ZshwGZiwPr40TIekMjs9h1bD_EEU26Ki_ZNfYx0DiY0ccwS_iRWGdGZOkukB38_ljx4YEATY3tDBHScZAJpjuQp9v2Nvaxi7sDG-MdmtMerXfesoBTkr53QbfGF5uzYHLzPHviTEf44rSfZz8-vP---ZTffP34eXN1k9tS1GOOrhYWQMJacOEaDmqrBEeHnDfOynVtoRRNtZZFwzmAKVzpOKSvrlE6tXXiPHu96CY7vyekUfee5keagMmPVrwUXCr-XxDkjAIkUC6gHSLRgE7vB9-b4aCB6zl3fcxdz6FqUPqYu1ap7-I0YGp63N53LUGn-qtT3ZA1nUvxWE8PsKpMz68S93LhWr9r__gBdeOjbbHXRVVpkUBRin-yXMSx</recordid><startdate>19910125</startdate><enddate>19910125</enddate><creator>SERAFIN, W. E</creator><creator>SULLIVAN, T. P</creator><creator>CONDER, G. A</creator><creator>EBRAHIMI, A</creator><creator>MARCHAM, P</creator><creator>JOHNSON, S. S</creator><creator>AUSTEN, K. F</creator><creator>REYNOLDS, D. S</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19910125</creationdate><title>Cloning of the cDNA and gene for mouse mast cell protease 4. Demonstration of its late transcription in mast cell subclasses and analysis of its homology to subclass-specific neutral proteases of the mouse and rat</title><author>SERAFIN, W. E ; SULLIVAN, T. P ; CONDER, G. A ; EBRAHIMI, A ; MARCHAM, P ; JOHNSON, S. S ; AUSTEN, K. F ; REYNOLDS, D. S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-ef93c11517303fb018d830efe00bfc579c143b6752b0011a2f4f015239e5f8df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Cloning, Molecular</topic><topic>DNA - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Genes</topic><topic>mast cells</topic><topic>Mast Cells - enzymology</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Oligonucleotides - chemistry</topic><topic>Rats</topic><topic>RNA, Messenger - genetics</topic><topic>Serine Endopeptidases - genetics</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SERAFIN, W. E</creatorcontrib><creatorcontrib>SULLIVAN, T. P</creatorcontrib><creatorcontrib>CONDER, G. A</creatorcontrib><creatorcontrib>EBRAHIMI, A</creatorcontrib><creatorcontrib>MARCHAM, P</creatorcontrib><creatorcontrib>JOHNSON, S. S</creatorcontrib><creatorcontrib>AUSTEN, K. F</creatorcontrib><creatorcontrib>REYNOLDS, D. 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P</au><au>CONDER, G. A</au><au>EBRAHIMI, A</au><au>MARCHAM, P</au><au>JOHNSON, S. S</au><au>AUSTEN, K. F</au><au>REYNOLDS, D. S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of the cDNA and gene for mouse mast cell protease 4. Demonstration of its late transcription in mast cell subclasses and analysis of its homology to subclass-specific neutral proteases of the mouse and rat</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-01-25</date><risdate>1991</risdate><volume>266</volume><issue>3</issue><spage>1934</spage><epage>1941</epage><pages>1934-1941</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Based on the amino-terminal amino acid sequence of the mature form of mouse mast cell protease 4 (MMCP-4), previously identified
in peritoneal connective tissue mast cells (CTMC) and Kirsten sarcoma virus-immortalized mast cells (KiSV-MC), a 26-mer oligonucleotide
probe was constructed and used to clone cDNAs for MMCP-4 from a KiSV-MC1 cDNA library. MMCP-4 is the first secretory granule
serine protease of CTMC to be molecularly cloned. Using a cDNA probe derived from the 3'-untranslated portion of the MMCP-4
cDNA, the gene for MMCP-4 and a second highly related gene (mouse mast cell protease-like, MMCP-L) were cloned from a BALB/c
mouse genomic DNA library and sequenced entirely, including approximately 2 kilobases of the 5'-flanking region. MMCP-4 and
MMCP-L have five exons of identical length, four introns of nearly identical length, and approximately 900 base pairs of 5'-flanking
DNA with sequence similarity by dot matrix analysis. By RNA blot analysis with gene-specific probes for MMCP-4 (bases 497-633
of the cDNA) and MMCP-L (bases 502-638 of the cDNA), mRNA for MMCP-4 was present in KiSV-MC5, CTMC, and the intestine of a
mouse infected with the parasite Nippostrongylus brasiliensis markedly enriched for mucosal mast cells (MMC); MMCP-L mRNA
was detected only in the intestine of the N. brasiliensis-infected mouse. MMCP-4 mRNA was not expressed in normal mouse intestine
or in interleukin 3-dependent bone marrow-derived mast cells, which can serve as precursors to both MMC and CTMC. This finding
suggests that MMCP-4 is transcribed relatively late in the development of both the CTMC and MMC subclasses and underscores
the fact that mouse bone-marrow-derived mast cells are immature mast cells, rather than tissue culture equivalents of the
MMC subclass.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1988455</pmid><doi>10.1016/S0021-9258(18)52383-8</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1991-01, Vol.266 (3), p.1934-1941 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80430580 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Blotting, Northern Cloning, Molecular DNA - genetics Fundamental and applied biological sciences. Psychology Gene Expression Genes mast cells Mast Cells - enzymology Mice Molecular and cellular biology Molecular genetics Molecular Sequence Data Oligonucleotides - chemistry Rats RNA, Messenger - genetics Serine Endopeptidases - genetics Transcription, Genetic |
| title | Cloning of the cDNA and gene for mouse mast cell protease 4. Demonstration of its late transcription in mast cell subclasses and analysis of its homology to subclass-specific neutral proteases of the mouse and rat |
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