The cloning and expression of matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase 2 in normal canine lymph nodes and in canine lymphoma
Matrix metalloproteinase-2 (MMP-2) and its inhibitor, tissue inhibitor of matrix metalloproteinase 2 (TIMP2), are known to be important in cancer. The purposes of this study were to determine the cDNA sequence of canine MMP-2 and to investigate the expression patterns of MMP-2 and TIMP2 in normal ca...
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| Veröffentlicht in: | Research in veterinary science 2008-04, Vol.84 (2), p.206-214 |
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| creator | Newman, R.G. Kitchell, B.E. Wallig, M.A. Paria, B. |
| description | Matrix metalloproteinase-2 (MMP-2) and its inhibitor, tissue inhibitor of matrix metalloproteinase 2 (TIMP2), are known to be important in cancer. The purposes of this study were to determine the cDNA sequence of canine MMP-2 and to investigate the expression patterns of MMP-2 and TIMP2 in normal canine lymph nodes and spontaneously arising canine lymphomas. We cloned and sequenced a PCR product containing most (1901 base pairs) of the coding sequence of canine MMP-2 that translates into a 623 amino acid protein. The cDNA and deduced amino acid sequences are highly homologous to those of other mammalian species. Canine MMP-2 and TIMP2 mRNAs were detectable in the majority of normal lymph node and lymphomatous samples evaluated. No statistical difference was identified when comparing the expression of either gene with regard to normal versus neoplastic nodes, nodal versus extranodal lymphoma, lymphoma grade, or B versus T cell immunophenotype. |
| doi_str_mv | 10.1016/j.rvsc.2007.04.016 |
| format | Article |
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The purposes of this study were to determine the cDNA sequence of canine MMP-2 and to investigate the expression patterns of MMP-2 and TIMP2 in normal canine lymph nodes and spontaneously arising canine lymphomas. We cloned and sequenced a PCR product containing most (1901 base pairs) of the coding sequence of canine MMP-2 that translates into a 623 amino acid protein. The cDNA and deduced amino acid sequences are highly homologous to those of other mammalian species. Canine MMP-2 and TIMP2 mRNAs were detectable in the majority of normal lymph node and lymphomatous samples evaluated. No statistical difference was identified when comparing the expression of either gene with regard to normal versus neoplastic nodes, nodal versus extranodal lymphoma, lymphoma grade, or B versus T cell immunophenotype.</description><identifier>ISSN: 0034-5288</identifier><identifier>EISSN: 1532-2661</identifier><identifier>DOI: 10.1016/j.rvsc.2007.04.016</identifier><identifier>PMID: 17604063</identifier><language>eng</language><publisher>England: Elsevier India Pvt Ltd</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Animals ; Base Sequence ; Binding sites ; Canine ; carcinogenesis ; Cloning ; Cloning, Molecular ; complementary DNA ; DNA fingerprinting ; Dog ; dog diseases ; Dogs ; gene expression ; Gene Expression Regulation ; genes ; Health ; histopathology ; inhibitors ; lymph nodes ; Lymph Nodes - enzymology ; Lymphocytes ; Lymphoma ; Lymphoma - enzymology ; Matrix metalloproteinase 2 ; Matrix Metalloproteinase 2 - chemistry ; Matrix Metalloproteinase 2 - genetics ; Matrix Metalloproteinase 2 - metabolism ; metalloproteinases ; molecular cloning ; molecular genetics ; Molecular Sequence Data ; phenotype ; Plasmids ; protein synthesis ; sequence analysis ; Studies ; TIMP2 ; tissue inhibitor of matrix metalloproteinase-2 ; Tissue Inhibitor of Metalloproteinase-2 - genetics ; Tissue Inhibitor of Metalloproteinase-2 - metabolism ; Veterinary medicine ; Wound healing</subject><ispartof>Research in veterinary science, 2008-04, Vol.84 (2), p.206-214</ispartof><rights>2007</rights><rights>Copyright Elsevier Limited Apr 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-a54d3db1e9e57a0f6bfa642681e1e7b663378fbd79f7cda02c9996a14ed916ba3</citedby><cites>FETCH-LOGICAL-c406t-a54d3db1e9e57a0f6bfa642681e1e7b663378fbd79f7cda02c9996a14ed916ba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.rvsc.2007.04.016$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17604063$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Newman, R.G.</creatorcontrib><creatorcontrib>Kitchell, B.E.</creatorcontrib><creatorcontrib>Wallig, M.A.</creatorcontrib><creatorcontrib>Paria, B.</creatorcontrib><title>The cloning and expression of matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase 2 in normal canine lymph nodes and in canine lymphoma</title><title>Research in veterinary science</title><addtitle>Res Vet Sci</addtitle><description>Matrix metalloproteinase-2 (MMP-2) and its inhibitor, tissue inhibitor of matrix metalloproteinase 2 (TIMP2), are known to be important in cancer. The purposes of this study were to determine the cDNA sequence of canine MMP-2 and to investigate the expression patterns of MMP-2 and TIMP2 in normal canine lymph nodes and spontaneously arising canine lymphomas. We cloned and sequenced a PCR product containing most (1901 base pairs) of the coding sequence of canine MMP-2 that translates into a 623 amino acid protein. The cDNA and deduced amino acid sequences are highly homologous to those of other mammalian species. Canine MMP-2 and TIMP2 mRNAs were detectable in the majority of normal lymph node and lymphomatous samples evaluated. No statistical difference was identified when comparing the expression of either gene with regard to normal versus neoplastic nodes, nodal versus extranodal lymphoma, lymphoma grade, or B versus T cell immunophenotype.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding sites</subject><subject>Canine</subject><subject>carcinogenesis</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>complementary DNA</subject><subject>DNA fingerprinting</subject><subject>Dog</subject><subject>dog diseases</subject><subject>Dogs</subject><subject>gene expression</subject><subject>Gene Expression Regulation</subject><subject>genes</subject><subject>Health</subject><subject>histopathology</subject><subject>inhibitors</subject><subject>lymph nodes</subject><subject>Lymph Nodes - enzymology</subject><subject>Lymphocytes</subject><subject>Lymphoma</subject><subject>Lymphoma - enzymology</subject><subject>Matrix metalloproteinase 2</subject><subject>Matrix Metalloproteinase 2 - chemistry</subject><subject>Matrix Metalloproteinase 2 - genetics</subject><subject>Matrix Metalloproteinase 2 - metabolism</subject><subject>metalloproteinases</subject><subject>molecular cloning</subject><subject>molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>phenotype</subject><subject>Plasmids</subject><subject>protein synthesis</subject><subject>sequence analysis</subject><subject>Studies</subject><subject>TIMP2</subject><subject>tissue inhibitor of matrix metalloproteinase-2</subject><subject>Tissue Inhibitor of Metalloproteinase-2 - genetics</subject><subject>Tissue Inhibitor of Metalloproteinase-2 - metabolism</subject><subject>Veterinary medicine</subject><subject>Wound healing</subject><issn>0034-5288</issn><issn>1532-2661</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kdFqFDEUhoModl19AS80IPRuxpNkJpkBb6RYFQpe2F6HTHKmm2UmWZPZ0j6Nr2q2u6B4UQgEzvnOf_7kJ-Qtg5oBkx-3dbrLtuYAqoamLqVnZMVawSsuJXtOVgCiqVredWfkVc5bAGgYUy_JGVMSGpBiRX5fb5DaKQYfbqkJjuL9LmHOPgYaRzqbJfl7OuNipinuUlzQB5Ox4o_w4nPeI_Vh4we_xPTUCOWFoyGm2UzUmrIQ6fQw7zal5jA_6hXg306czWvyYjRTxjene01uLr9cX3yrrn58_X7x-aqy5R1LZdrGCTcw7LFVBkY5jEY2XHYMGapBSiFUNw5O9aOyzgC3fd9Lwxp0PZODEWtyftQthn_tMS969tniNJmAcZ-1AtYWOVXAD_-B27hPoXjTDERbTstFofiRsinmnHDUu-Rnkx4KpA_h6a0-hKcP4WlodCmVoXcn6f0wo_s7ckqrAO-PwGiiNrfJZ33zkwMTAF3TQ1m-Jp-OBJa_uvOYdLYeg0XnE9pFu-ifcvAHcFm3jw</recordid><startdate>20080401</startdate><enddate>20080401</enddate><creator>Newman, R.G.</creator><creator>Kitchell, B.E.</creator><creator>Wallig, M.A.</creator><creator>Paria, B.</creator><general>Elsevier India Pvt Ltd</general><general>Elsevier Limited</general><scope>FBQ</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>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20080401</creationdate><title>The cloning and expression of matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase 2 in normal canine lymph nodes and in canine lymphoma</title><author>Newman, R.G. ; Kitchell, B.E. ; Wallig, M.A. ; Paria, B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-a54d3db1e9e57a0f6bfa642681e1e7b663378fbd79f7cda02c9996a14ed916ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding sites</topic><topic>Canine</topic><topic>carcinogenesis</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>complementary DNA</topic><topic>DNA fingerprinting</topic><topic>Dog</topic><topic>dog diseases</topic><topic>Dogs</topic><topic>gene expression</topic><topic>Gene Expression Regulation</topic><topic>genes</topic><topic>Health</topic><topic>histopathology</topic><topic>inhibitors</topic><topic>lymph nodes</topic><topic>Lymph Nodes - enzymology</topic><topic>Lymphocytes</topic><topic>Lymphoma</topic><topic>Lymphoma - enzymology</topic><topic>Matrix metalloproteinase 2</topic><topic>Matrix Metalloproteinase 2 - chemistry</topic><topic>Matrix Metalloproteinase 2 - genetics</topic><topic>Matrix Metalloproteinase 2 - metabolism</topic><topic>metalloproteinases</topic><topic>molecular cloning</topic><topic>molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>phenotype</topic><topic>Plasmids</topic><topic>protein synthesis</topic><topic>sequence analysis</topic><topic>Studies</topic><topic>TIMP2</topic><topic>tissue inhibitor of matrix metalloproteinase-2</topic><topic>Tissue Inhibitor of Metalloproteinase-2 - genetics</topic><topic>Tissue Inhibitor of Metalloproteinase-2 - metabolism</topic><topic>Veterinary medicine</topic><topic>Wound healing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Newman, R.G.</creatorcontrib><creatorcontrib>Kitchell, B.E.</creatorcontrib><creatorcontrib>Wallig, M.A.</creatorcontrib><creatorcontrib>Paria, B.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Research in veterinary science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Newman, R.G.</au><au>Kitchell, B.E.</au><au>Wallig, M.A.</au><au>Paria, B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The cloning and expression of matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase 2 in normal canine lymph nodes and in canine lymphoma</atitle><jtitle>Research in veterinary science</jtitle><addtitle>Res Vet Sci</addtitle><date>2008-04-01</date><risdate>2008</risdate><volume>84</volume><issue>2</issue><spage>206</spage><epage>214</epage><pages>206-214</pages><issn>0034-5288</issn><eissn>1532-2661</eissn><abstract>Matrix metalloproteinase-2 (MMP-2) and its inhibitor, tissue inhibitor of matrix metalloproteinase 2 (TIMP2), are known to be important in cancer. The purposes of this study were to determine the cDNA sequence of canine MMP-2 and to investigate the expression patterns of MMP-2 and TIMP2 in normal canine lymph nodes and spontaneously arising canine lymphomas. We cloned and sequenced a PCR product containing most (1901 base pairs) of the coding sequence of canine MMP-2 that translates into a 623 amino acid protein. The cDNA and deduced amino acid sequences are highly homologous to those of other mammalian species. Canine MMP-2 and TIMP2 mRNAs were detectable in the majority of normal lymph node and lymphomatous samples evaluated. No statistical difference was identified when comparing the expression of either gene with regard to normal versus neoplastic nodes, nodal versus extranodal lymphoma, lymphoma grade, or B versus T cell immunophenotype.</abstract><cop>England</cop><pub>Elsevier India Pvt Ltd</pub><pmid>17604063</pmid><doi>10.1016/j.rvsc.2007.04.016</doi><tpages>9</tpages></addata></record> |
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| subjects | Amino Acid Sequence amino acid sequences Animals Base Sequence Binding sites Canine carcinogenesis Cloning Cloning, Molecular complementary DNA DNA fingerprinting Dog dog diseases Dogs gene expression Gene Expression Regulation genes Health histopathology inhibitors lymph nodes Lymph Nodes - enzymology Lymphocytes Lymphoma Lymphoma - enzymology Matrix metalloproteinase 2 Matrix Metalloproteinase 2 - chemistry Matrix Metalloproteinase 2 - genetics Matrix Metalloproteinase 2 - metabolism metalloproteinases molecular cloning molecular genetics Molecular Sequence Data phenotype Plasmids protein synthesis sequence analysis Studies TIMP2 tissue inhibitor of matrix metalloproteinase-2 Tissue Inhibitor of Metalloproteinase-2 - genetics Tissue Inhibitor of Metalloproteinase-2 - metabolism Veterinary medicine Wound healing |
| title | The cloning and expression of matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase 2 in normal canine lymph nodes and in canine lymphoma |
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