{"id":{"repo_id":"tdl","oai_identifier":"oai:tdl-ir.tdl.org:20.500.12503/29538"},"canonical_url":"https://search.dev.ndltd.org/etd/tdl/oai:tdl-ir.tdl.org:20.500.12503/29538","repository":{"repo_id":"tdl","name":"Texas Digital Library","base_url":"https://tdl-ir.tdl.org/server/oai/request"},"display":{"title":"Production of Extracellular Matrix-Degrading Proteases by a Rat B Cell Line.CRL-1631","abstract":"Badeaux, K. Production of Extracellular Matrix-Degrading Proteases by a Rat B Cell Line.CRL-1631. Master of Science (Microbiology and Immunology), May 2002. 30 pp., 9 illustrations, 1 table, 16 bibliography titles. Previously B lymphocytes have been reported to accumulate at the site of tumor development and to play a role in immune surveillance against metastatic tumors. Investigating this mechanism, we studied B lymphocyte production of extracellular matrix-degrading proteinases: matrix metalloproteinases (MMPs) and components of the urokinase plasminogen activator (uP A) system. Our studies include RT-PCR of CRL-1631 eDNA revealing mRNA for MMP-2, MMP-9, TIMP-1, TIMP-2 and uPAR. MMP-2 and MMP-9 activity was verified by gelatin zymography. TIMP-1, TIMP-2 and uPAR protein expression was confirmed by Western blot analyses. I also report, for the first time, MT -1 MMP gene and protein expression in B cells by RT-PCR and Western blot, respectively. CRL-1631 invasion through Matrigel model basement membrane was significantly inhibited by BB-94, confirming MMP involvement in this cell line's invasiveness. Therefore, B cells use multiple proteases in the degradation of the extracellular matrix, ECM, and this may be one factor responsible for their accumulation at the site of established tumors.","abstract_html":"Badeaux, K. Production of Extracellular Matrix-Degrading Proteases by a Rat B Cell Line.CRL-1631. Master of Science (Microbiology and Immunology), May 2002. 30 pp., 9 illustrations, 1 table, 16 bibliography titles. Previously B lymphocytes have been reported to accumulate at the site of tumor development and to play a role in immune surveillance against metastatic tumors. Investigating this mechanism, we studied B lymphocyte production of extracellular matrix-degrading proteinases: matrix metalloproteinases (MMPs) and components of the urokinase plasminogen activator (uP A) system. Our studies include RT-PCR of CRL-1631 eDNA revealing mRNA for MMP-2, MMP-9, TIMP-1, TIMP-2 and uPAR. MMP-2 and MMP-9 activity was verified by gelatin zymography. TIMP-1, TIMP-2 and uPAR protein expression was confirmed by Western blot analyses. I also report, for the first time, MT -1 MMP gene and protein expression in B cells by RT-PCR and Western blot, respectively. CRL-1631 invasion through Matrigel model basement membrane was significantly inhibited by BB-94, confirming MMP involvement in this cell line's invasiveness. Therefore, B cells use multiple proteases in the degradation of the extracellular matrix, ECM, and this may be one factor responsible for their accumulation at the site of established tumors.","abstract_has_math":false,"creators":["Badeaux, Kathleen S."],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["R. 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Production of Extracellular Matrix-Degrading Proteases by a Rat B Cell Line.CRL-1631. Master of Science (Microbiology and Immunology), May 2002. 30 pp., 9 illustrations, 1 table, 16 bibliography titles. Previously B lymphocytes have been reported to accumulate at the site of tumor development and to play a role in immune surveillance against metastatic tumors. Investigating this mechanism, we studied B lymphocyte production of extracellular matrix-degrading proteinases: matrix metalloproteinases (MMPs) and components of the urokinase plasminogen activator (uP A) system. Our studies include RT-PCR of CRL-1631 eDNA revealing mRNA for MMP-2, MMP-9, TIMP-1, TIMP-2 and uPAR. MMP-2 and MMP-9 activity was verified by gelatin zymography. TIMP-1, TIMP-2 and uPAR protein expression was confirmed by Western blot analyses. I also report, for the first time, MT -1 MMP gene and protein expression in B cells by RT-PCR and Western blot, respectively. CRL-1631 invasion through Matrigel model basement membrane was significantly inhibited by BB-94, confirming MMP involvement in this cell line's invasiveness. Therefore, B cells use multiple proteases in the degradation of the extracellular matrix, ECM, and this may be one factor responsible for their accumulation at the site of established tumors."]},{"key":"dc:title","label":"Title","values":["Production of Extracellular Matrix-Degrading Proteases by a Rat B Cell Line.CRL-1631"]}]}],"canonical_facts":{"dc:contributor":["R. Goldfarb"],"dc:creator":["Badeaux, Kathleen S."],"dc:date.accessioned":["2019-08-22T21:43:32Z","2026-03-24T17:24:37Z"],"dc:date.available":["2019-08-22T21:43:32Z"],"dc:date.issued":["2002-05-01"],"dc:description.abstract":["Badeaux, K. Production of Extracellular Matrix-Degrading Proteases by a Rat B Cell Line.CRL-1631. Master of Science (Microbiology and Immunology), May 2002. 30 pp., 9 illustrations, 1 table, 16 bibliography titles. Previously B lymphocytes have been reported to accumulate at the site of tumor development and to play a role in immune surveillance against metastatic tumors. Investigating this mechanism, we studied B lymphocyte production of extracellular matrix-degrading proteinases: matrix metalloproteinases (MMPs) and components of the urokinase plasminogen activator (uP A) system. Our studies include RT-PCR of CRL-1631 eDNA revealing mRNA for MMP-2, MMP-9, TIMP-1, TIMP-2 and uPAR. MMP-2 and MMP-9 activity was verified by gelatin zymography. TIMP-1, TIMP-2 and uPAR protein expression was confirmed by Western blot analyses. I also report, for the first time, MT -1 MMP gene and protein expression in B cells by RT-PCR and Western blot, respectively. CRL-1631 invasion through Matrigel model basement membrane was significantly inhibited by BB-94, confirming MMP involvement in this cell line's invasiveness. Therefore, B cells use multiple proteases in the degradation of the extracellular matrix, ECM, and this may be one factor responsible for their accumulation at the site of established tumors."],"dc:identifier":["https://hdl.handle.net/20.500.12503/29538"],"dc:identifier.uri":["https://hdl.handle.net/20.500.12503/29538"],"dc:language":["en"],"dc:subject":["Genetics and Genomics","Medicine and Health Sciences","Molecular Genetics","Oncology","Lymphocytes","tumors","cancer","genetics","protein expression"],"dc:title":["Production of Extracellular Matrix-Degrading Proteases by a Rat B Cell Line.CRL-1631"],"dc:type":["Thesis"]},"updated_at":"2026-07-27T21:19:01Z"}