Induction of MMP-9 mediated gelatinolytic activity in human monocytic cells by cell wall components of Mycobacterium tuberculosis
Mycobacterium tuberculosis (Mtb) infection induces the expression of host matrix metalloIproteinases (MMPs) capable of tissue degradation. We show that infection of mice with Mtb results in differential expression of MMPs in the lung. MMP-9 activity increased by week 1 post-infection, while MMP-2 ac...
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| Veröffentlicht in: | Microbial pathogenesis 2000-10, Vol.29 (4), p.231-244 |
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| creator | RIVERA-MARRERO, Carlos A SCHUYLER, William ROSER, Susanne ROMAN, Jesse |
| description | Mycobacterium tuberculosis (Mtb) infection induces the expression of host matrix metalloIproteinases (MMPs) capable of tissue degradation. We show that infection of mice with Mtb results in differential expression of MMPs in the lung. MMP-9 activity increased by week 1 post-infection, while MMP-2 activity increased after week 2. RT-PCR analysis for gene expression of gelatinases and their respective inhibitors showed: a small increase in MMP-9 by week 1, no change in TIMP-1 and MMP-2, and a significant decrease in TIMP-2 by week 4. The increase in MMP-2 could be due to a decrease in TIMP-2 expression. Addition of 4-aminophenylmercuric acid to lung extracts increased MMP-9 activity, suggesting that its regulation could be due to endogenous activation by proteases. In vitro, attenuated and virulent Mtb strains equally induced MMP-9 expression in U937 monocytes. The inducer of MMP-9 in Mtb was present in culture filtrates, and was active after paraformaldehyde fixation. LAM stimulated MMP-9 expression in THP-1 cells, but not U937 cells. However, LAM-free extracts also induced MMP-9 activity in THP-1 cells. Fractionation of Mtb extracts by chromatography revealed fractions of 17 and 156 kDa with MMP-9 inducing activity. In conclusion, LAM and other components of Mtb induce the expression of MMP-9. |
| doi_str_mv | 10.1006/mpat.2000.0383 |
| format | Article |
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We show that infection of mice with Mtb results in differential expression of MMPs in the lung. MMP-9 activity increased by week 1 post-infection, while MMP-2 activity increased after week 2. RT-PCR analysis for gene expression of gelatinases and their respective inhibitors showed: a small increase in MMP-9 by week 1, no change in TIMP-1 and MMP-2, and a significant decrease in TIMP-2 by week 4. The increase in MMP-2 could be due to a decrease in TIMP-2 expression. Addition of 4-aminophenylmercuric acid to lung extracts increased MMP-9 activity, suggesting that its regulation could be due to endogenous activation by proteases. In vitro, attenuated and virulent Mtb strains equally induced MMP-9 expression in U937 monocytes. The inducer of MMP-9 in Mtb was present in culture filtrates, and was active after paraformaldehyde fixation. LAM stimulated MMP-9 expression in THP-1 cells, but not U937 cells. However, LAM-free extracts also induced MMP-9 activity in THP-1 cells. Fractionation of Mtb extracts by chromatography revealed fractions of 17 and 156 kDa with MMP-9 inducing activity. In conclusion, LAM and other components of Mtb induce the expression of MMP-9.</description><identifier>ISSN: 0882-4010</identifier><identifier>EISSN: 1096-1208</identifier><identifier>DOI: 10.1006/mpat.2000.0383</identifier><identifier>PMID: 10993742</identifier><identifier>CODEN: MIPAEV</identifier><language>eng</language><publisher>Oxford: Elsevier</publisher><subject>Animals ; Antigens, Bacterial - pharmacology ; Bacterial diseases ; Bacteriology ; Biological and medical sciences ; Cell Line ; Cell Wall - immunology ; Chromatography ; Experimental bacterial diseases and models ; Female ; Fundamental and applied biological sciences. Psychology ; Gelatin - metabolism ; Humans ; Infectious diseases ; Lipopolysaccharides - pharmacology ; Lung - drug effects ; Lung - enzymology ; Lung - microbiology ; Matrix Metalloproteinase 2 - biosynthesis ; Matrix Metalloproteinase 9 - analysis ; Matrix Metalloproteinase 9 - biosynthesis ; Matrix Metalloproteinase 9 - chemistry ; Medical sciences ; Mice ; Mice, Inbred C57BL ; Microbiology ; Molecular Weight ; Mycobacterium tuberculosis - immunology ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Phenylmercuric Acetate - analogs & derivatives ; Phenylmercuric Acetate - pharmacology ; Time Factors ; Tissue Inhibitor of Metalloproteinase-2 - biosynthesis ; Tuberculosis - metabolism ; Tuberculosis - microbiology ; U937 Cells</subject><ispartof>Microbial pathogenesis, 2000-10, Vol.29 (4), p.231-244</ispartof><rights>2000 INIST-CNRS</rights><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1518939$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10993742$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>RIVERA-MARRERO, Carlos A</creatorcontrib><creatorcontrib>SCHUYLER, William</creatorcontrib><creatorcontrib>ROSER, Susanne</creatorcontrib><creatorcontrib>ROMAN, Jesse</creatorcontrib><title>Induction of MMP-9 mediated gelatinolytic activity in human monocytic cells by cell wall components of Mycobacterium tuberculosis</title><title>Microbial pathogenesis</title><addtitle>Microb Pathog</addtitle><description>Mycobacterium tuberculosis (Mtb) infection induces the expression of host matrix metalloIproteinases (MMPs) capable of tissue degradation. We show that infection of mice with Mtb results in differential expression of MMPs in the lung. MMP-9 activity increased by week 1 post-infection, while MMP-2 activity increased after week 2. RT-PCR analysis for gene expression of gelatinases and their respective inhibitors showed: a small increase in MMP-9 by week 1, no change in TIMP-1 and MMP-2, and a significant decrease in TIMP-2 by week 4. The increase in MMP-2 could be due to a decrease in TIMP-2 expression. Addition of 4-aminophenylmercuric acid to lung extracts increased MMP-9 activity, suggesting that its regulation could be due to endogenous activation by proteases. In vitro, attenuated and virulent Mtb strains equally induced MMP-9 expression in U937 monocytes. The inducer of MMP-9 in Mtb was present in culture filtrates, and was active after paraformaldehyde fixation. LAM stimulated MMP-9 expression in THP-1 cells, but not U937 cells. However, LAM-free extracts also induced MMP-9 activity in THP-1 cells. Fractionation of Mtb extracts by chromatography revealed fractions of 17 and 156 kDa with MMP-9 inducing activity. In conclusion, LAM and other components of Mtb induce the expression of MMP-9.</description><subject>Animals</subject><subject>Antigens, Bacterial - pharmacology</subject><subject>Bacterial diseases</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Cell Wall - immunology</subject><subject>Chromatography</subject><subject>Experimental bacterial diseases and models</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gelatin - metabolism</subject><subject>Humans</subject><subject>Infectious diseases</subject><subject>Lipopolysaccharides - pharmacology</subject><subject>Lung - drug effects</subject><subject>Lung - enzymology</subject><subject>Lung - microbiology</subject><subject>Matrix Metalloproteinase 2 - biosynthesis</subject><subject>Matrix Metalloproteinase 9 - analysis</subject><subject>Matrix Metalloproteinase 9 - biosynthesis</subject><subject>Matrix Metalloproteinase 9 - chemistry</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Mycobacterium tuberculosis - immunology</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Phenylmercuric Acetate - analogs & derivatives</subject><subject>Phenylmercuric Acetate - pharmacology</subject><subject>Time Factors</subject><subject>Tissue Inhibitor of Metalloproteinase-2 - biosynthesis</subject><subject>Tuberculosis - metabolism</subject><subject>Tuberculosis - microbiology</subject><subject>U937 Cells</subject><issn>0882-4010</issn><issn>1096-1208</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpF0EtLxDAQB_AgiruuXj1KDuKta17N4yjiY2EXPei5pGmqkTapTar06De3riteZgbmx59hADjFaIkR4pdtp9OSIISWiEq6B-YYKZ5hguQ-mCMpScYQRjNwFOPbpBSj6hDMJqSoYGQOvla-GkxywcNQw83mMVOwtZXTyVbwxTY6OR-aMTkD9cQ-XBqh8_B1aLWHbfDBbHfGNk2E5bgd4KeeigltF7z1KW6TRxPKKcH2bmhhGkrbm6EJ0cVjcFDrJtqTXV-A59ubp-v7bP1wt7q-WmcdoTxltKJKyRIzpiQ1tiaYY4x5ibUUeYUU0VXNtRA5q0ohytwaIhQTTAptuGWKLsDFb27Xh_fBxlS0Lv6cq70NQywEIQJzRSd4toNDOb2i6HrX6n4s_p42gfMd0NHopu61Ny7-uxxLRRX9Bns5fTs</recordid><startdate>20001001</startdate><enddate>20001001</enddate><creator>RIVERA-MARRERO, Carlos A</creator><creator>SCHUYLER, William</creator><creator>ROSER, Susanne</creator><creator>ROMAN, Jesse</creator><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20001001</creationdate><title>Induction of MMP-9 mediated gelatinolytic activity in human monocytic cells by cell wall components of Mycobacterium tuberculosis</title><author>RIVERA-MARRERO, Carlos A ; SCHUYLER, William ; ROSER, Susanne ; ROMAN, Jesse</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p236t-3d3998b144983cef2161116b1a875d092adf6a7754db77b5ec27947487ac6e493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Antigens, Bacterial - pharmacology</topic><topic>Bacterial diseases</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Cell Wall - immunology</topic><topic>Chromatography</topic><topic>Experimental bacterial diseases and models</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gelatin - metabolism</topic><topic>Humans</topic><topic>Infectious diseases</topic><topic>Lipopolysaccharides - pharmacology</topic><topic>Lung - drug effects</topic><topic>Lung - enzymology</topic><topic>Lung - microbiology</topic><topic>Matrix Metalloproteinase 2 - biosynthesis</topic><topic>Matrix Metalloproteinase 9 - analysis</topic><topic>Matrix Metalloproteinase 9 - biosynthesis</topic><topic>Matrix Metalloproteinase 9 - chemistry</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Mycobacterium tuberculosis - immunology</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Phenylmercuric Acetate - analogs & derivatives</topic><topic>Phenylmercuric Acetate - pharmacology</topic><topic>Time Factors</topic><topic>Tissue Inhibitor of Metalloproteinase-2 - biosynthesis</topic><topic>Tuberculosis - metabolism</topic><topic>Tuberculosis - microbiology</topic><topic>U937 Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RIVERA-MARRERO, Carlos A</creatorcontrib><creatorcontrib>SCHUYLER, William</creatorcontrib><creatorcontrib>ROSER, Susanne</creatorcontrib><creatorcontrib>ROMAN, Jesse</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Microbial pathogenesis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RIVERA-MARRERO, Carlos A</au><au>SCHUYLER, William</au><au>ROSER, Susanne</au><au>ROMAN, Jesse</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Induction of MMP-9 mediated gelatinolytic activity in human monocytic cells by cell wall components of Mycobacterium tuberculosis</atitle><jtitle>Microbial pathogenesis</jtitle><addtitle>Microb Pathog</addtitle><date>2000-10-01</date><risdate>2000</risdate><volume>29</volume><issue>4</issue><spage>231</spage><epage>244</epage><pages>231-244</pages><issn>0882-4010</issn><eissn>1096-1208</eissn><coden>MIPAEV</coden><abstract>Mycobacterium tuberculosis (Mtb) infection induces the expression of host matrix metalloIproteinases (MMPs) capable of tissue degradation. We show that infection of mice with Mtb results in differential expression of MMPs in the lung. MMP-9 activity increased by week 1 post-infection, while MMP-2 activity increased after week 2. RT-PCR analysis for gene expression of gelatinases and their respective inhibitors showed: a small increase in MMP-9 by week 1, no change in TIMP-1 and MMP-2, and a significant decrease in TIMP-2 by week 4. The increase in MMP-2 could be due to a decrease in TIMP-2 expression. Addition of 4-aminophenylmercuric acid to lung extracts increased MMP-9 activity, suggesting that its regulation could be due to endogenous activation by proteases. In vitro, attenuated and virulent Mtb strains equally induced MMP-9 expression in U937 monocytes. The inducer of MMP-9 in Mtb was present in culture filtrates, and was active after paraformaldehyde fixation. LAM stimulated MMP-9 expression in THP-1 cells, but not U937 cells. However, LAM-free extracts also induced MMP-9 activity in THP-1 cells. Fractionation of Mtb extracts by chromatography revealed fractions of 17 and 156 kDa with MMP-9 inducing activity. In conclusion, LAM and other components of Mtb induce the expression of MMP-9.</abstract><cop>Oxford</cop><pub>Elsevier</pub><pmid>10993742</pmid><doi>10.1006/mpat.2000.0383</doi><tpages>14</tpages></addata></record> |
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| subjects | Animals Antigens, Bacterial - pharmacology Bacterial diseases Bacteriology Biological and medical sciences Cell Line Cell Wall - immunology Chromatography Experimental bacterial diseases and models Female Fundamental and applied biological sciences. Psychology Gelatin - metabolism Humans Infectious diseases Lipopolysaccharides - pharmacology Lung - drug effects Lung - enzymology Lung - microbiology Matrix Metalloproteinase 2 - biosynthesis Matrix Metalloproteinase 9 - analysis Matrix Metalloproteinase 9 - biosynthesis Matrix Metalloproteinase 9 - chemistry Medical sciences Mice Mice, Inbred C57BL Microbiology Molecular Weight Mycobacterium tuberculosis - immunology Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Phenylmercuric Acetate - analogs & derivatives Phenylmercuric Acetate - pharmacology Time Factors Tissue Inhibitor of Metalloproteinase-2 - biosynthesis Tuberculosis - metabolism Tuberculosis - microbiology U937 Cells |
| title | Induction of MMP-9 mediated gelatinolytic activity in human monocytic cells by cell wall components of Mycobacterium tuberculosis |
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