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A phosphoramidon-sensitive metalloprotease induces apoptosis of human endothelial cells by Group B Streptococcus
We explored Group B Streptococcus (GBS)-induced apoptosis in human umbilical vein endothelial cells (HUVEC) and the role of phosphoramidon, a zinc metalloprotease inhibitor, in this process. GBS 90186 strain (serotype V, a blood isolate) and concentrated supernatant (CS) were used to investigate the...
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Published in: | Antonie van Leeuwenhoek 2013-12, Vol.104 (6), p.1125-1133 |
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creator | dos Santos, Michelle Hanthequeste Bittencourt da Costa, Andréia Ferreira Eduardo Ferreira, Beatriz Jandre Souza, Simone Lima da Silva Lannes, Pamella Santos, Gabriela Silva Mattos-Guaraldi, Ana Luiza Nagao, Prescilla Emy |
description | We explored Group B
Streptococcus
(GBS)-induced apoptosis in human umbilical vein endothelial cells (HUVEC) and the role of phosphoramidon, a zinc metalloprotease inhibitor, in this process. GBS 90186 strain (serotype V, a blood isolate) and concentrated supernatant (CS) were used to investigate the viability and morphological alterations in HUVEC by Trypan blue uptake, electrophoresis in 2 % agarose gel and scanning electron microscopy assays. Apoptosis before and after phosphoramidon-treatment were verified by flow cytometry using annexin V-FITC labeling. Differences were considered significant when
P
|
doi_str_mv | 10.1007/s10482-013-0034-y |
format | article |
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Streptococcus
(GBS)-induced apoptosis in human umbilical vein endothelial cells (HUVEC) and the role of phosphoramidon, a zinc metalloprotease inhibitor, in this process. GBS 90186 strain (serotype V, a blood isolate) and concentrated supernatant (CS) were used to investigate the viability and morphological alterations in HUVEC by Trypan blue uptake, electrophoresis in 2 % agarose gel and scanning electron microscopy assays. Apoptosis before and after phosphoramidon-treatment were verified by flow cytometry using annexin V-FITC labeling. Differences were considered significant when
P
< 0.05 using unpaired Student’s
t
test. GBS and CS induced HUVEC death by apoptosis (76.5 and 32 %, respectively) with an increasing pro-apoptotic Bax expression and decreasing anti-apoptotic Bcl-2 expression. Caspase-3 was activated during GBS-induced endothelial apoptosis. Phosphoramidon reduced 89.3 and 100 % of GBS and CS cell death by apoptosis, respectively. Some GBS strains may induce cell death by apoptosis with involvement of metalloproteases and signaling through the intrinsic pathway of apoptosis, which may contribute to GBS survival during sepsis of adults and neonates.</description><identifier>ISSN: 0003-6072</identifier><identifier>EISSN: 1572-9699</identifier><identifier>DOI: 10.1007/s10482-013-0034-y</identifier><identifier>PMID: 24052367</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Annexin A5 - analysis ; Apoptosis ; Biomedical and Life Sciences ; Cell Survival ; Cells, Cultured ; Electrophoresis ; Endothelial Cells - microbiology ; Endothelial Cells - physiology ; Glycopeptides - metabolism ; Humans ; Life Sciences ; Medical Microbiology ; Metalloproteases - antagonists & inhibitors ; Metalloproteases - metabolism ; Microbiology ; Microscopy, Electron ; Mortality ; Neonates ; Original Paper ; Plant Sciences ; Protease Inhibitors - metabolism ; Proteases ; Soil Science & Conservation ; Staining and Labeling - methods ; Streptococcus agalactiae - enzymology ; Streptococcus infections ; Trypan Blue - metabolism</subject><ispartof>Antonie van Leeuwenhoek, 2013-12, Vol.104 (6), p.1125-1133</ispartof><rights>Springer Science+Business Media Dordrecht 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-4c85cf56c8e1a584059bfb3136cc7676c46d2494375d785ea0d526590f32782c3</citedby><cites>FETCH-LOGICAL-c372t-4c85cf56c8e1a584059bfb3136cc7676c46d2494375d785ea0d526590f32782c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24052367$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>dos Santos, Michelle Hanthequeste Bittencourt</creatorcontrib><creatorcontrib>da Costa, Andréia Ferreira Eduardo</creatorcontrib><creatorcontrib>Ferreira, Beatriz Jandre</creatorcontrib><creatorcontrib>Souza, Simone Lima</creatorcontrib><creatorcontrib>da Silva Lannes, Pamella</creatorcontrib><creatorcontrib>Santos, Gabriela Silva</creatorcontrib><creatorcontrib>Mattos-Guaraldi, Ana Luiza</creatorcontrib><creatorcontrib>Nagao, Prescilla Emy</creatorcontrib><title>A phosphoramidon-sensitive metalloprotease induces apoptosis of human endothelial cells by Group B Streptococcus</title><title>Antonie van Leeuwenhoek</title><addtitle>Antonie van Leeuwenhoek</addtitle><addtitle>Antonie Van Leeuwenhoek</addtitle><description>We explored Group B
Streptococcus
(GBS)-induced apoptosis in human umbilical vein endothelial cells (HUVEC) and the role of phosphoramidon, a zinc metalloprotease inhibitor, in this process. GBS 90186 strain (serotype V, a blood isolate) and concentrated supernatant (CS) were used to investigate the viability and morphological alterations in HUVEC by Trypan blue uptake, electrophoresis in 2 % agarose gel and scanning electron microscopy assays. Apoptosis before and after phosphoramidon-treatment were verified by flow cytometry using annexin V-FITC labeling. Differences were considered significant when
P
< 0.05 using unpaired Student’s
t
test. GBS and CS induced HUVEC death by apoptosis (76.5 and 32 %, respectively) with an increasing pro-apoptotic Bax expression and decreasing anti-apoptotic Bcl-2 expression. Caspase-3 was activated during GBS-induced endothelial apoptosis. Phosphoramidon reduced 89.3 and 100 % of GBS and CS cell death by apoptosis, respectively. Some GBS strains may induce cell death by apoptosis with involvement of metalloproteases and signaling through the intrinsic pathway of apoptosis, which may contribute to GBS survival during sepsis of adults and neonates.</description><subject>Annexin A5 - analysis</subject><subject>Apoptosis</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Survival</subject><subject>Cells, Cultured</subject><subject>Electrophoresis</subject><subject>Endothelial Cells - microbiology</subject><subject>Endothelial Cells - physiology</subject><subject>Glycopeptides - metabolism</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Medical Microbiology</subject><subject>Metalloproteases - antagonists & inhibitors</subject><subject>Metalloproteases - metabolism</subject><subject>Microbiology</subject><subject>Microscopy, Electron</subject><subject>Mortality</subject><subject>Neonates</subject><subject>Original Paper</subject><subject>Plant Sciences</subject><subject>Protease Inhibitors - metabolism</subject><subject>Proteases</subject><subject>Soil Science & Conservation</subject><subject>Staining and Labeling - methods</subject><subject>Streptococcus agalactiae - enzymology</subject><subject>Streptococcus infections</subject><subject>Trypan Blue - metabolism</subject><issn>0003-6072</issn><issn>1572-9699</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNp1kUtr3DAUhUVpSCZpfkA2QdBNNkr0lr1MQ_OAQBdt10IjX3ccbMvVtQvz76vJJKEUshBC0nfOPegQcib4peDcXaHgupKMC8U4V5ptP5CVME6y2tb1R7Li5ZZZ7uQROUZ8KsfaVu6QHEnNjVTWrch0TadNwrJyGLomjQxhxG7u_gAdYA59n6acZggItBubJQLSMKVpTtghTS3dLEMYKYxNmjfQd6GnEfoe6XpL73JaJvqFfp8zFEFMMS74iRy0oUc4fdlPyM_brz9u7tnjt7uHm-tHFpWTM9OxMrE1NlYggqlK3nrdrpVQNkZnnY3aNlLXWjnTuMpA4I2R1tS8VdJVMqoTcrH3LfF_L4CzHzrcRQsjpAW90Lp2jhsuC_r5P_QpLXks6Z4paaQxulBiT8WcEDO0fsrdEPLWC-53dfh9Hb7U4Xd1-G3RnL84L-sBmjfF6_8XQO4BLE_jL8j_jH7X9S-AhpZ-</recordid><startdate>20131201</startdate><enddate>20131201</enddate><creator>dos Santos, Michelle Hanthequeste Bittencourt</creator><creator>da Costa, Andréia Ferreira Eduardo</creator><creator>Ferreira, Beatriz Jandre</creator><creator>Souza, Simone Lima</creator><creator>da Silva Lannes, Pamella</creator><creator>Santos, Gabriela Silva</creator><creator>Mattos-Guaraldi, Ana Luiza</creator><creator>Nagao, Prescilla Emy</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20131201</creationdate><title>A phosphoramidon-sensitive metalloprotease induces apoptosis of human endothelial cells by Group B Streptococcus</title><author>dos Santos, Michelle Hanthequeste Bittencourt ; da Costa, Andréia Ferreira Eduardo ; Ferreira, Beatriz Jandre ; Souza, Simone Lima ; da Silva Lannes, Pamella ; Santos, Gabriela Silva ; Mattos-Guaraldi, Ana Luiza ; Nagao, Prescilla Emy</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c372t-4c85cf56c8e1a584059bfb3136cc7676c46d2494375d785ea0d526590f32782c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Annexin A5 - 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Academic</collection><jtitle>Antonie van Leeuwenhoek</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>dos Santos, Michelle Hanthequeste Bittencourt</au><au>da Costa, Andréia Ferreira Eduardo</au><au>Ferreira, Beatriz Jandre</au><au>Souza, Simone Lima</au><au>da Silva Lannes, Pamella</au><au>Santos, Gabriela Silva</au><au>Mattos-Guaraldi, Ana Luiza</au><au>Nagao, Prescilla Emy</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A phosphoramidon-sensitive metalloprotease induces apoptosis of human endothelial cells by Group B Streptococcus</atitle><jtitle>Antonie van Leeuwenhoek</jtitle><stitle>Antonie van Leeuwenhoek</stitle><addtitle>Antonie Van Leeuwenhoek</addtitle><date>2013-12-01</date><risdate>2013</risdate><volume>104</volume><issue>6</issue><spage>1125</spage><epage>1133</epage><pages>1125-1133</pages><issn>0003-6072</issn><eissn>1572-9699</eissn><abstract>We explored Group B
Streptococcus
(GBS)-induced apoptosis in human umbilical vein endothelial cells (HUVEC) and the role of phosphoramidon, a zinc metalloprotease inhibitor, in this process. GBS 90186 strain (serotype V, a blood isolate) and concentrated supernatant (CS) were used to investigate the viability and morphological alterations in HUVEC by Trypan blue uptake, electrophoresis in 2 % agarose gel and scanning electron microscopy assays. Apoptosis before and after phosphoramidon-treatment were verified by flow cytometry using annexin V-FITC labeling. Differences were considered significant when
P
< 0.05 using unpaired Student’s
t
test. GBS and CS induced HUVEC death by apoptosis (76.5 and 32 %, respectively) with an increasing pro-apoptotic Bax expression and decreasing anti-apoptotic Bcl-2 expression. Caspase-3 was activated during GBS-induced endothelial apoptosis. Phosphoramidon reduced 89.3 and 100 % of GBS and CS cell death by apoptosis, respectively. Some GBS strains may induce cell death by apoptosis with involvement of metalloproteases and signaling through the intrinsic pathway of apoptosis, which may contribute to GBS survival during sepsis of adults and neonates.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>24052367</pmid><doi>10.1007/s10482-013-0034-y</doi><tpages>9</tpages></addata></record> |
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subjects | Annexin A5 - analysis Apoptosis Biomedical and Life Sciences Cell Survival Cells, Cultured Electrophoresis Endothelial Cells - microbiology Endothelial Cells - physiology Glycopeptides - metabolism Humans Life Sciences Medical Microbiology Metalloproteases - antagonists & inhibitors Metalloproteases - metabolism Microbiology Microscopy, Electron Mortality Neonates Original Paper Plant Sciences Protease Inhibitors - metabolism Proteases Soil Science & Conservation Staining and Labeling - methods Streptococcus agalactiae - enzymology Streptococcus infections Trypan Blue - metabolism |
title | A phosphoramidon-sensitive metalloprotease induces apoptosis of human endothelial cells by Group B Streptococcus |
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