Apoptosis induced by a snake venom metalloproteinase from Bothrops alternatus venom in C2C12 muscle cells
In this study, the apoptosis inducing effects of baltergin as well as its influence on cell adhesion and migration on muscles cells in vitro were studied. Morphological analysis made by scanning electron and phase contrast microscopy demonstrated typical futures of programmed cell death, apoptosis....
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Veröffentlicht in: | Apoptosis (London) 2017-04, Vol.22 (4), p.491-501 |
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creator | Bustillo, Soledad Van de Velde, Andrea C. Matzner Perfumo, Verónica Gay, Claudia C. Leiva, Laura C. |
description | In this study, the apoptosis inducing effects of baltergin as well as its influence on cell adhesion and migration on muscles cells in vitro were studied. Morphological analysis made by scanning electron and phase contrast microscopy demonstrated typical futures of programmed cell death, apoptosis. This mechanism was confirmed by fluorescence staining, molecular analysis of endonuclease activity and increased mRNA expression level of two representative genes (p53 and bax). On the other hand, baltergin exert an inhibition effect on myoblast cell adhesion and migration in vitro probably through a mechanism that involves the interaction of this enzyme with cell integrins. In conclusion, our results suggest that the absence of appropriate extracellular matrix contacts triggers anoikis. Therefore, this is the first report that demonstrated the mechanism of programmed cell death triggered by baltergin, a PIII metalloprotease isolated from
Bothrops alternatus
venom, in a myoblast cell line. |
doi_str_mv | 10.1007/s10495-017-1350-x |
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Bothrops alternatus
venom, in a myoblast cell line.</description><identifier>ISSN: 1360-8185</identifier><identifier>EISSN: 1573-675X</identifier><identifier>DOI: 10.1007/s10495-017-1350-x</identifier><identifier>PMID: 28205127</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Adhesion ; Analysis ; Animals ; Anoikis - drug effects ; Apoptosis ; bcl-2-Associated X Protein - biosynthesis ; bcl-2-Associated X Protein - genetics ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bothrops - metabolism ; Cancer Research ; Cell Adhesion - drug effects ; Cell Biology ; Cell Line ; Cell Movement - drug effects ; Crotalid Venoms - enzymology ; Crotalid Venoms - isolation & purification ; Crotalid Venoms - pharmacology ; Enzymes ; Ethylenediaminetetraacetic acid ; Integrins ; Metalloproteases - isolation & purification ; Metalloproteases - pharmacology ; Mice ; Mice, Inbred C3H ; Microscopy, Electron, Scanning ; Microscopy, Phase-Contrast ; Muscles ; Myoblasts - cytology ; Myoblasts - drug effects ; Oncology ; RNA ; RNA, Messenger - biosynthesis ; RNA, Messenger - genetics ; Tumor proteins ; Tumor Suppressor Protein p53 - biosynthesis ; Tumor Suppressor Protein p53 - genetics ; Up-Regulation ; Venom ; Virology</subject><ispartof>Apoptosis (London), 2017-04, Vol.22 (4), p.491-501</ispartof><rights>Springer Science+Business Media New York 2017</rights><rights>COPYRIGHT 2017 Springer</rights><rights>Apoptosis is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c515t-27305c9df9ae3800b8619d4ed9b6e3aa72c2f566a1a4fe5437a3b73691e2299d3</citedby><cites>FETCH-LOGICAL-c515t-27305c9df9ae3800b8619d4ed9b6e3aa72c2f566a1a4fe5437a3b73691e2299d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10495-017-1350-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10495-017-1350-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28205127$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bustillo, Soledad</creatorcontrib><creatorcontrib>Van de Velde, Andrea C.</creatorcontrib><creatorcontrib>Matzner Perfumo, Verónica</creatorcontrib><creatorcontrib>Gay, Claudia C.</creatorcontrib><creatorcontrib>Leiva, Laura C.</creatorcontrib><title>Apoptosis induced by a snake venom metalloproteinase from Bothrops alternatus venom in C2C12 muscle cells</title><title>Apoptosis (London)</title><addtitle>Apoptosis</addtitle><addtitle>Apoptosis</addtitle><description>In this study, the apoptosis inducing effects of baltergin as well as its influence on cell adhesion and migration on muscles cells in vitro were studied. Morphological analysis made by scanning electron and phase contrast microscopy demonstrated typical futures of programmed cell death, apoptosis. This mechanism was confirmed by fluorescence staining, molecular analysis of endonuclease activity and increased mRNA expression level of two representative genes (p53 and bax). On the other hand, baltergin exert an inhibition effect on myoblast cell adhesion and migration in vitro probably through a mechanism that involves the interaction of this enzyme with cell integrins. In conclusion, our results suggest that the absence of appropriate extracellular matrix contacts triggers anoikis. Therefore, this is the first report that demonstrated the mechanism of programmed cell death triggered by baltergin, a PIII metalloprotease isolated from
Bothrops alternatus
venom, in a myoblast cell line.</description><subject>Adhesion</subject><subject>Analysis</subject><subject>Animals</subject><subject>Anoikis - drug effects</subject><subject>Apoptosis</subject><subject>bcl-2-Associated X Protein - biosynthesis</subject><subject>bcl-2-Associated X Protein - genetics</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bothrops - metabolism</subject><subject>Cancer Research</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Biology</subject><subject>Cell Line</subject><subject>Cell Movement - drug effects</subject><subject>Crotalid Venoms - enzymology</subject><subject>Crotalid Venoms - isolation & purification</subject><subject>Crotalid Venoms - pharmacology</subject><subject>Enzymes</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Integrins</subject><subject>Metalloproteases - isolation & purification</subject><subject>Metalloproteases - pharmacology</subject><subject>Mice</subject><subject>Mice, Inbred C3H</subject><subject>Microscopy, Electron, Scanning</subject><subject>Microscopy, Phase-Contrast</subject><subject>Muscles</subject><subject>Myoblasts - cytology</subject><subject>Myoblasts - drug effects</subject><subject>Oncology</subject><subject>RNA</subject><subject>RNA, Messenger - biosynthesis</subject><subject>RNA, Messenger - genetics</subject><subject>Tumor proteins</subject><subject>Tumor Suppressor Protein p53 - biosynthesis</subject><subject>Tumor Suppressor Protein p53 - genetics</subject><subject>Up-Regulation</subject><subject>Venom</subject><subject>Virology</subject><issn>1360-8185</issn><issn>1573-675X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkk1v1DAQhiMEoqXwA7ggS1y4pMzYcWwflxVfUiUuIHGznGRSXBJ7sZOq_fd42eVTICEfbI2f99WM5q2qxwjnCKCeZ4TGyBpQ1Sgk1Dd3qlOUStStkh_vlrdoodao5Un1IOcrABBaNPerE645SOTqtPKbXdwtMfvMfBjWngbW3TLHcnCfiV1TiDObaXHTFHcpLuSDy8TGVMov4vIpxV1mblooBbes-SjwgW35Fjmb19xPxHqapvywuje6KdOj431WfXj18v32TX3x7vXb7eai7iXKpeZKgOzNMBpHQgN0ukUzNDSYriXhnOI9H2XbOnTNSLIRyolOidYgcW7MIM6qZwff0u-XlfJiZ5_3HbhAcc0WtVK60YDmP9DWQGukxII-_QO9imsZevpmiA03SsNP6tJNZH0Y45Jcvze1G8Ub4KYRolDnf6HKGWj2fQw0-lL_TYAHQZ9izolGu0t-dunWIth9EuwhCbYkwe6TYG-K5smx4bWbafih-L76AvADkMtXuKT0y0T_dP0KKY28YA</recordid><startdate>20170401</startdate><enddate>20170401</enddate><creator>Bustillo, Soledad</creator><creator>Van de Velde, Andrea C.</creator><creator>Matzner Perfumo, Verónica</creator><creator>Gay, Claudia C.</creator><creator>Leiva, Laura C.</creator><general>Springer US</general><general>Springer</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>7QP</scope><scope>7RQ</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</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>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>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>U9A</scope><scope>7X8</scope></search><sort><creationdate>20170401</creationdate><title>Apoptosis induced by a snake venom metalloproteinase from Bothrops alternatus venom in C2C12 muscle cells</title><author>Bustillo, Soledad ; Van de Velde, Andrea C. ; Matzner Perfumo, Verónica ; Gay, Claudia C. ; Leiva, Laura C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c515t-27305c9df9ae3800b8619d4ed9b6e3aa72c2f566a1a4fe5437a3b73691e2299d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Adhesion</topic><topic>Analysis</topic><topic>Animals</topic><topic>Anoikis - drug effects</topic><topic>Apoptosis</topic><topic>bcl-2-Associated X Protein - biosynthesis</topic><topic>bcl-2-Associated X Protein - genetics</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bothrops - metabolism</topic><topic>Cancer Research</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Biology</topic><topic>Cell Line</topic><topic>Cell Movement - drug effects</topic><topic>Crotalid Venoms - enzymology</topic><topic>Crotalid Venoms - isolation & purification</topic><topic>Crotalid Venoms - pharmacology</topic><topic>Enzymes</topic><topic>Ethylenediaminetetraacetic acid</topic><topic>Integrins</topic><topic>Metalloproteases - isolation & purification</topic><topic>Metalloproteases - pharmacology</topic><topic>Mice</topic><topic>Mice, Inbred C3H</topic><topic>Microscopy, Electron, Scanning</topic><topic>Microscopy, Phase-Contrast</topic><topic>Muscles</topic><topic>Myoblasts - cytology</topic><topic>Myoblasts - 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Academic</collection><jtitle>Apoptosis (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bustillo, Soledad</au><au>Van de Velde, Andrea C.</au><au>Matzner Perfumo, Verónica</au><au>Gay, Claudia C.</au><au>Leiva, Laura C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Apoptosis induced by a snake venom metalloproteinase from Bothrops alternatus venom in C2C12 muscle cells</atitle><jtitle>Apoptosis (London)</jtitle><stitle>Apoptosis</stitle><addtitle>Apoptosis</addtitle><date>2017-04-01</date><risdate>2017</risdate><volume>22</volume><issue>4</issue><spage>491</spage><epage>501</epage><pages>491-501</pages><issn>1360-8185</issn><eissn>1573-675X</eissn><abstract>In this study, the apoptosis inducing effects of baltergin as well as its influence on cell adhesion and migration on muscles cells in vitro were studied. Morphological analysis made by scanning electron and phase contrast microscopy demonstrated typical futures of programmed cell death, apoptosis. This mechanism was confirmed by fluorescence staining, molecular analysis of endonuclease activity and increased mRNA expression level of two representative genes (p53 and bax). On the other hand, baltergin exert an inhibition effect on myoblast cell adhesion and migration in vitro probably through a mechanism that involves the interaction of this enzyme with cell integrins. In conclusion, our results suggest that the absence of appropriate extracellular matrix contacts triggers anoikis. Therefore, this is the first report that demonstrated the mechanism of programmed cell death triggered by baltergin, a PIII metalloprotease isolated from
Bothrops alternatus
venom, in a myoblast cell line.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>28205127</pmid><doi>10.1007/s10495-017-1350-x</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adhesion Analysis Animals Anoikis - drug effects Apoptosis bcl-2-Associated X Protein - biosynthesis bcl-2-Associated X Protein - genetics Biochemistry Biomedical and Life Sciences Biomedicine Bothrops - metabolism Cancer Research Cell Adhesion - drug effects Cell Biology Cell Line Cell Movement - drug effects Crotalid Venoms - enzymology Crotalid Venoms - isolation & purification Crotalid Venoms - pharmacology Enzymes Ethylenediaminetetraacetic acid Integrins Metalloproteases - isolation & purification Metalloproteases - pharmacology Mice Mice, Inbred C3H Microscopy, Electron, Scanning Microscopy, Phase-Contrast Muscles Myoblasts - cytology Myoblasts - drug effects Oncology RNA RNA, Messenger - biosynthesis RNA, Messenger - genetics Tumor proteins Tumor Suppressor Protein p53 - biosynthesis Tumor Suppressor Protein p53 - genetics Up-Regulation Venom Virology |
title | Apoptosis induced by a snake venom metalloproteinase from Bothrops alternatus venom in C2C12 muscle cells |
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