Phosphatidylserine Efflux and Intercellular Fusion in a BeWo Model of Human Villous Cytotrophoblast
Phosphatidylserine (PS) efflux characterizes cytotrophoblast apoptosis and differentiation. To evaluate whether PS externalization and intercellular fusion were secondary to apoptosis, BeWo cells were induced to differentiate by forskolin or undergo apoptosis by staurosporine. PS externalization was...
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| Veröffentlicht in: | Placenta (Eastbourne) 2004-05, Vol.25 (5), p.396-407 |
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| creator | Das, M. Xu, B. Lin, L. Chakrabarti, S. Shivaswamy, V. Rote, N.S. |
| description | Phosphatidylserine (PS) efflux characterizes cytotrophoblast apoptosis and differentiation. To evaluate whether PS externalization and intercellular fusion were secondary to apoptosis, BeWo cells were induced to differentiate by forskolin or undergo apoptosis by staurosporine. PS externalization was measured by FITC–annexin V binding, and intercellular fusion was quantified by counting nuclei in syncytial cells. During forskolin treatment, vanadate decreased PS efflux by 78.0 per cent from 68.0 [5.3] (mean [SD]) to 15.0 [8.8] Lum (×10
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| doi_str_mv | 10.1016/j.placenta.2003.11.004 |
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3) (
P<0.001), whereas Z-VAD-fmk had no effect (66.5 [7.3]). Vanadate decreased intercellular fusion from 78.1 per cent [4.1] fusion in uninhibited cultures to 23.4 per cent [2.5], compared with 10.0 per cent [1.7] in media alone. Z-VAD-fmk did not affect fusion (80.4 per cent [6.8]). Staurosporine induced PS efflux was not affected by vanadate (69.6 [5.5] Lum ×10
3), but was inhibited 87.8 per cent by Z-VAD-fmk; from 71.5 [6.2] to 8.7 [3.6] Lum (×10
3) (
P<0.001). Apoptosis was measured by the TUNEL and COMET assays, lamin B fragmentation, activation of procaspase 3, mitochondrial membrane potential, and release of mitochondrial cytochrome c and apoptosis inducing factor. There was no indication of apoptosis associated with differentiation. Thus, PS efflux and intercellular fusion occurred through a vanadate-sensitive mechanism that was independent of apoptosis.</description><identifier>ISSN: 0143-4004</identifier><identifier>EISSN: 1532-3102</identifier><identifier>DOI: 10.1016/j.placenta.2003.11.004</identifier><identifier>PMID: 15081634</identifier><identifier>CODEN: PLACDF</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Ageing, cell death ; Amino Acid Chloromethyl Ketones - pharmacology ; Apoptosis - drug effects ; Apoptosis - physiology ; Apoptosis Inducing Factor ; Biological and medical sciences ; Blotting, Western ; Caspase 3 ; Caspase Inhibitors ; Caspases - metabolism ; Cell Differentiation - drug effects ; Cell Differentiation - physiology ; Cell Fusion ; Cell Line, Tumor ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cell physiology ; Colforsin - pharmacology ; Cysteine Proteinase Inhibitors - pharmacology ; Cytochromes c - antagonists & inhibitors ; Cytochromes c - metabolism ; Cytosol - chemistry ; DNA Fragmentation - drug effects ; Flavoproteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Humans ; Lamin Type B - metabolism ; Membrane Lipids - metabolism ; Membrane Potentials - drug effects ; Membrane Proteins - metabolism ; Microscopy, Fluorescence ; Mitochondria - chemistry ; Mitochondria - drug effects ; Mitochondria - metabolism ; Models, Biological ; Molecular and cellular biology ; Phosphatidylserines - metabolism ; Staurosporine - pharmacology ; Trophoblasts - cytology ; Trophoblasts - drug effects ; Trophoblasts - physiology ; Vanadates - pharmacology</subject><ispartof>Placenta (Eastbourne), 2004-05, Vol.25 (5), p.396-407</ispartof><rights>2003 Elsevier Science Ltd</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c460t-3599656c49149941130cf17b71ed60843fc5db46a5ea6aaee98e6e2ba70ff1d03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.placenta.2003.11.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15659254$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15081634$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Das, M.</creatorcontrib><creatorcontrib>Xu, B.</creatorcontrib><creatorcontrib>Lin, L.</creatorcontrib><creatorcontrib>Chakrabarti, S.</creatorcontrib><creatorcontrib>Shivaswamy, V.</creatorcontrib><creatorcontrib>Rote, N.S.</creatorcontrib><title>Phosphatidylserine Efflux and Intercellular Fusion in a BeWo Model of Human Villous Cytotrophoblast</title><title>Placenta (Eastbourne)</title><addtitle>Placenta</addtitle><description>Phosphatidylserine (PS) efflux characterizes cytotrophoblast apoptosis and differentiation. To evaluate whether PS externalization and intercellular fusion were secondary to apoptosis, BeWo cells were induced to differentiate by forskolin or undergo apoptosis by staurosporine. PS externalization was measured by FITC–annexin V binding, and intercellular fusion was quantified by counting nuclei in syncytial cells. During forskolin treatment, vanadate decreased PS efflux by 78.0 per cent from 68.0 [5.3] (mean [SD]) to 15.0 [8.8] Lum (×10
3) (
P<0.001), whereas Z-VAD-fmk had no effect (66.5 [7.3]). Vanadate decreased intercellular fusion from 78.1 per cent [4.1] fusion in uninhibited cultures to 23.4 per cent [2.5], compared with 10.0 per cent [1.7] in media alone. Z-VAD-fmk did not affect fusion (80.4 per cent [6.8]). Staurosporine induced PS efflux was not affected by vanadate (69.6 [5.5] Lum ×10
3), but was inhibited 87.8 per cent by Z-VAD-fmk; from 71.5 [6.2] to 8.7 [3.6] Lum (×10
3) (
P<0.001). Apoptosis was measured by the TUNEL and COMET assays, lamin B fragmentation, activation of procaspase 3, mitochondrial membrane potential, and release of mitochondrial cytochrome c and apoptosis inducing factor. There was no indication of apoptosis associated with differentiation. Thus, PS efflux and intercellular fusion occurred through a vanadate-sensitive mechanism that was independent of apoptosis.</description><subject>Ageing, cell death</subject><subject>Amino Acid Chloromethyl Ketones - pharmacology</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>Apoptosis Inducing Factor</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Caspase 3</subject><subject>Caspase Inhibitors</subject><subject>Caspases - metabolism</subject><subject>Cell Differentiation - drug effects</subject><subject>Cell Differentiation - physiology</subject><subject>Cell Fusion</subject><subject>Cell Line, Tumor</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>Cell physiology</subject><subject>Colforsin - pharmacology</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Cytochromes c - antagonists & inhibitors</subject><subject>Cytochromes c - metabolism</subject><subject>Cytosol - chemistry</subject><subject>DNA Fragmentation - drug effects</subject><subject>Flavoproteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Lamin Type B - metabolism</subject><subject>Membrane Lipids - metabolism</subject><subject>Membrane Potentials - drug effects</subject><subject>Membrane Proteins - metabolism</subject><subject>Microscopy, Fluorescence</subject><subject>Mitochondria - chemistry</subject><subject>Mitochondria - drug effects</subject><subject>Mitochondria - metabolism</subject><subject>Models, Biological</subject><subject>Molecular and cellular biology</subject><subject>Phosphatidylserines - metabolism</subject><subject>Staurosporine - pharmacology</subject><subject>Trophoblasts - cytology</subject><subject>Trophoblasts - drug effects</subject><subject>Trophoblasts - physiology</subject><subject>Vanadates - pharmacology</subject><issn>0143-4004</issn><issn>1532-3102</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQhi0EokvhL1S-wC2pJ3aczQ1YtbRSERz4OFqOM9Z65bWD7VTsvyerXVRunEYaPe_Mq4eQK2A1MJDXu3ry2mAoum4Y4zVAzZh4RlbQ8qbiwJrnZMVA8Eos-wvyKucdY6wX0LwkF9CyNUguVsR83cY8bXVx48FnTC4gvbHWz7-pDiO9DwWTQe9nrxO9nbOLgbpANf2IPyP9HEf0NFp6N-91oD-c93HOdHMosaQ4bePgdS6vyQurl-NvzvOSfL-9-ba5qx6-fLrffHiojJCsVLzte9lKI3oQ_VIUODMWuqEDHCVbC25NOw5C6ha11BqxX6PEZtAdsxZGxi_Ju9PdKcVfM-ai9i4fy-uASy3VwZoz2TULKE-gSTHnhFZNye11Oihg6qhX7dRfveqoVwGoReMSvDp_mIc9jk-xs88FeHsGdDba26SDcfkfTrZ90x659ycOFx-PDpPKxmEwOLqEpqgxuv91-QMTOJzH</recordid><startdate>20040501</startdate><enddate>20040501</enddate><creator>Das, M.</creator><creator>Xu, B.</creator><creator>Lin, L.</creator><creator>Chakrabarti, S.</creator><creator>Shivaswamy, V.</creator><creator>Rote, N.S.</creator><general>Elsevier Ltd</general><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>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040501</creationdate><title>Phosphatidylserine Efflux and Intercellular Fusion in a BeWo Model of Human Villous Cytotrophoblast</title><author>Das, M. ; Xu, B. ; Lin, L. ; Chakrabarti, S. ; Shivaswamy, V. ; Rote, N.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c460t-3599656c49149941130cf17b71ed60843fc5db46a5ea6aaee98e6e2ba70ff1d03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Ageing, cell death</topic><topic>Amino Acid Chloromethyl Ketones - pharmacology</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>Apoptosis Inducing Factor</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Caspase 3</topic><topic>Caspase Inhibitors</topic><topic>Caspases - metabolism</topic><topic>Cell Differentiation - drug effects</topic><topic>Cell Differentiation - physiology</topic><topic>Cell Fusion</topic><topic>Cell Line, Tumor</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Cell physiology</topic><topic>Colforsin - pharmacology</topic><topic>Cysteine Proteinase Inhibitors - pharmacology</topic><topic>Cytochromes c - antagonists & inhibitors</topic><topic>Cytochromes c - metabolism</topic><topic>Cytosol - chemistry</topic><topic>DNA Fragmentation - drug effects</topic><topic>Flavoproteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Lamin Type B - metabolism</topic><topic>Membrane Lipids - metabolism</topic><topic>Membrane Potentials - drug effects</topic><topic>Membrane Proteins - metabolism</topic><topic>Microscopy, Fluorescence</topic><topic>Mitochondria - chemistry</topic><topic>Mitochondria - drug effects</topic><topic>Mitochondria - metabolism</topic><topic>Models, Biological</topic><topic>Molecular and cellular biology</topic><topic>Phosphatidylserines - metabolism</topic><topic>Staurosporine - pharmacology</topic><topic>Trophoblasts - cytology</topic><topic>Trophoblasts - drug effects</topic><topic>Trophoblasts - physiology</topic><topic>Vanadates - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Das, M.</creatorcontrib><creatorcontrib>Xu, B.</creatorcontrib><creatorcontrib>Lin, L.</creatorcontrib><creatorcontrib>Chakrabarti, S.</creatorcontrib><creatorcontrib>Shivaswamy, V.</creatorcontrib><creatorcontrib>Rote, N.S.</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>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Placenta (Eastbourne)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Das, M.</au><au>Xu, B.</au><au>Lin, L.</au><au>Chakrabarti, S.</au><au>Shivaswamy, V.</au><au>Rote, N.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphatidylserine Efflux and Intercellular Fusion in a BeWo Model of Human Villous Cytotrophoblast</atitle><jtitle>Placenta (Eastbourne)</jtitle><addtitle>Placenta</addtitle><date>2004-05-01</date><risdate>2004</risdate><volume>25</volume><issue>5</issue><spage>396</spage><epage>407</epage><pages>396-407</pages><issn>0143-4004</issn><eissn>1532-3102</eissn><coden>PLACDF</coden><abstract>Phosphatidylserine (PS) efflux characterizes cytotrophoblast apoptosis and differentiation. To evaluate whether PS externalization and intercellular fusion were secondary to apoptosis, BeWo cells were induced to differentiate by forskolin or undergo apoptosis by staurosporine. PS externalization was measured by FITC–annexin V binding, and intercellular fusion was quantified by counting nuclei in syncytial cells. During forskolin treatment, vanadate decreased PS efflux by 78.0 per cent from 68.0 [5.3] (mean [SD]) to 15.0 [8.8] Lum (×10
3) (
P<0.001), whereas Z-VAD-fmk had no effect (66.5 [7.3]). Vanadate decreased intercellular fusion from 78.1 per cent [4.1] fusion in uninhibited cultures to 23.4 per cent [2.5], compared with 10.0 per cent [1.7] in media alone. Z-VAD-fmk did not affect fusion (80.4 per cent [6.8]). Staurosporine induced PS efflux was not affected by vanadate (69.6 [5.5] Lum ×10
3), but was inhibited 87.8 per cent by Z-VAD-fmk; from 71.5 [6.2] to 8.7 [3.6] Lum (×10
3) (
P<0.001). Apoptosis was measured by the TUNEL and COMET assays, lamin B fragmentation, activation of procaspase 3, mitochondrial membrane potential, and release of mitochondrial cytochrome c and apoptosis inducing factor. There was no indication of apoptosis associated with differentiation. Thus, PS efflux and intercellular fusion occurred through a vanadate-sensitive mechanism that was independent of apoptosis.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>15081634</pmid><doi>10.1016/j.placenta.2003.11.004</doi><tpages>12</tpages></addata></record> |
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| subjects | Ageing, cell death Amino Acid Chloromethyl Ketones - pharmacology Apoptosis - drug effects Apoptosis - physiology Apoptosis Inducing Factor Biological and medical sciences Blotting, Western Caspase 3 Caspase Inhibitors Caspases - metabolism Cell Differentiation - drug effects Cell Differentiation - physiology Cell Fusion Cell Line, Tumor Cell Membrane - drug effects Cell Membrane - metabolism Cell physiology Colforsin - pharmacology Cysteine Proteinase Inhibitors - pharmacology Cytochromes c - antagonists & inhibitors Cytochromes c - metabolism Cytosol - chemistry DNA Fragmentation - drug effects Flavoproteins - metabolism Fundamental and applied biological sciences. Psychology Humans Lamin Type B - metabolism Membrane Lipids - metabolism Membrane Potentials - drug effects Membrane Proteins - metabolism Microscopy, Fluorescence Mitochondria - chemistry Mitochondria - drug effects Mitochondria - metabolism Models, Biological Molecular and cellular biology Phosphatidylserines - metabolism Staurosporine - pharmacology Trophoblasts - cytology Trophoblasts - drug effects Trophoblasts - physiology Vanadates - pharmacology |
| title | Phosphatidylserine Efflux and Intercellular Fusion in a BeWo Model of Human Villous Cytotrophoblast |
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