Extracellular signal-regulated kinase activation involved in human sperm-zona pellucida binding
In a previous study involving the inhibition of the mitogen‐activated protein kinase (MAPK), extracellular signal regulated kinase (ERK), we found that the very specific MAPK kinase (MEK) inhibitor, PD098059, inhibited the zona pellucida (ZP) induced acrosome reaction. As an intact acrosome on the s...
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| Veröffentlicht in: | Andrologia 2002-02, Vol.34 (1), p.55-59 |
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| creator | Du Plessis, S. S. Page, C. Franken, D. R. |
| description | In a previous study involving the inhibition of the mitogen‐activated protein kinase (MAPK), extracellular signal regulated kinase (ERK), we found that the very specific MAPK kinase (MEK) inhibitor, PD098059, inhibited the zona pellucida (ZP) induced acrosome reaction. As an intact acrosome on the spermatozoa is a prerequisite in ensuring tight binding to the ZP, we investigated the zona binding potential of spermatozoa after PD098059 treatment of sperm, followed by exposure to solubilised human ZP and calcium ionophore (A23187). PD098059 treated spermatozoa, exposed to solubilised ZP, bound significantly more to the ZP, as compared to control spermatozoa also exposed to solubilised ZP (26.5±3.7 vs. 13.8±2.8, P |
| doi_str_mv | 10.1046/j.0303-4569.2001.00475.x |
| format | Article |
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S. ; Page, C. ; Franken, D. R.</creator><creatorcontrib>Du Plessis, S. S. ; Page, C. ; Franken, D. R.</creatorcontrib><description>In a previous study involving the inhibition of the mitogen‐activated protein kinase (MAPK), extracellular signal regulated kinase (ERK), we found that the very specific MAPK kinase (MEK) inhibitor, PD098059, inhibited the zona pellucida (ZP) induced acrosome reaction. As an intact acrosome on the spermatozoa is a prerequisite in ensuring tight binding to the ZP, we investigated the zona binding potential of spermatozoa after PD098059 treatment of sperm, followed by exposure to solubilised human ZP and calcium ionophore (A23187). PD098059 treated spermatozoa, exposed to solubilised ZP, bound significantly more to the ZP, as compared to control spermatozoa also exposed to solubilised ZP (26.5±3.7 vs. 13.8±2.8, P<0.05). No significant differences in binding to the ZP were observed between PD098059 treated and untreated sperm populations after A23187 exposure. These results can be interpreted to support the idea that the ZP‐induced AR is the physiologically relevant exocytotic event, as it is the ZP‐induced AR, and not the spontaneous (culture medium) or A23187 induced AR, that appears to be mediated through an ERK‐mediated signal transduction process.</description><identifier>ISSN: 0303-4569</identifier><identifier>EISSN: 1439-0272</identifier><identifier>DOI: 10.1046/j.0303-4569.2001.00475.x</identifier><identifier>PMID: 11996182</identifier><identifier>CODEN: ANDRDQ</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science, Ltd</publisher><subject>Acrosome ; Biological and medical sciences ; Calcimycin - pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors ; Enzyme Activation ; Enzyme Inhibitors - pharmacology ; ERK ; Female ; Flavonoids - pharmacology ; hemizona ; Humans ; Ionophores - pharmacology ; Male ; Mitogen-Activated Protein Kinases - metabolism ; Signal Transduction ; Sperm-Ovum Interactions ; spermatozoa ; Spermatozoa - drug effects ; Spermatozoa - metabolism ; zona pellucida ; Zona Pellucida - metabolism</subject><ispartof>Andrologia, 2002-02, Vol.34 (1), p.55-59</ispartof><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.0303-4569.2001.00475.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.0303-4569.2001.00475.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13476530$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11996182$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Du Plessis, S. S.</creatorcontrib><creatorcontrib>Page, C.</creatorcontrib><creatorcontrib>Franken, D. R.</creatorcontrib><title>Extracellular signal-regulated kinase activation involved in human sperm-zona pellucida binding</title><title>Andrologia</title><addtitle>Andrologia</addtitle><description>In a previous study involving the inhibition of the mitogen‐activated protein kinase (MAPK), extracellular signal regulated kinase (ERK), we found that the very specific MAPK kinase (MEK) inhibitor, PD098059, inhibited the zona pellucida (ZP) induced acrosome reaction. As an intact acrosome on the spermatozoa is a prerequisite in ensuring tight binding to the ZP, we investigated the zona binding potential of spermatozoa after PD098059 treatment of sperm, followed by exposure to solubilised human ZP and calcium ionophore (A23187). PD098059 treated spermatozoa, exposed to solubilised ZP, bound significantly more to the ZP, as compared to control spermatozoa also exposed to solubilised ZP (26.5±3.7 vs. 13.8±2.8, P<0.05). No significant differences in binding to the ZP were observed between PD098059 treated and untreated sperm populations after A23187 exposure. These results can be interpreted to support the idea that the ZP‐induced AR is the physiologically relevant exocytotic event, as it is the ZP‐induced AR, and not the spontaneous (culture medium) or A23187 induced AR, that appears to be mediated through an ERK‐mediated signal transduction process.</description><subject>Acrosome</subject><subject>Biological and medical sciences</subject><subject>Calcimycin - pharmacology</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</subject><subject>Enzyme Activation</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>ERK</subject><subject>Female</subject><subject>Flavonoids - pharmacology</subject><subject>hemizona</subject><subject>Humans</subject><subject>Ionophores - pharmacology</subject><subject>Male</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Signal Transduction</subject><subject>Sperm-Ovum Interactions</subject><subject>spermatozoa</subject><subject>Spermatozoa - drug effects</subject><subject>Spermatozoa - metabolism</subject><subject>zona pellucida</subject><subject>Zona Pellucida - metabolism</subject><issn>0303-4569</issn><issn>1439-0272</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkU9v1DAQxS0EoqulXwH5ArcE_3cscalKW0BV2UMlJC7WbOIs3ibOYifLlk-Pwy6tL-PR_N5I8x5CmJKSEqE-bEvCCS-EVKZkhNCSEKFleXiBFlRwUxCm2Uu0eILO0HlKW5KfkFoL8RqdUWqMohVbIHt1GCPUruumDiJOfhOgK6Lb5HZ0DX7wAZLDUI9-D6MfAvZhP3T7PPIB_5x6CDjtXOyLP0MAvJsX1b4BvPah8WHzBr1qoUvu_FSX6P766v7yc3H77ebL5cVt4TmrZMEkYQRAs3XNqpZpZUyljdStqListalZvpQpqThwbrhsW0KBaUfWjXFO8iV6f1y7i8OvyaXR9j7NV0Fww5SspqqqGBEZfHsCp3XvGruLvof4aP87koF3JwBSDV0bIdQ-PXNcaCWztUv08cj99p17fJ4TO4dkt3b2387-2zkk-y8ke7AXd5_yJ8uLo9yn0R2e5BAfrNI8k9_vbuxqxciPleL2K_8LroiTLw</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>Du Plessis, S. S.</creator><creator>Page, C.</creator><creator>Franken, D. R.</creator><general>Blackwell Science, Ltd</general><general>Blackwell</general><scope>BSCLL</scope><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>20020201</creationdate><title>Extracellular signal-regulated kinase activation involved in human sperm-zona pellucida binding</title><author>Du Plessis, S. S. ; Page, C. ; Franken, D. R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i3285-25020aa72bc28f2769987957f4835c79c220026563a33935ff01a27e0bd9ee53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Acrosome</topic><topic>Biological and medical sciences</topic><topic>Calcimycin - pharmacology</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</topic><topic>Enzyme Activation</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>ERK</topic><topic>Female</topic><topic>Flavonoids - pharmacology</topic><topic>hemizona</topic><topic>Humans</topic><topic>Ionophores - pharmacology</topic><topic>Male</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Signal Transduction</topic><topic>Sperm-Ovum Interactions</topic><topic>spermatozoa</topic><topic>Spermatozoa - drug effects</topic><topic>Spermatozoa - metabolism</topic><topic>zona pellucida</topic><topic>Zona Pellucida - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Du Plessis, S. S.</creatorcontrib><creatorcontrib>Page, C.</creatorcontrib><creatorcontrib>Franken, D. R.</creatorcontrib><collection>Istex</collection><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>Andrologia</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Du Plessis, S. S.</au><au>Page, C.</au><au>Franken, D. R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Extracellular signal-regulated kinase activation involved in human sperm-zona pellucida binding</atitle><jtitle>Andrologia</jtitle><addtitle>Andrologia</addtitle><date>2002-02-01</date><risdate>2002</risdate><volume>34</volume><issue>1</issue><spage>55</spage><epage>59</epage><pages>55-59</pages><issn>0303-4569</issn><eissn>1439-0272</eissn><coden>ANDRDQ</coden><abstract>In a previous study involving the inhibition of the mitogen‐activated protein kinase (MAPK), extracellular signal regulated kinase (ERK), we found that the very specific MAPK kinase (MEK) inhibitor, PD098059, inhibited the zona pellucida (ZP) induced acrosome reaction. As an intact acrosome on the spermatozoa is a prerequisite in ensuring tight binding to the ZP, we investigated the zona binding potential of spermatozoa after PD098059 treatment of sperm, followed by exposure to solubilised human ZP and calcium ionophore (A23187). PD098059 treated spermatozoa, exposed to solubilised ZP, bound significantly more to the ZP, as compared to control spermatozoa also exposed to solubilised ZP (26.5±3.7 vs. 13.8±2.8, P<0.05). No significant differences in binding to the ZP were observed between PD098059 treated and untreated sperm populations after A23187 exposure. These results can be interpreted to support the idea that the ZP‐induced AR is the physiologically relevant exocytotic event, as it is the ZP‐induced AR, and not the spontaneous (culture medium) or A23187 induced AR, that appears to be mediated through an ERK‐mediated signal transduction process.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science, Ltd</pub><pmid>11996182</pmid><doi>10.1046/j.0303-4569.2001.00475.x</doi><tpages>5</tpages></addata></record> |
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| subjects | Acrosome Biological and medical sciences Calcimycin - pharmacology Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors Enzyme Activation Enzyme Inhibitors - pharmacology ERK Female Flavonoids - pharmacology hemizona Humans Ionophores - pharmacology Male Mitogen-Activated Protein Kinases - metabolism Signal Transduction Sperm-Ovum Interactions spermatozoa Spermatozoa - drug effects Spermatozoa - metabolism zona pellucida Zona Pellucida - metabolism |
| title | Extracellular signal-regulated kinase activation involved in human sperm-zona pellucida binding |
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