Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction
The sperm acrosome reaction and penetration of the egg follow zona pellucida binding only if the sperm has previously undergone the poorly understood maturation process known as capacitation. We demonstrate here that in vitro capacitation of bull, ram, mouse, and human sperm was accompanied by a tim...
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| Veröffentlicht in: | Biology of reproduction 2003-03, Vol.68 (3), p.837-845 |
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| creator | Brener, E Rubinstein, S Cohen, G Shternall, K Rivlin, J Breibart, H |
| description | The sperm acrosome reaction and penetration of the egg follow zona pellucida binding only if the sperm has previously undergone
the poorly understood maturation process known as capacitation. We demonstrate here that in vitro capacitation of bull, ram,
mouse, and human sperm was accompanied by a time-dependent increase in actin polymerization. Induction of the acrosome reaction
in capacitated cells initiated fast F-actin breakdown. Incubation of sperm in media lacking BSA or methyl-β-cyclodextrin,
Ca 2+ , or NaHCO 3 , components that are all required for capacitation, prevented actin polymerization as well as capacitation, as assessed by
the ability of the cells to undergo the acrosome reaction. Inhibition of F-actin formation by cytochalasin D blocked sperm
capacitation and reduced the in vitro fertilization rate of metaphase II-arrested mouse eggs. It has been suggested that protein
tyrosine phosphorylation may represent an important regulatory pathway that is associated with sperm capacitation. We show
here that factors known to stimulate sperm protein tyrosine phosphorylation (i.e., NaHCO 3 , cAMP, epidermal growth factor, H 2 O 2 , and sodium vanadate) were able to enhance actin polymerization, whereas inhibition of tyrosine kinases prevented F-actin
formation. These data suggest that actin polymerization may represent an important regulatory pathway in with sperm capacitation,
whereas F-actin breakdown occurs before the acrosome reaction. |
| doi_str_mv | 10.1095/biolreprod.102.009233 |
| format | Article |
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the poorly understood maturation process known as capacitation. We demonstrate here that in vitro capacitation of bull, ram,
mouse, and human sperm was accompanied by a time-dependent increase in actin polymerization. Induction of the acrosome reaction
in capacitated cells initiated fast F-actin breakdown. Incubation of sperm in media lacking BSA or methyl-β-cyclodextrin,
Ca 2+ , or NaHCO 3 , components that are all required for capacitation, prevented actin polymerization as well as capacitation, as assessed by
the ability of the cells to undergo the acrosome reaction. Inhibition of F-actin formation by cytochalasin D blocked sperm
capacitation and reduced the in vitro fertilization rate of metaphase II-arrested mouse eggs. It has been suggested that protein
tyrosine phosphorylation may represent an important regulatory pathway that is associated with sperm capacitation. We show
here that factors known to stimulate sperm protein tyrosine phosphorylation (i.e., NaHCO 3 , cAMP, epidermal growth factor, H 2 O 2 , and sodium vanadate) were able to enhance actin polymerization, whereas inhibition of tyrosine kinases prevented F-actin
formation. These data suggest that actin polymerization may represent an important regulatory pathway in with sperm capacitation,
whereas F-actin breakdown occurs before the acrosome reaction.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod.102.009233</identifier><identifier>PMID: 12604633</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>acrosome reaction ; Acrosome Reaction - physiology ; actin ; actin remodeling ; Actins - physiology ; Animals ; Biological and medical sciences ; bulls ; Calcimycin - pharmacology ; Calcium - antagonists & inhibitors ; Calcium - physiology ; capacitation ; Cattle ; cytochalasin D ; cytoskeleton ; Cytoskeleton - physiology ; depolymerization ; enzyme inhibitors ; Female ; Fertilization in Vitro ; Fundamental and applied biological sciences. Psychology ; Humans ; Immunoblotting ; in vitro fertilization ; Ionophores - pharmacology ; Male ; Mammalian male genital system ; Mice ; Mice, Inbred BALB C ; Microscopy, Fluorescence ; Morphology. Physiology ; polymerization ; protein phosphorylation ; rams ; Sheep ; Sperm Capacitation - physiology ; Sperm-Ovum Interactions - physiology ; spermatozoa ; Spermatozoa - physiology ; tyrosine ; tyrosine phosphorylation ; Vertebrates: reproduction</subject><ispartof>Biology of reproduction, 2003-03, Vol.68 (3), p.837-845</ispartof><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14568396$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12604633$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brener, E</creatorcontrib><creatorcontrib>Rubinstein, S</creatorcontrib><creatorcontrib>Cohen, G</creatorcontrib><creatorcontrib>Shternall, K</creatorcontrib><creatorcontrib>Rivlin, J</creatorcontrib><creatorcontrib>Breibart, H</creatorcontrib><title>Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>The sperm acrosome reaction and penetration of the egg follow zona pellucida binding only if the sperm has previously undergone
the poorly understood maturation process known as capacitation. We demonstrate here that in vitro capacitation of bull, ram,
mouse, and human sperm was accompanied by a time-dependent increase in actin polymerization. Induction of the acrosome reaction
in capacitated cells initiated fast F-actin breakdown. Incubation of sperm in media lacking BSA or methyl-β-cyclodextrin,
Ca 2+ , or NaHCO 3 , components that are all required for capacitation, prevented actin polymerization as well as capacitation, as assessed by
the ability of the cells to undergo the acrosome reaction. Inhibition of F-actin formation by cytochalasin D blocked sperm
capacitation and reduced the in vitro fertilization rate of metaphase II-arrested mouse eggs. It has been suggested that protein
tyrosine phosphorylation may represent an important regulatory pathway that is associated with sperm capacitation. We show
here that factors known to stimulate sperm protein tyrosine phosphorylation (i.e., NaHCO 3 , cAMP, epidermal growth factor, H 2 O 2 , and sodium vanadate) were able to enhance actin polymerization, whereas inhibition of tyrosine kinases prevented F-actin
formation. These data suggest that actin polymerization may represent an important regulatory pathway in with sperm capacitation,
whereas F-actin breakdown occurs before the acrosome reaction.</description><subject>acrosome reaction</subject><subject>Acrosome Reaction - physiology</subject><subject>actin</subject><subject>actin remodeling</subject><subject>Actins - physiology</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>bulls</subject><subject>Calcimycin - pharmacology</subject><subject>Calcium - antagonists & inhibitors</subject><subject>Calcium - physiology</subject><subject>capacitation</subject><subject>Cattle</subject><subject>cytochalasin D</subject><subject>cytoskeleton</subject><subject>Cytoskeleton - physiology</subject><subject>depolymerization</subject><subject>enzyme inhibitors</subject><subject>Female</subject><subject>Fertilization in Vitro</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>in vitro fertilization</subject><subject>Ionophores - pharmacology</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microscopy, Fluorescence</subject><subject>Morphology. Physiology</subject><subject>polymerization</subject><subject>protein phosphorylation</subject><subject>rams</subject><subject>Sheep</subject><subject>Sperm Capacitation - physiology</subject><subject>Sperm-Ovum Interactions - physiology</subject><subject>spermatozoa</subject><subject>Spermatozoa - physiology</subject><subject>tyrosine</subject><subject>tyrosine phosphorylation</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpF0V1vFCEUBmBiNHb78RPUudG7qcAZBrg0TbUmTUzU3pawzGEXhWGF2Wz670vTNb06IXl4c_IeQt4xesmoFp_XIceCu5Kn9uaXlGoO8IqsmOC6l3xUr8mKUjr2ACOckNNa_1DKBuDwlpwwPtJhBFiR-5-Y8oQxzJsu-27ZYmfdEubOPSy5_sWIS567aV-eQLIp2Rjs3NUdltQ5u7MuLHYJzdh5al9LrjlhV_ApJc_n5I23seLFcZ6Ru6_Xv69u-tsf375ffbntPdds6QfUTnDhlRKo9DRxKbyXTAyK8YGDFYJKCUKNfu08rKVSbFJMOYdMas0onJFPz7mtkH97rItJoTqM0c6Y99VIoEMLYQ2-P8L9OuFkdiUkWx7M_0Ya-HgEtjobfbGzC_XFDWJUoMcXtw2b7SEUNLV1E1ssmMPhMCoDRoFs7sOz8zYbuykt6-4Xb5u0iwkt29UeAS8BiQc</recordid><startdate>20030301</startdate><enddate>20030301</enddate><creator>Brener, E</creator><creator>Rubinstein, S</creator><creator>Cohen, G</creator><creator>Shternall, K</creator><creator>Rivlin, J</creator><creator>Breibart, H</creator><general>Society for the Study of Reproduction</general><scope>FBQ</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>20030301</creationdate><title>Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction</title><author>Brener, E ; Rubinstein, S ; Cohen, G ; Shternall, K ; Rivlin, J ; Breibart, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f291t-4e9c525f885e89dd275ff7154812423a550773586fbcf3b7881d818cce1799103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>acrosome reaction</topic><topic>Acrosome Reaction - physiology</topic><topic>actin</topic><topic>actin remodeling</topic><topic>Actins - physiology</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>bulls</topic><topic>Calcimycin - pharmacology</topic><topic>Calcium - antagonists & inhibitors</topic><topic>Calcium - physiology</topic><topic>capacitation</topic><topic>Cattle</topic><topic>cytochalasin D</topic><topic>cytoskeleton</topic><topic>Cytoskeleton - physiology</topic><topic>depolymerization</topic><topic>enzyme inhibitors</topic><topic>Female</topic><topic>Fertilization in Vitro</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>in vitro fertilization</topic><topic>Ionophores - pharmacology</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microscopy, Fluorescence</topic><topic>Morphology. Physiology</topic><topic>polymerization</topic><topic>protein phosphorylation</topic><topic>rams</topic><topic>Sheep</topic><topic>Sperm Capacitation - physiology</topic><topic>Sperm-Ovum Interactions - physiology</topic><topic>spermatozoa</topic><topic>Spermatozoa - physiology</topic><topic>tyrosine</topic><topic>tyrosine phosphorylation</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brener, E</creatorcontrib><creatorcontrib>Rubinstein, S</creatorcontrib><creatorcontrib>Cohen, G</creatorcontrib><creatorcontrib>Shternall, K</creatorcontrib><creatorcontrib>Rivlin, J</creatorcontrib><creatorcontrib>Breibart, H</creatorcontrib><collection>AGRIS</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>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brener, E</au><au>Rubinstein, S</au><au>Cohen, G</au><au>Shternall, K</au><au>Rivlin, J</au><au>Breibart, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2003-03-01</date><risdate>2003</risdate><volume>68</volume><issue>3</issue><spage>837</spage><epage>845</epage><pages>837-845</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>The sperm acrosome reaction and penetration of the egg follow zona pellucida binding only if the sperm has previously undergone
the poorly understood maturation process known as capacitation. We demonstrate here that in vitro capacitation of bull, ram,
mouse, and human sperm was accompanied by a time-dependent increase in actin polymerization. Induction of the acrosome reaction
in capacitated cells initiated fast F-actin breakdown. Incubation of sperm in media lacking BSA or methyl-β-cyclodextrin,
Ca 2+ , or NaHCO 3 , components that are all required for capacitation, prevented actin polymerization as well as capacitation, as assessed by
the ability of the cells to undergo the acrosome reaction. Inhibition of F-actin formation by cytochalasin D blocked sperm
capacitation and reduced the in vitro fertilization rate of metaphase II-arrested mouse eggs. It has been suggested that protein
tyrosine phosphorylation may represent an important regulatory pathway that is associated with sperm capacitation. We show
here that factors known to stimulate sperm protein tyrosine phosphorylation (i.e., NaHCO 3 , cAMP, epidermal growth factor, H 2 O 2 , and sodium vanadate) were able to enhance actin polymerization, whereas inhibition of tyrosine kinases prevented F-actin
formation. These data suggest that actin polymerization may represent an important regulatory pathway in with sperm capacitation,
whereas F-actin breakdown occurs before the acrosome reaction.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>12604633</pmid><doi>10.1095/biolreprod.102.009233</doi><tpages>9</tpages></addata></record> |
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| source | MEDLINE; BioOne Complete; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals |
| subjects | acrosome reaction Acrosome Reaction - physiology actin actin remodeling Actins - physiology Animals Biological and medical sciences bulls Calcimycin - pharmacology Calcium - antagonists & inhibitors Calcium - physiology capacitation Cattle cytochalasin D cytoskeleton Cytoskeleton - physiology depolymerization enzyme inhibitors Female Fertilization in Vitro Fundamental and applied biological sciences. Psychology Humans Immunoblotting in vitro fertilization Ionophores - pharmacology Male Mammalian male genital system Mice Mice, Inbred BALB C Microscopy, Fluorescence Morphology. Physiology polymerization protein phosphorylation rams Sheep Sperm Capacitation - physiology Sperm-Ovum Interactions - physiology spermatozoa Spermatozoa - physiology tyrosine tyrosine phosphorylation Vertebrates: reproduction |
| title | Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction |
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