Na+/K+ATPase as a Signaling Molecule During Bovine Sperm Capacitation

A heteromeric integral membrane protein, Na + /K + ATPase is composed of two polypeptides, alpha and beta, and is active in many cell types, including testis and spermatozoa. It is a well-known ion transporter, but binding of ouabain, a specific inhibitor of Na + /K + ATPase, to Na + /K + ATPase in...

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Veröffentlicht in:Biology of reproduction 2006-09, Vol.75 (3), p.308-317
Hauptverfasser: THUNDATHIL, Jacob C, ANZAR, Muhammad, BUHR, Mary M
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ANZAR, Muhammad
BUHR, Mary M
description A heteromeric integral membrane protein, Na + /K + ATPase is composed of two polypeptides, alpha and beta, and is active in many cell types, including testis and spermatozoa. It is a well-known ion transporter, but binding of ouabain, a specific inhibitor of Na + /K + ATPase, to Na + /K + ATPase in somatic cells initiates responses that are similar to signaling events associated with bovine sperm capacitation. The objectives of the present study were to demonstrate the presence of Na + /K + ATPase in bovine sperm and to investigate its role in the regulation of bovine sperm capacitation. The presence of Na + /K + ATPase in sperm from mature Holstein bulls was demonstrated by immunoblotting and immunocytochemistry using a monoclonal antibody developed in mouse against the beta 1 polypeptide of Na + /K + ATPase. Binding of ouabain to Na + /K + ATPase inhibited motility (decreased progressive motility, average path velocity, and curvilinear velocity) and induced tyrosine phosphorylation and capacitation but did not increase intracellular calcium levels in spermatozoa. Furthermore, binding of ouabain to Na + /K + ATPase induced depolarization of sperm plasma membrane. Therefore, binding of ouabain to Na + /K + ATPase induced sperm capacitation through depolarization of sperm plasma membrane and signaling via the tyrosine phosphorylation pathway without an appreciable increase in intracellular calcium. To our knowledge, this is the first report concerning the signaling role of Na + /K + ATPase in mammalian sperm capacitation. Abstract Na + /K + ATPase is involved in the regulation of protein tyrosine phosphorylation and capacitation of bovine spermatozoa.
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It is a well-known ion transporter, but binding of ouabain, a specific inhibitor of Na + /K + ATPase, to Na + /K + ATPase in somatic cells initiates responses that are similar to signaling events associated with bovine sperm capacitation. The objectives of the present study were to demonstrate the presence of Na + /K + ATPase in bovine sperm and to investigate its role in the regulation of bovine sperm capacitation. The presence of Na + /K + ATPase in sperm from mature Holstein bulls was demonstrated by immunoblotting and immunocytochemistry using a monoclonal antibody developed in mouse against the beta 1 polypeptide of Na + /K + ATPase. Binding of ouabain to Na + /K + ATPase inhibited motility (decreased progressive motility, average path velocity, and curvilinear velocity) and induced tyrosine phosphorylation and capacitation but did not increase intracellular calcium levels in spermatozoa. Furthermore, binding of ouabain to Na + /K + ATPase induced depolarization of sperm plasma membrane. Therefore, binding of ouabain to Na + /K + ATPase induced sperm capacitation through depolarization of sperm plasma membrane and signaling via the tyrosine phosphorylation pathway without an appreciable increase in intracellular calcium. To our knowledge, this is the first report concerning the signaling role of Na + /K + ATPase in mammalian sperm capacitation. Abstract Na + /K + ATPase is involved in the regulation of protein tyrosine phosphorylation and capacitation of bovine spermatozoa.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod.105.047852</identifier><identifier>PMID: 16687652</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Animals ; Biological and medical sciences ; Calcium - metabolism ; Cattle ; Cell Membrane - physiology ; Enzyme Inhibitors - pharmacology ; Fundamental and applied biological sciences. Psychology ; Immunohistochemistry ; In Vitro Techniques ; Indicators and Reagents ; Male ; Mammalian male genital system ; Membrane Potentials - physiology ; Morphology. 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It is a well-known ion transporter, but binding of ouabain, a specific inhibitor of Na + /K + ATPase, to Na + /K + ATPase in somatic cells initiates responses that are similar to signaling events associated with bovine sperm capacitation. The objectives of the present study were to demonstrate the presence of Na + /K + ATPase in bovine sperm and to investigate its role in the regulation of bovine sperm capacitation. The presence of Na + /K + ATPase in sperm from mature Holstein bulls was demonstrated by immunoblotting and immunocytochemistry using a monoclonal antibody developed in mouse against the beta 1 polypeptide of Na + /K + ATPase. Binding of ouabain to Na + /K + ATPase inhibited motility (decreased progressive motility, average path velocity, and curvilinear velocity) and induced tyrosine phosphorylation and capacitation but did not increase intracellular calcium levels in spermatozoa. Furthermore, binding of ouabain to Na + /K + ATPase induced depolarization of sperm plasma membrane. Therefore, binding of ouabain to Na + /K + ATPase induced sperm capacitation through depolarization of sperm plasma membrane and signaling via the tyrosine phosphorylation pathway without an appreciable increase in intracellular calcium. To our knowledge, this is the first report concerning the signaling role of Na + /K + ATPase in mammalian sperm capacitation. Abstract Na + /K + ATPase is involved in the regulation of protein tyrosine phosphorylation and capacitation of bovine spermatozoa.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Cattle</subject><subject>Cell Membrane - physiology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunohistochemistry</subject><subject>In Vitro Techniques</subject><subject>Indicators and Reagents</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Membrane Potentials - physiology</subject><subject>Morphology. Physiology</subject><subject>Ouabain - pharmacology</subject><subject>Phosphorylation</subject><subject>Signal Transduction - physiology</subject><subject>Sodium-Potassium-Exchanging ATPase - antagonists &amp; inhibitors</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><subject>Sodium-Potassium-Exchanging ATPase - physiology</subject><subject>Sperm Capacitation - physiology</subject><subject>Sperm Motility - physiology</subject><subject>Spermatozoa - enzymology</subject><subject>Tyrosine - metabolism</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFj8lOwzAURS0EoqXwCaBsYFOl9RAPWZZSBlEGqWUdvcZOa-QMxA0Vf48RRazeu9LR1T0InRM8Ijjl45WtXWuattYh8xFOpOL0APUJp2ksqVCHqI8xFjFjgvXQiffvGJOEUXaMekQIJQWnfTR7huH4cThZvoI3EfgIooVdV-BstY6eamfyzpnopmt_8nX9aSsTLRrTltEUGsjtFra2rk7RUQHOm7P9HaC329lyeh_PX-4eppN5vKEi3cYp0VwpSCCn2uiEUhweUgijw-hcE01IIZkGLCTmeaopJ9IQSYiiKWdasQG6-u0N3h-d8dustD43zkFl6s5nwUqmQvEAXuzBblUanTWtLaH9yv7EA3C5B8Dn4IoWqtz6f07hsJTgf25j15udbU3mS3Au1LJst9tJnrGMYcW-AWOPdQw</recordid><startdate>20060901</startdate><enddate>20060901</enddate><creator>THUNDATHIL, Jacob C</creator><creator>ANZAR, Muhammad</creator><creator>BUHR, Mary M</creator><general>Society for the Study of Reproduction</general><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>20060901</creationdate><title>Na+/K+ATPase as a Signaling Molecule During Bovine Sperm Capacitation</title><author>THUNDATHIL, Jacob C ; ANZAR, Muhammad ; BUHR, Mary M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h269t-91d588a4ac2ded4220c2d1f6ed529cd1d11f73da06705c9d2517e171182953d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium - metabolism</topic><topic>Cattle</topic><topic>Cell Membrane - physiology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunohistochemistry</topic><topic>In Vitro Techniques</topic><topic>Indicators and Reagents</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Membrane Potentials - physiology</topic><topic>Morphology. Physiology</topic><topic>Ouabain - pharmacology</topic><topic>Phosphorylation</topic><topic>Signal Transduction - physiology</topic><topic>Sodium-Potassium-Exchanging ATPase - antagonists &amp; inhibitors</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><topic>Sodium-Potassium-Exchanging ATPase - physiology</topic><topic>Sperm Capacitation - physiology</topic><topic>Sperm Motility - physiology</topic><topic>Spermatozoa - enzymology</topic><topic>Tyrosine - metabolism</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>THUNDATHIL, Jacob C</creatorcontrib><creatorcontrib>ANZAR, Muhammad</creatorcontrib><creatorcontrib>BUHR, Mary M</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>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>THUNDATHIL, Jacob C</au><au>ANZAR, Muhammad</au><au>BUHR, Mary M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Na+/K+ATPase as a Signaling Molecule During Bovine Sperm Capacitation</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2006-09-01</date><risdate>2006</risdate><volume>75</volume><issue>3</issue><spage>308</spage><epage>317</epage><pages>308-317</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>A heteromeric integral membrane protein, Na + /K + ATPase is composed of two polypeptides, alpha and beta, and is active in many cell types, including testis and spermatozoa. 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source MEDLINE; BioOne Complete; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals
subjects Animals
Biological and medical sciences
Calcium - metabolism
Cattle
Cell Membrane - physiology
Enzyme Inhibitors - pharmacology
Fundamental and applied biological sciences. Psychology
Immunohistochemistry
In Vitro Techniques
Indicators and Reagents
Male
Mammalian male genital system
Membrane Potentials - physiology
Morphology. Physiology
Ouabain - pharmacology
Phosphorylation
Signal Transduction - physiology
Sodium-Potassium-Exchanging ATPase - antagonists & inhibitors
Sodium-Potassium-Exchanging ATPase - metabolism
Sodium-Potassium-Exchanging ATPase - physiology
Sperm Capacitation - physiology
Sperm Motility - physiology
Spermatozoa - enzymology
Tyrosine - metabolism
Vertebrates: reproduction
title Na+/K+ATPase as a Signaling Molecule During Bovine Sperm Capacitation
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