Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium [Dogs]
Motility and protein phosphorylation have been measured under identical experimental conditions in ejaculated dog sperm lysed with low concentrations of Triton X-100 and reactivated with [gamma-32P]ATP. Cyclic AMP stimulates motility and protein phosphorylation while calcium inhibits motility and th...
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| Veröffentlicht in: | Biology of reproduction 1982-05, Vol.26 (4), p.745-763 |
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| creator | Tash, J S Means, A R |
| description | Motility and protein phosphorylation have been measured under identical experimental conditions in ejaculated dog sperm lysed
with low concentrations of Triton X-100 and reactivated with [gamma-32P]ATP. Cyclic AMP stimulates motility and protein phosphorylation
while calcium inhibits motility and the overall incorporation of phosphate into endogenous proteins. Analysis of 32P-labeled
sperm proteins on 1- and 2-dimensional polyacrylamide gels demonstrates that an enhanced phosphorylation of a defined number
of specific proteins is associated with cAMP-stimulated motility. A major axonemal proteins, namely tubulin, has been tentatively
identified as a phosphoprotein subject to regulation by cAMP. The phosphorylation of tubulin is almost completely dependent
upon cAMP and is not affected by microM calcium. On the other hand, the cAMP-dependent stimulated phosphorylation of the other
sperm proteins still occurs, but in most instances at a reduced rate in the presence of calcium. Two high molecular weight
(Mr) phosphoproteins (350,000 and 260,000 daltons) whose phosphorylation states are modified by cAMP and calcium also were
identified. It is suggested that 1 or both these proteins may be high Mr subunits of dynein. The phosphorylation of 1 of these
proteins is stimulated by cAMP, but not affected by calcium; the other is stimulated by cAMP and inhibited by calcium. Three
major cAMP-independent phosphoproteins of Mr 98,000, 43,000 and 26,000 have been identified. The phosphorylation of the 98,000
Mr protein is markedly reduced by micromolar calcium and not restored by cAMP. Using anticalmodulin drugs to inhibit motility,
we suggest that the inhibitory effects of calcium on flagellar motility may be mediated in part by calmodulin. We conclude
that the regulation of flagellar motility in cAMP and calcium includes mechanisms involving the control of the phosphorylation
state of sperm proteins, some of which may be axonemal components. |
| doi_str_mv | 10.1095/biolreprod26.4.745 |
| format | Article |
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with low concentrations of Triton X-100 and reactivated with [gamma-32P]ATP. Cyclic AMP stimulates motility and protein phosphorylation
while calcium inhibits motility and the overall incorporation of phosphate into endogenous proteins. Analysis of 32P-labeled
sperm proteins on 1- and 2-dimensional polyacrylamide gels demonstrates that an enhanced phosphorylation of a defined number
of specific proteins is associated with cAMP-stimulated motility. A major axonemal proteins, namely tubulin, has been tentatively
identified as a phosphoprotein subject to regulation by cAMP. The phosphorylation of tubulin is almost completely dependent
upon cAMP and is not affected by microM calcium. On the other hand, the cAMP-dependent stimulated phosphorylation of the other
sperm proteins still occurs, but in most instances at a reduced rate in the presence of calcium. Two high molecular weight
(Mr) phosphoproteins (350,000 and 260,000 daltons) whose phosphorylation states are modified by cAMP and calcium also were
identified. It is suggested that 1 or both these proteins may be high Mr subunits of dynein. The phosphorylation of 1 of these
proteins is stimulated by cAMP, but not affected by calcium; the other is stimulated by cAMP and inhibited by calcium. Three
major cAMP-independent phosphoproteins of Mr 98,000, 43,000 and 26,000 have been identified. The phosphorylation of the 98,000
Mr protein is markedly reduced by micromolar calcium and not restored by cAMP. Using anticalmodulin drugs to inhibit motility,
we suggest that the inhibitory effects of calcium on flagellar motility may be mediated in part by calmodulin. We conclude
that the regulation of flagellar motility in cAMP and calcium includes mechanisms involving the control of the phosphorylation
state of sperm proteins, some of which may be axonemal components.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod26.4.745</identifier><identifier>PMID: 6282354</identifier><language>eng</language><publisher>United States: Society for the Study of Reproduction</publisher><subject>Animals ; Calcium - pharmacology ; Calmodulin - analysis ; Calmodulin - antagonists & inhibitors ; Cyclic AMP - pharmacology ; Dogs ; Fluorides - pharmacology ; Hydrogen-Ion Concentration ; Male ; Models, Biological ; Phosphoproteins - analysis ; Phosphorylation ; Protein Kinases - analysis ; Proteins - metabolism ; Sperm Motility - drug effects ; Spermatozoa - analysis ; Time Factors ; Tubulin - analysis</subject><ispartof>Biology of reproduction, 1982-05, Vol.26 (4), p.745-763</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-fce35afc33d48c429608cf2c45608f2586046f4a15258622d980e5dd9d72d3e33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6282354$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tash, J S</creatorcontrib><creatorcontrib>Means, A R</creatorcontrib><creatorcontrib>Centro Nacional de Pesquisa de Suinos e Aves, Concordia, SC (Brazil)</creatorcontrib><title>Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium [Dogs]</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>Motility and protein phosphorylation have been measured under identical experimental conditions in ejaculated dog sperm lysed
with low concentrations of Triton X-100 and reactivated with [gamma-32P]ATP. Cyclic AMP stimulates motility and protein phosphorylation
while calcium inhibits motility and the overall incorporation of phosphate into endogenous proteins. Analysis of 32P-labeled
sperm proteins on 1- and 2-dimensional polyacrylamide gels demonstrates that an enhanced phosphorylation of a defined number
of specific proteins is associated with cAMP-stimulated motility. A major axonemal proteins, namely tubulin, has been tentatively
identified as a phosphoprotein subject to regulation by cAMP. The phosphorylation of tubulin is almost completely dependent
upon cAMP and is not affected by microM calcium. On the other hand, the cAMP-dependent stimulated phosphorylation of the other
sperm proteins still occurs, but in most instances at a reduced rate in the presence of calcium. Two high molecular weight
(Mr) phosphoproteins (350,000 and 260,000 daltons) whose phosphorylation states are modified by cAMP and calcium also were
identified. It is suggested that 1 or both these proteins may be high Mr subunits of dynein. The phosphorylation of 1 of these
proteins is stimulated by cAMP, but not affected by calcium; the other is stimulated by cAMP and inhibited by calcium. Three
major cAMP-independent phosphoproteins of Mr 98,000, 43,000 and 26,000 have been identified. The phosphorylation of the 98,000
Mr protein is markedly reduced by micromolar calcium and not restored by cAMP. Using anticalmodulin drugs to inhibit motility,
we suggest that the inhibitory effects of calcium on flagellar motility may be mediated in part by calmodulin. We conclude
that the regulation of flagellar motility in cAMP and calcium includes mechanisms involving the control of the phosphorylation
state of sperm proteins, some of which may be axonemal components.</description><subject>Animals</subject><subject>Calcium - pharmacology</subject><subject>Calmodulin - analysis</subject><subject>Calmodulin - antagonists & inhibitors</subject><subject>Cyclic AMP - pharmacology</subject><subject>Dogs</subject><subject>Fluorides - pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Male</subject><subject>Models, Biological</subject><subject>Phosphoproteins - analysis</subject><subject>Phosphorylation</subject><subject>Protein Kinases - analysis</subject><subject>Proteins - metabolism</subject><subject>Sperm Motility - drug effects</subject><subject>Spermatozoa - analysis</subject><subject>Time Factors</subject><subject>Tubulin - analysis</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkF9rFDEUxYModdv6BQRlXvRt1kz-zeRRWq1CQdD2qUjIJje7kcxkTGZY5ts3dRbpw-VeOL9z4B6E3jZ422DJP-18DAnGFC0RW7ZtGX-BNg0nsm6J6F6iDcZY1JQK-hqd5_wH44ZRQs_QmSAdoZxt0PgT9nPQk49DFV1VsibwQzUeYi6TlpOkB1v1cfLBT8sTl0dIfbVbKrOY4E2lLQwx-wEKNcTVrSf45zM6GD_31cN13Offl-iV0yHDm9O-QPdfv9xdfatvf9x8v_p8Wxsmmql2BijXzlBqWWcYkQJ3xhHDeDkc4Z3ATDimy7flJsTKDgO3VtqWWAqUXqCPa2556e8MeVK9zwZC0APEOauWYUkwkwUkK2hSzDmBU2PyvU6LarB6qlk9r1mx4uTF9O6UPu96sP8tp16L_mHVD35_OPoEKvc6hEJTdTwen-W8Xzmno9L75LO6_9XIjuJOMsZb-gjmGJPh</recordid><startdate>198205</startdate><enddate>198205</enddate><creator>Tash, J S</creator><creator>Means, A R</creator><general>Society for the Study of Reproduction</general><scope>FBQ</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>198205</creationdate><title>Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium [Dogs]</title><author>Tash, J S ; Means, A R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-fce35afc33d48c429608cf2c45608f2586046f4a15258622d980e5dd9d72d3e33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>Calcium - pharmacology</topic><topic>Calmodulin - analysis</topic><topic>Calmodulin - antagonists & inhibitors</topic><topic>Cyclic AMP - pharmacology</topic><topic>Dogs</topic><topic>Fluorides - pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Male</topic><topic>Models, Biological</topic><topic>Phosphoproteins - analysis</topic><topic>Phosphorylation</topic><topic>Protein Kinases - analysis</topic><topic>Proteins - metabolism</topic><topic>Sperm Motility - drug effects</topic><topic>Spermatozoa - analysis</topic><topic>Time Factors</topic><topic>Tubulin - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tash, J S</creatorcontrib><creatorcontrib>Means, A R</creatorcontrib><creatorcontrib>Centro Nacional de Pesquisa de Suinos e Aves, Concordia, SC (Brazil)</creatorcontrib><collection>AGRIS</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>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tash, J S</au><au>Means, A R</au><aucorp>Centro Nacional de Pesquisa de Suinos e Aves, Concordia, SC (Brazil)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium [Dogs]</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>1982-05</date><risdate>1982</risdate><volume>26</volume><issue>4</issue><spage>745</spage><epage>763</epage><pages>745-763</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><abstract>Motility and protein phosphorylation have been measured under identical experimental conditions in ejaculated dog sperm lysed
with low concentrations of Triton X-100 and reactivated with [gamma-32P]ATP. Cyclic AMP stimulates motility and protein phosphorylation
while calcium inhibits motility and the overall incorporation of phosphate into endogenous proteins. Analysis of 32P-labeled
sperm proteins on 1- and 2-dimensional polyacrylamide gels demonstrates that an enhanced phosphorylation of a defined number
of specific proteins is associated with cAMP-stimulated motility. A major axonemal proteins, namely tubulin, has been tentatively
identified as a phosphoprotein subject to regulation by cAMP. The phosphorylation of tubulin is almost completely dependent
upon cAMP and is not affected by microM calcium. On the other hand, the cAMP-dependent stimulated phosphorylation of the other
sperm proteins still occurs, but in most instances at a reduced rate in the presence of calcium. Two high molecular weight
(Mr) phosphoproteins (350,000 and 260,000 daltons) whose phosphorylation states are modified by cAMP and calcium also were
identified. It is suggested that 1 or both these proteins may be high Mr subunits of dynein. The phosphorylation of 1 of these
proteins is stimulated by cAMP, but not affected by calcium; the other is stimulated by cAMP and inhibited by calcium. Three
major cAMP-independent phosphoproteins of Mr 98,000, 43,000 and 26,000 have been identified. The phosphorylation of the 98,000
Mr protein is markedly reduced by micromolar calcium and not restored by cAMP. Using anticalmodulin drugs to inhibit motility,
we suggest that the inhibitory effects of calcium on flagellar motility may be mediated in part by calmodulin. We conclude
that the regulation of flagellar motility in cAMP and calcium includes mechanisms involving the control of the phosphorylation
state of sperm proteins, some of which may be axonemal components.</abstract><cop>United States</cop><pub>Society for the Study of Reproduction</pub><pmid>6282354</pmid><doi>10.1095/biolreprod26.4.745</doi><tpages>19</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3363 |
| ispartof | Biology of reproduction, 1982-05, Vol.26 (4), p.745-763 |
| issn | 0006-3363 1529-7268 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74092049 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Calcium - pharmacology Calmodulin - analysis Calmodulin - antagonists & inhibitors Cyclic AMP - pharmacology Dogs Fluorides - pharmacology Hydrogen-Ion Concentration Male Models, Biological Phosphoproteins - analysis Phosphorylation Protein Kinases - analysis Proteins - metabolism Sperm Motility - drug effects Spermatozoa - analysis Time Factors Tubulin - analysis |
| title | Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium [Dogs] |
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