Regulation of tyrosine kinase activity during capacitation in goat sperm
Protein tyrosine phosphorylation is a key event accompanying sperm capacitation. Although this signaling cascade generates an array of tyrosine-phosphorylated polypeptides, their molecular characterization is still limited. It is necessary to differentiate the localization of the tyrosine-phosphoryl...
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| Veröffentlicht in: | Molecular and cellular biochemistry 2010-03, Vol.336 (1-2), p.39-48 |
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| description | Protein tyrosine phosphorylation is a key event accompanying sperm capacitation. Although this signaling cascade generates an array of tyrosine-phosphorylated polypeptides, their molecular characterization is still limited. It is necessary to differentiate the localization of the tyrosine-phosphorylated proteins in spermatozoa to understand the link between the different phosphorylated proteins and the corresponding regulated sperm function. cAMP plays a pivotal role in the regulation of tyrosine phosphorylation. The intracellular cAMP levels were raised in goat spermatozoa by the addition of the phosphodiesterase inhibitor, IBMX in conjugation with caffeine. Tyrosine phosphorylation was significantly up-regulated following treatment with these two reagents. Treatment of caudal spermatozoa with IBMX and caffeine, time dependent up-regulated phosphorylation of the protein of molecular weights 50 and 200 kDa was observed. Increased phosphorylation was observed with a combination of IBMX and caffeine treatment. Tyrosine phosphorylation in caput spermatozoa was not affected significantly under these conditions. The expression level of tyrosine kinase in sperm was examined with specific inhibitors and with anti-phosphotyrosine antibody. The indirect immunofluorescence staining was carried out on ethanol permeabilized sperm using anti-phosphotyrosine antibody. Western blot analysis was done using two separate PKA antibodies: anti-PKA catalytic and anti-PKA RIα. Almost no difference was found in the intracellular presence of the PKA RIα and RIIα subunits in caput and caudal epididymal spermatozoa. However, the catalytic subunit seemed to be present in higher amount in caudal spermatozoa. The results show that caprine sperm displays an enhancement of phosphorylation in the tyrosine residues of specific proteins under in vitro capacitation conditions. |
| doi_str_mv | 10.1007/s11010-009-0261-8 |
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Although this signaling cascade generates an array of tyrosine-phosphorylated polypeptides, their molecular characterization is still limited. It is necessary to differentiate the localization of the tyrosine-phosphorylated proteins in spermatozoa to understand the link between the different phosphorylated proteins and the corresponding regulated sperm function. cAMP plays a pivotal role in the regulation of tyrosine phosphorylation. The intracellular cAMP levels were raised in goat spermatozoa by the addition of the phosphodiesterase inhibitor, IBMX in conjugation with caffeine. Tyrosine phosphorylation was significantly up-regulated following treatment with these two reagents. Treatment of caudal spermatozoa with IBMX and caffeine, time dependent up-regulated phosphorylation of the protein of molecular weights 50 and 200 kDa was observed. Increased phosphorylation was observed with a combination of IBMX and caffeine treatment. Tyrosine phosphorylation in caput spermatozoa was not affected significantly under these conditions. The expression level of tyrosine kinase in sperm was examined with specific inhibitors and with anti-phosphotyrosine antibody. The indirect immunofluorescence staining was carried out on ethanol permeabilized sperm using anti-phosphotyrosine antibody. Western blot analysis was done using two separate PKA antibodies: anti-PKA catalytic and anti-PKA RIα. Almost no difference was found in the intracellular presence of the PKA RIα and RIIα subunits in caput and caudal epididymal spermatozoa. However, the catalytic subunit seemed to be present in higher amount in caudal spermatozoa. The results show that caprine sperm displays an enhancement of phosphorylation in the tyrosine residues of specific proteins under in vitro capacitation conditions.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/s11010-009-0261-8</identifier><identifier>PMID: 19802524</identifier><language>eng</language><publisher>Boston: Boston : Springer US</publisher><subject>1-Methyl-3-isobutylxanthine - pharmacology ; Analysis ; Animal reproduction ; Animals ; Antibodies, Phospho-Specific ; Biochemistry ; Biomedical and Life Sciences ; Caffeine ; Caffeine - pharmacology ; Cardiology ; Cellular biology ; Cyclic AMP - metabolism ; Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Epididymis - cytology ; Ethanol ; Goats ; Kinases ; Life Sciences ; Male ; Medical Biochemistry ; Molecular biology ; Oncology ; Organ Specificity ; Phenols ; Phosphodiesterase Inhibitors - pharmacology ; Phosphoproteins - metabolism ; Phosphorylation - drug effects ; Protein Subunits - metabolism ; Protein Transport - drug effects ; Protein-Tyrosine Kinases - antagonists & inhibitors ; Protein-Tyrosine Kinases - metabolism ; Proteins ; Reagents ; Signal Transduction ; Sperm Capacitation - drug effects ; Sperm Capacitation - physiology ; Sperm Head - drug effects ; Sperm Head - metabolism ; Spermatozoa ; Spermatozoa - drug effects ; Spermatozoa - metabolism ; Spermatozoa - physiology ; Tyrosine ; Tyrosine - metabolism</subject><ispartof>Molecular and cellular biochemistry, 2010-03, Vol.336 (1-2), p.39-48</ispartof><rights>Springer Science+Business Media, LLC. 2009</rights><rights>COPYRIGHT 2010 Springer</rights><rights>Springer Science+Business Media, LLC. 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-406244e01cc5cc5209d361a6be2e2e12b7f8e73b2a8226d3c19eeb39a3d40e63</citedby><cites>FETCH-LOGICAL-c461t-406244e01cc5cc5209d361a6be2e2e12b7f8e73b2a8226d3c19eeb39a3d40e63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11010-009-0261-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11010-009-0261-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19802524$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chatterjee, Madhumouli</creatorcontrib><creatorcontrib>Nandi, Pinki</creatorcontrib><creatorcontrib>Ghosh, Swatilekha</creatorcontrib><creatorcontrib>Sen, Parimal C</creatorcontrib><title>Regulation of tyrosine kinase activity during capacitation in goat sperm</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><addtitle>Mol Cell Biochem</addtitle><description>Protein tyrosine phosphorylation is a key event accompanying sperm capacitation. Although this signaling cascade generates an array of tyrosine-phosphorylated polypeptides, their molecular characterization is still limited. It is necessary to differentiate the localization of the tyrosine-phosphorylated proteins in spermatozoa to understand the link between the different phosphorylated proteins and the corresponding regulated sperm function. cAMP plays a pivotal role in the regulation of tyrosine phosphorylation. The intracellular cAMP levels were raised in goat spermatozoa by the addition of the phosphodiesterase inhibitor, IBMX in conjugation with caffeine. Tyrosine phosphorylation was significantly up-regulated following treatment with these two reagents. Treatment of caudal spermatozoa with IBMX and caffeine, time dependent up-regulated phosphorylation of the protein of molecular weights 50 and 200 kDa was observed. Increased phosphorylation was observed with a combination of IBMX and caffeine treatment. Tyrosine phosphorylation in caput spermatozoa was not affected significantly under these conditions. The expression level of tyrosine kinase in sperm was examined with specific inhibitors and with anti-phosphotyrosine antibody. The indirect immunofluorescence staining was carried out on ethanol permeabilized sperm using anti-phosphotyrosine antibody. Western blot analysis was done using two separate PKA antibodies: anti-PKA catalytic and anti-PKA RIα. Almost no difference was found in the intracellular presence of the PKA RIα and RIIα subunits in caput and caudal epididymal spermatozoa. However, the catalytic subunit seemed to be present in higher amount in caudal spermatozoa. The results show that caprine sperm displays an enhancement of phosphorylation in the tyrosine residues of specific proteins under in vitro capacitation conditions.</description><subject>1-Methyl-3-isobutylxanthine - pharmacology</subject><subject>Analysis</subject><subject>Animal reproduction</subject><subject>Animals</subject><subject>Antibodies, Phospho-Specific</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Caffeine</subject><subject>Caffeine - pharmacology</subject><subject>Cardiology</subject><subject>Cellular biology</subject><subject>Cyclic AMP - metabolism</subject><subject>Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Epididymis - cytology</subject><subject>Ethanol</subject><subject>Goats</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Male</subject><subject>Medical Biochemistry</subject><subject>Molecular biology</subject><subject>Oncology</subject><subject>Organ Specificity</subject><subject>Phenols</subject><subject>Phosphodiesterase Inhibitors - pharmacology</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation - drug effects</subject><subject>Protein Subunits - metabolism</subject><subject>Protein Transport - drug effects</subject><subject>Protein-Tyrosine Kinases - antagonists & inhibitors</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins</subject><subject>Reagents</subject><subject>Signal Transduction</subject><subject>Sperm Capacitation - drug effects</subject><subject>Sperm Capacitation - physiology</subject><subject>Sperm Head - drug effects</subject><subject>Sperm Head - metabolism</subject><subject>Spermatozoa</subject><subject>Spermatozoa - drug effects</subject><subject>Spermatozoa - metabolism</subject><subject>Spermatozoa - physiology</subject><subject>Tyrosine</subject><subject>Tyrosine - metabolism</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kdGK1TAQhoO4uMfVB_BGi153nUnaJr1cFnWFhQVdr0OaTkvW06YmqXDefnPoARVkmYGB8P0zmfkZe4NwiQDyY0QEhBKgLYE3WKpnbIe1FGXVYvuc7UAAlAqlPGcvY3yADAPiC3aOrQJe82rHbr7RuO5Ncn4u_FCkQ_DRzVT8dLOJVBib3G-XDkW_BjePhTWLsS5tvJuL0ZtUxIXC9IqdDWYf6fWpXrD7z5_ur2_K27svX6-vbktbNZjKChpeVQRobZ2TQ9uLBk3TEc-BvJODIik6bhTnTS8stkSdaI3oK6BGXLD3W9sl-F8rxaQf_BrmPFFjK-u8LK8z9GGDRrMn7ebBp2Ds5KLVV6JWAhuQmKnL_1A5epqc9TMNLr__I8BNYPORYqBBL8FNJhw0gj4aojdDdDZEHw3RKmvenv67dhP1fxQnBzLANyAuxwtT-GuhJ7q-20SD8dqMwUX94zsHFIAKlKyUeASpk5zt</recordid><startdate>20100301</startdate><enddate>20100301</enddate><creator>Chatterjee, Madhumouli</creator><creator>Nandi, Pinki</creator><creator>Ghosh, Swatilekha</creator><creator>Sen, Parimal C</creator><general>Boston : Springer US</general><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope></search><sort><creationdate>20100301</creationdate><title>Regulation of tyrosine kinase activity during capacitation in goat sperm</title><author>Chatterjee, Madhumouli ; Nandi, Pinki ; Ghosh, Swatilekha ; Sen, Parimal C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-406244e01cc5cc5209d361a6be2e2e12b7f8e73b2a8226d3c19eeb39a3d40e63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>1-Methyl-3-isobutylxanthine - 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drug effects</topic><topic>Protein-Tyrosine Kinases - antagonists & inhibitors</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proteins</topic><topic>Reagents</topic><topic>Signal Transduction</topic><topic>Sperm Capacitation - drug effects</topic><topic>Sperm Capacitation - physiology</topic><topic>Sperm Head - drug effects</topic><topic>Sperm Head - metabolism</topic><topic>Spermatozoa</topic><topic>Spermatozoa - drug effects</topic><topic>Spermatozoa - metabolism</topic><topic>Spermatozoa - physiology</topic><topic>Tyrosine</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chatterjee, Madhumouli</creatorcontrib><creatorcontrib>Nandi, Pinki</creatorcontrib><creatorcontrib>Ghosh, Swatilekha</creatorcontrib><creatorcontrib>Sen, Parimal C</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><jtitle>Molecular and cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chatterjee, Madhumouli</au><au>Nandi, Pinki</au><au>Ghosh, Swatilekha</au><au>Sen, Parimal C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of tyrosine kinase activity during capacitation in goat sperm</atitle><jtitle>Molecular and cellular biochemistry</jtitle><stitle>Mol Cell Biochem</stitle><addtitle>Mol Cell Biochem</addtitle><date>2010-03-01</date><risdate>2010</risdate><volume>336</volume><issue>1-2</issue><spage>39</spage><epage>48</epage><pages>39-48</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>Protein tyrosine phosphorylation is a key event accompanying sperm capacitation. Although this signaling cascade generates an array of tyrosine-phosphorylated polypeptides, their molecular characterization is still limited. It is necessary to differentiate the localization of the tyrosine-phosphorylated proteins in spermatozoa to understand the link between the different phosphorylated proteins and the corresponding regulated sperm function. cAMP plays a pivotal role in the regulation of tyrosine phosphorylation. The intracellular cAMP levels were raised in goat spermatozoa by the addition of the phosphodiesterase inhibitor, IBMX in conjugation with caffeine. Tyrosine phosphorylation was significantly up-regulated following treatment with these two reagents. Treatment of caudal spermatozoa with IBMX and caffeine, time dependent up-regulated phosphorylation of the protein of molecular weights 50 and 200 kDa was observed. Increased phosphorylation was observed with a combination of IBMX and caffeine treatment. Tyrosine phosphorylation in caput spermatozoa was not affected significantly under these conditions. The expression level of tyrosine kinase in sperm was examined with specific inhibitors and with anti-phosphotyrosine antibody. The indirect immunofluorescence staining was carried out on ethanol permeabilized sperm using anti-phosphotyrosine antibody. Western blot analysis was done using two separate PKA antibodies: anti-PKA catalytic and anti-PKA RIα. Almost no difference was found in the intracellular presence of the PKA RIα and RIIα subunits in caput and caudal epididymal spermatozoa. However, the catalytic subunit seemed to be present in higher amount in caudal spermatozoa. The results show that caprine sperm displays an enhancement of phosphorylation in the tyrosine residues of specific proteins under in vitro capacitation conditions.</abstract><cop>Boston</cop><pub>Boston : Springer US</pub><pmid>19802524</pmid><doi>10.1007/s11010-009-0261-8</doi><tpages>10</tpages></addata></record> |
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| subjects | 1-Methyl-3-isobutylxanthine - pharmacology Analysis Animal reproduction Animals Antibodies, Phospho-Specific Biochemistry Biomedical and Life Sciences Caffeine Caffeine - pharmacology Cardiology Cellular biology Cyclic AMP - metabolism Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors Cyclic AMP-Dependent Protein Kinases - metabolism Epididymis - cytology Ethanol Goats Kinases Life Sciences Male Medical Biochemistry Molecular biology Oncology Organ Specificity Phenols Phosphodiesterase Inhibitors - pharmacology Phosphoproteins - metabolism Phosphorylation - drug effects Protein Subunits - metabolism Protein Transport - drug effects Protein-Tyrosine Kinases - antagonists & inhibitors Protein-Tyrosine Kinases - metabolism Proteins Reagents Signal Transduction Sperm Capacitation - drug effects Sperm Capacitation - physiology Sperm Head - drug effects Sperm Head - metabolism Spermatozoa Spermatozoa - drug effects Spermatozoa - metabolism Spermatozoa - physiology Tyrosine Tyrosine - metabolism |
| title | Regulation of tyrosine kinase activity during capacitation in goat sperm |
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