Endogenous activity of cyclic nucleotide-dependent protein kinase in plasma membranes isolated from Strongylocentrotus purpuratus sea urchin sperm
Activity of cyclic nucleotide-dependent protein kinase was investigated in flagellar plasma membranes of sea urchin sperm ( S. purpuratus). Membranes incubated with [γ- 32P]ATP showed in the presence of 1 μM cAMP an increased phosphorylation in multiple polypeptides. Half maximal response was seen a...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1991-11, Vol.180 (3), p.1436-1445 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Garcia-Soto, Jesus Araiza, Luz M. Barrios, Miriam Darszon, Alberto Luna-Arias, Juan P. |
| description | Activity of cyclic nucleotide-dependent protein kinase was investigated in flagellar plasma membranes of sea urchin sperm (
S. purpuratus). Membranes incubated with [γ-
32P]ATP showed in the presence of 1 μM cAMP an increased phosphorylation in multiple polypeptides. Half maximal response was seen at 0.6 μM of cAMP. In contrast, higher concentrations (100 μM) of cGMP were required to cause the same amount of protein phosphorylation. 80% of the protein kinase activity stimulatable by cAMP was resistant to extraction by 10 mM EGTA and sonication but it was entirely recovered in a detergent-solubilized fraction. Membranes pretreated with 200 μM cAMP, ultracentrifuged and resuspended in buffer solution did not undergo cAMP-stimulated phosphorylation in their polypeptides. This study demonstrates that flagellar plasma membranes isolated from
S. purpuratus sea urchin sperm have an endogenous cAMP-dependent protein kinase, which may be bound to the membrane via its regulatory subunit. |
| doi_str_mv | 10.1016/S0006-291X(05)81357-9 |
| format | Article |
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S. purpuratus). Membranes incubated with [γ-
32P]ATP showed in the presence of 1 μM cAMP an increased phosphorylation in multiple polypeptides. Half maximal response was seen at 0.6 μM of cAMP. In contrast, higher concentrations (100 μM) of cGMP were required to cause the same amount of protein phosphorylation. 80% of the protein kinase activity stimulatable by cAMP was resistant to extraction by 10 mM EGTA and sonication but it was entirely recovered in a detergent-solubilized fraction. Membranes pretreated with 200 μM cAMP, ultracentrifuged and resuspended in buffer solution did not undergo cAMP-stimulated phosphorylation in their polypeptides. This study demonstrates that flagellar plasma membranes isolated from
S. purpuratus sea urchin sperm have an endogenous cAMP-dependent protein kinase, which may be bound to the membrane via its regulatory subunit.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(05)81357-9</identifier><identifier>PMID: 1659417</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cell Fractionation ; Cell Membrane - enzymology ; Cyclic AMP - pharmacology ; Cyclic GMP - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Male ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Molecular Weight ; Phosphorylation ; Protein Kinases - isolation & purification ; Protein Kinases - metabolism ; Sea Urchins ; Spermatozoa - metabolism ; Transferases</subject><ispartof>Biochemical and biophysical research communications, 1991-11, Vol.180 (3), p.1436-1445</ispartof><rights>1991 Academic Press, Inc.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c304t-36c7c83fbb9f5119db6f70c8f9051a77fa8e3b044c120bf7aea5e1e395b4ed4f3</citedby><cites>FETCH-LOGICAL-c304t-36c7c83fbb9f5119db6f70c8f9051a77fa8e3b044c120bf7aea5e1e395b4ed4f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-291X(05)81357-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5015217$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1659417$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Garcia-Soto, Jesus</creatorcontrib><creatorcontrib>Araiza, Luz M.</creatorcontrib><creatorcontrib>Barrios, Miriam</creatorcontrib><creatorcontrib>Darszon, Alberto</creatorcontrib><creatorcontrib>Luna-Arias, Juan P.</creatorcontrib><title>Endogenous activity of cyclic nucleotide-dependent protein kinase in plasma membranes isolated from Strongylocentrotus purpuratus sea urchin sperm</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Activity of cyclic nucleotide-dependent protein kinase was investigated in flagellar plasma membranes of sea urchin sperm (
S. purpuratus). Membranes incubated with [γ-
32P]ATP showed in the presence of 1 μM cAMP an increased phosphorylation in multiple polypeptides. Half maximal response was seen at 0.6 μM of cAMP. In contrast, higher concentrations (100 μM) of cGMP were required to cause the same amount of protein phosphorylation. 80% of the protein kinase activity stimulatable by cAMP was resistant to extraction by 10 mM EGTA and sonication but it was entirely recovered in a detergent-solubilized fraction. Membranes pretreated with 200 μM cAMP, ultracentrifuged and resuspended in buffer solution did not undergo cAMP-stimulated phosphorylation in their polypeptides. This study demonstrates that flagellar plasma membranes isolated from
S. purpuratus sea urchin sperm have an endogenous cAMP-dependent protein kinase, which may be bound to the membrane via its regulatory subunit.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Fractionation</subject><subject>Cell Membrane - enzymology</subject><subject>Cyclic AMP - pharmacology</subject><subject>Cyclic GMP - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Male</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Weight</subject><subject>Phosphorylation</subject><subject>Protein Kinases - isolation & purification</subject><subject>Protein Kinases - metabolism</subject><subject>Sea Urchins</subject><subject>Spermatozoa - metabolism</subject><subject>Transferases</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcuKFTEQhoMo43H0EQayENFFa9Ld6T5ZyTCMFxhwMQruQrpSGaPppE3SA-c1fGJzLoxLIZCC-v66_EXIBWdvOePDu1vG2NC0kn9_zcSbLe_E2MhHZMOZZE3LWf-YbB6Qp-RZzj8Z47wf5Bk544OQPR835M91MPEOQ1wz1VDcvSs7Gi2FHXgHNKzgMRZnsDG4YDAYCl1SLOgC_eWCzkhrtHidZ01nnKekA2bqcvS6oKE2xZnelhTD3c5HqPIqrr2WNdWn92FGTdcEP2qdvGCan5MnVvuML07_Ofn24frr1afm5svHz1eXNw10rC9NN8AI285Ok7SCc2mmwY4MtlYywfU4Wr3FbmJ9D7xlkx01aoEcOymmHk1vu3Py6li37vN7xVzU7DKg93WDaoca215WaVdBcQQhxZwTWrUkN-u0U5yp_S3U4RZqb7RiQh1uoWTVXZwarNOM5p_qaH7NvzzldQbtbbUOXH7ABOOiPWDvjxhWM-4dJpXBYQA0LiEUZaL7zyB_AZioq3c</recordid><startdate>19911114</startdate><enddate>19911114</enddate><creator>Garcia-Soto, Jesus</creator><creator>Araiza, Luz M.</creator><creator>Barrios, Miriam</creator><creator>Darszon, Alberto</creator><creator>Luna-Arias, Juan P.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>19911114</creationdate><title>Endogenous activity of cyclic nucleotide-dependent protein kinase in plasma membranes isolated from Strongylocentrotus purpuratus sea urchin sperm</title><author>Garcia-Soto, Jesus ; Araiza, Luz M. ; Barrios, Miriam ; Darszon, Alberto ; Luna-Arias, Juan P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c304t-36c7c83fbb9f5119db6f70c8f9051a77fa8e3b044c120bf7aea5e1e395b4ed4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Fractionation</topic><topic>Cell Membrane - enzymology</topic><topic>Cyclic AMP - pharmacology</topic><topic>Cyclic GMP - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Male</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Weight</topic><topic>Phosphorylation</topic><topic>Protein Kinases - isolation & purification</topic><topic>Protein Kinases - metabolism</topic><topic>Sea Urchins</topic><topic>Spermatozoa - metabolism</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Garcia-Soto, Jesus</creatorcontrib><creatorcontrib>Araiza, Luz M.</creatorcontrib><creatorcontrib>Barrios, Miriam</creatorcontrib><creatorcontrib>Darszon, Alberto</creatorcontrib><creatorcontrib>Luna-Arias, Juan P.</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>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Garcia-Soto, Jesus</au><au>Araiza, Luz M.</au><au>Barrios, Miriam</au><au>Darszon, Alberto</au><au>Luna-Arias, Juan P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endogenous activity of cyclic nucleotide-dependent protein kinase in plasma membranes isolated from Strongylocentrotus purpuratus sea urchin sperm</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1991-11-14</date><risdate>1991</risdate><volume>180</volume><issue>3</issue><spage>1436</spage><epage>1445</epage><pages>1436-1445</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Activity of cyclic nucleotide-dependent protein kinase was investigated in flagellar plasma membranes of sea urchin sperm (
S. purpuratus). Membranes incubated with [γ-
32P]ATP showed in the presence of 1 μM cAMP an increased phosphorylation in multiple polypeptides. Half maximal response was seen at 0.6 μM of cAMP. In contrast, higher concentrations (100 μM) of cGMP were required to cause the same amount of protein phosphorylation. 80% of the protein kinase activity stimulatable by cAMP was resistant to extraction by 10 mM EGTA and sonication but it was entirely recovered in a detergent-solubilized fraction. Membranes pretreated with 200 μM cAMP, ultracentrifuged and resuspended in buffer solution did not undergo cAMP-stimulated phosphorylation in their polypeptides. This study demonstrates that flagellar plasma membranes isolated from
S. purpuratus sea urchin sperm have an endogenous cAMP-dependent protein kinase, which may be bound to the membrane via its regulatory subunit.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1659417</pmid><doi>10.1016/S0006-291X(05)81357-9</doi><tpages>10</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1991-11, Vol.180 (3), p.1436-1445 |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cell Fractionation Cell Membrane - enzymology Cyclic AMP - pharmacology Cyclic GMP - pharmacology Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Kinetics Male Membrane Proteins - isolation & purification Membrane Proteins - metabolism Molecular Weight Phosphorylation Protein Kinases - isolation & purification Protein Kinases - metabolism Sea Urchins Spermatozoa - metabolism Transferases |
| title | Endogenous activity of cyclic nucleotide-dependent protein kinase in plasma membranes isolated from Strongylocentrotus purpuratus sea urchin sperm |
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