Specific Binding of [α -32P]GTP to Cytosolic and Membrane-Bound Proteins of Human Platelets Correlates with the Activation of Phospholipase C
We have assessed the binding of [α -32P]GTP to platelet proteins from cytosolic and membrane fractions. Proteins were separated by NaDodSO4/PAGE and electrophoretically transferred to nitrocellulose. Incubation of the nitrocellulose blots with [α -32P]GTP indicated the presence of specific and disti...
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| Veröffentlicht in: | Proc. Natl. Acad. Sci. U.S.A.; (United States) 1987-04, Vol.84 (8), p.2261-2265 |
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| creator | Lapetina, Eduardo G. Reep, Bryan R. |
| description | We have assessed the binding of [α -32P]GTP to platelet proteins from cytosolic and membrane fractions. Proteins were separated by NaDodSO4/PAGE and electrophoretically transferred to nitrocellulose. Incubation of the nitrocellulose blots with [α -32P]GTP indicated the presence of specific and distinct GTP-binding proteins in cytosol and membranes. Binding was prevented by 10-100 nM GTP and by 100 nM guanosine 5′-[γ -thio]triphosphate (GTP[γ S]) or GDP; binding was unaffected by 1 nM-1 μ M ATP. One main GTP-binding protein (29.5 kDa) was detected in the membrane fraction, while three others (29, 27, and 21 kDa) were detected in the soluble fraction. Two cytosolic GTP-binding proteins (29 and 27 kDa) were degraded by trypsin; another cytosolic protein (21 kDa) and the membrane-bound protein (29.5 kDa) were resistant to the action of trypsin. Treatment of intact platelets with trypsin or thrombin, followed by lysis and fractionation, did not affect the binding of [α -32P]GTP to the membrane-bound protein. GTP[γ S] still stimulated phospholipase C in permeabilized platelets already preincubated with trypsin. This suggests that trypsin-resistant GTP-binding proteins might regulate phospholipase C stimulated by GTP[γ S]. |
| doi_str_mv | 10.1073/pnas.84.8.2261 |
| format | Article |
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Proteins were separated by NaDodSO4/PAGE and electrophoretically transferred to nitrocellulose. Incubation of the nitrocellulose blots with [α -32P]GTP indicated the presence of specific and distinct GTP-binding proteins in cytosol and membranes. Binding was prevented by 10-100 nM GTP and by 100 nM guanosine 5′-[γ -thio]triphosphate (GTP[γ S]) or GDP; binding was unaffected by 1 nM-1 μ M ATP. One main GTP-binding protein (29.5 kDa) was detected in the membrane fraction, while three others (29, 27, and 21 kDa) were detected in the soluble fraction. Two cytosolic GTP-binding proteins (29 and 27 kDa) were degraded by trypsin; another cytosolic protein (21 kDa) and the membrane-bound protein (29.5 kDa) were resistant to the action of trypsin. Treatment of intact platelets with trypsin or thrombin, followed by lysis and fractionation, did not affect the binding of [α -32P]GTP to the membrane-bound protein. GTP[γ S] still stimulated phospholipase C in permeabilized platelets already preincubated with trypsin. This suggests that trypsin-resistant GTP-binding proteins might regulate phospholipase C stimulated by GTP[γ S].</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.84.8.2261</identifier><identifier>PMID: 3470789</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Agonists ; ANIMALS ; ATP ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BETA-MINUS DECAY RADIOISOTOPES ; BIOCHEMICAL REACTION KINETICS ; Biological and medical sciences ; BIOLOGICAL MATERIALS ; BLOOD ; BLOOD CELLS ; Blood coagulation. Blood cells ; BLOOD PLATELETS ; Blood Platelets - enzymology ; Blood Proteins - isolation & purification ; Blood Proteins - metabolism ; BODY FLUIDS ; CARBOXYLESTERASES ; CELL CONSTITUENTS ; CELL MEMBRANES ; Cellulose nitrate ; Cytosol ; Cytosol - metabolism ; DAYS LIVING RADIOISOTOPES ; ELECTROPHORESIS ; Enzyme Activation ; ENZYME ACTIVITY ; ENZYMES ; ESTERASES ; Fractionation ; Fundamental and applied biological sciences. Psychology ; Guanosine Triphosphate - blood ; GUANYLIC ACID ; Humans ; HYDROLASES ; ISOTOPE APPLICATIONS ; ISOTOPES ; KINETICS ; LIGHT NUCLEI ; LIPASE ; MAMMALS ; MAN ; MATERIALS ; Membrane Proteins - blood ; Membrane Proteins - isolation & purification ; MEMBRANES ; Molecular and cellular biology ; NUCLEI ; NUCLEOTIDES ; ODD-ODD NUCLEI ; ORGANIC COMPOUNDS ; P branes ; Particulate matter ; PEPTIDE HYDROLASES ; PHOSPHORUS 32 ; PHOSPHORUS ISOTOPES ; Phosphorus Radioisotopes ; Platelet ; Platelets ; PRIMATES ; PROTEINS ; RADIOISOTOPES ; REACTION KINETICS ; Saponins ; SERINE PROTEINASES ; Soybeans ; Subcellular fractions ; TRACER TECHNIQUES ; TRYPSIN ; Type C Phospholipases - blood ; VERTEBRATES 550201 -- Biochemistry-- Tracer Techniques</subject><ispartof>Proc. Natl. Acad. Sci. U.S.A.; (United States), 1987-04, Vol.84 (8), p.2261-2265</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c512t-8719850495371bee07710a14da6a9e38fa63992ead129ec0bc6ad3fbfefe28ff3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/84/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/29691$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/29691$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8210479$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3470789$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6793275$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Lapetina, Eduardo G.</creatorcontrib><creatorcontrib>Reep, Bryan R.</creatorcontrib><creatorcontrib>Burroughs Wellcome Co., Research Triangle Park, NC</creatorcontrib><title>Specific Binding of [α -32P]GTP to Cytosolic and Membrane-Bound Proteins of Human Platelets Correlates with the Activation of Phospholipase C</title><title>Proc. Natl. Acad. Sci. U.S.A.; (United States)</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We have assessed the binding of [α -32P]GTP to platelet proteins from cytosolic and membrane fractions. Proteins were separated by NaDodSO4/PAGE and electrophoretically transferred to nitrocellulose. Incubation of the nitrocellulose blots with [α -32P]GTP indicated the presence of specific and distinct GTP-binding proteins in cytosol and membranes. Binding was prevented by 10-100 nM GTP and by 100 nM guanosine 5′-[γ -thio]triphosphate (GTP[γ S]) or GDP; binding was unaffected by 1 nM-1 μ M ATP. One main GTP-binding protein (29.5 kDa) was detected in the membrane fraction, while three others (29, 27, and 21 kDa) were detected in the soluble fraction. Two cytosolic GTP-binding proteins (29 and 27 kDa) were degraded by trypsin; another cytosolic protein (21 kDa) and the membrane-bound protein (29.5 kDa) were resistant to the action of trypsin. Treatment of intact platelets with trypsin or thrombin, followed by lysis and fractionation, did not affect the binding of [α -32P]GTP to the membrane-bound protein. GTP[γ S] still stimulated phospholipase C in permeabilized platelets already preincubated with trypsin. This suggests that trypsin-resistant GTP-binding proteins might regulate phospholipase C stimulated by GTP[γ S].</description><subject>Agonists</subject><subject>ANIMALS</subject><subject>ATP</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>BIOCHEMICAL REACTION KINETICS</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL MATERIALS</subject><subject>BLOOD</subject><subject>BLOOD CELLS</subject><subject>Blood coagulation. Blood cells</subject><subject>BLOOD PLATELETS</subject><subject>Blood Platelets - enzymology</subject><subject>Blood Proteins - isolation & purification</subject><subject>Blood Proteins - metabolism</subject><subject>BODY FLUIDS</subject><subject>CARBOXYLESTERASES</subject><subject>CELL CONSTITUENTS</subject><subject>CELL MEMBRANES</subject><subject>Cellulose nitrate</subject><subject>Cytosol</subject><subject>Cytosol - metabolism</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>ELECTROPHORESIS</subject><subject>Enzyme Activation</subject><subject>ENZYME ACTIVITY</subject><subject>ENZYMES</subject><subject>ESTERASES</subject><subject>Fractionation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guanosine Triphosphate - blood</subject><subject>GUANYLIC ACID</subject><subject>Humans</subject><subject>HYDROLASES</subject><subject>ISOTOPE APPLICATIONS</subject><subject>ISOTOPES</subject><subject>KINETICS</subject><subject>LIGHT NUCLEI</subject><subject>LIPASE</subject><subject>MAMMALS</subject><subject>MAN</subject><subject>MATERIALS</subject><subject>Membrane Proteins - blood</subject><subject>Membrane Proteins - isolation & purification</subject><subject>MEMBRANES</subject><subject>Molecular and cellular biology</subject><subject>NUCLEI</subject><subject>NUCLEOTIDES</subject><subject>ODD-ODD NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>P branes</subject><subject>Particulate matter</subject><subject>PEPTIDE HYDROLASES</subject><subject>PHOSPHORUS 32</subject><subject>PHOSPHORUS ISOTOPES</subject><subject>Phosphorus Radioisotopes</subject><subject>Platelet</subject><subject>Platelets</subject><subject>PRIMATES</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>REACTION KINETICS</subject><subject>Saponins</subject><subject>SERINE PROTEINASES</subject><subject>Soybeans</subject><subject>Subcellular fractions</subject><subject>TRACER TECHNIQUES</subject><subject>TRYPSIN</subject><subject>Type C Phospholipases - blood</subject><subject>VERTEBRATES 550201 -- Biochemistry-- Tracer Techniques</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kdFqFDEUhgex1LV664UgBJHezZpkspPkwot20VaouGC9EgnZzEknZTYZk0y1L-G7-CI-U2fYZVlvvAqH__v_c8hfFC8InhPMq7e912ku2FzMKa3Jo2JGsCRlzSR-XMwwprwUjLInxdOUbjHGciHwcXFcMY65kLPi95cejLPOoHPnG-dvULDo298_qKzo6vvF9QrlgJb3OaTQjZD2DfoEm3XUHsrzMIzjKoYMzqfJeDlstEerTmfoICe0DDHCNCX00-UW5RbQmcnuTmcX_ORYtSH17Zjd6wRo-aw4srpL8Hz3nhRfP7y_Xl6WV58vPi7PrkqzIDSXghMpFpjJRcXJGgBzTrAmrNG1llAJq-tKSgq6IVSCwWtT66ayawsWqLC2OinebXP7Yb2BxoDPUXeqj26j470K2ql_Fe9adRPuVIVZTeXof731h5SdSsZlMK0J3oPJquayonwxQqe7JTH8GCBltXHJQNeNnxeGpDhnNWF0Audb0MSQUgS7P4RgNbWsppaVYEqoqeXR8Orw_D2-q3XU3-x0nYzu7FiXcWmPCUow4_IgZorfqwdrTv-nKzt0XYZfeQRfbsHblEPck1TWklQP7fTTWA</recordid><startdate>19870401</startdate><enddate>19870401</enddate><creator>Lapetina, Eduardo G.</creator><creator>Reep, Bryan R.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>19870401</creationdate><title>Specific Binding of [α -32P]GTP to Cytosolic and Membrane-Bound Proteins of Human Platelets Correlates with the Activation of Phospholipase C</title><author>Lapetina, Eduardo G. ; Reep, Bryan R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c512t-8719850495371bee07710a14da6a9e38fa63992ead129ec0bc6ad3fbfefe28ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Agonists</topic><topic>ANIMALS</topic><topic>ATP</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>BIOCHEMICAL REACTION KINETICS</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL MATERIALS</topic><topic>BLOOD</topic><topic>BLOOD CELLS</topic><topic>Blood coagulation. Blood cells</topic><topic>BLOOD PLATELETS</topic><topic>Blood Platelets - enzymology</topic><topic>Blood Proteins - isolation & purification</topic><topic>Blood Proteins - metabolism</topic><topic>BODY FLUIDS</topic><topic>CARBOXYLESTERASES</topic><topic>CELL CONSTITUENTS</topic><topic>CELL MEMBRANES</topic><topic>Cellulose nitrate</topic><topic>Cytosol</topic><topic>Cytosol - metabolism</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>ELECTROPHORESIS</topic><topic>Enzyme Activation</topic><topic>ENZYME ACTIVITY</topic><topic>ENZYMES</topic><topic>ESTERASES</topic><topic>Fractionation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guanosine Triphosphate - blood</topic><topic>GUANYLIC ACID</topic><topic>Humans</topic><topic>HYDROLASES</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPES</topic><topic>KINETICS</topic><topic>LIGHT NUCLEI</topic><topic>LIPASE</topic><topic>MAMMALS</topic><topic>MAN</topic><topic>MATERIALS</topic><topic>Membrane Proteins - blood</topic><topic>Membrane Proteins - isolation & purification</topic><topic>MEMBRANES</topic><topic>Molecular and cellular biology</topic><topic>NUCLEI</topic><topic>NUCLEOTIDES</topic><topic>ODD-ODD NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>P branes</topic><topic>Particulate matter</topic><topic>PEPTIDE HYDROLASES</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>Phosphorus Radioisotopes</topic><topic>Platelet</topic><topic>Platelets</topic><topic>PRIMATES</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>REACTION KINETICS</topic><topic>Saponins</topic><topic>SERINE PROTEINASES</topic><topic>Soybeans</topic><topic>Subcellular fractions</topic><topic>TRACER TECHNIQUES</topic><topic>TRYPSIN</topic><topic>Type C Phospholipases - blood</topic><topic>VERTEBRATES 550201 -- Biochemistry-- Tracer Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lapetina, Eduardo G.</creatorcontrib><creatorcontrib>Reep, Bryan R.</creatorcontrib><creatorcontrib>Burroughs Wellcome Co., Research Triangle Park, NC</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><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proc. Natl. Acad. Sci. U.S.A.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lapetina, Eduardo G.</au><au>Reep, Bryan R.</au><aucorp>Burroughs Wellcome Co., Research Triangle Park, NC</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific Binding of [α -32P]GTP to Cytosolic and Membrane-Bound Proteins of Human Platelets Correlates with the Activation of Phospholipase C</atitle><jtitle>Proc. Natl. Acad. Sci. U.S.A.; (United States)</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1987-04-01</date><risdate>1987</risdate><volume>84</volume><issue>8</issue><spage>2261</spage><epage>2265</epage><pages>2261-2265</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>We have assessed the binding of [α -32P]GTP to platelet proteins from cytosolic and membrane fractions. Proteins were separated by NaDodSO4/PAGE and electrophoretically transferred to nitrocellulose. Incubation of the nitrocellulose blots with [α -32P]GTP indicated the presence of specific and distinct GTP-binding proteins in cytosol and membranes. Binding was prevented by 10-100 nM GTP and by 100 nM guanosine 5′-[γ -thio]triphosphate (GTP[γ S]) or GDP; binding was unaffected by 1 nM-1 μ M ATP. One main GTP-binding protein (29.5 kDa) was detected in the membrane fraction, while three others (29, 27, and 21 kDa) were detected in the soluble fraction. Two cytosolic GTP-binding proteins (29 and 27 kDa) were degraded by trypsin; another cytosolic protein (21 kDa) and the membrane-bound protein (29.5 kDa) were resistant to the action of trypsin. Treatment of intact platelets with trypsin or thrombin, followed by lysis and fractionation, did not affect the binding of [α -32P]GTP to the membrane-bound protein. GTP[γ S] still stimulated phospholipase C in permeabilized platelets already preincubated with trypsin. This suggests that trypsin-resistant GTP-binding proteins might regulate phospholipase C stimulated by GTP[γ S].</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3470789</pmid><doi>10.1073/pnas.84.8.2261</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proc. Natl. Acad. Sci. U.S.A.; (United States), 1987-04, Vol.84 (8), p.2261-2265 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_8210479 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Agonists ANIMALS ATP BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES BIOCHEMICAL REACTION KINETICS Biological and medical sciences BIOLOGICAL MATERIALS BLOOD BLOOD CELLS Blood coagulation. Blood cells BLOOD PLATELETS Blood Platelets - enzymology Blood Proteins - isolation & purification Blood Proteins - metabolism BODY FLUIDS CARBOXYLESTERASES CELL CONSTITUENTS CELL MEMBRANES Cellulose nitrate Cytosol Cytosol - metabolism DAYS LIVING RADIOISOTOPES ELECTROPHORESIS Enzyme Activation ENZYME ACTIVITY ENZYMES ESTERASES Fractionation Fundamental and applied biological sciences. Psychology Guanosine Triphosphate - blood GUANYLIC ACID Humans HYDROLASES ISOTOPE APPLICATIONS ISOTOPES KINETICS LIGHT NUCLEI LIPASE MAMMALS MAN MATERIALS Membrane Proteins - blood Membrane Proteins - isolation & purification MEMBRANES Molecular and cellular biology NUCLEI NUCLEOTIDES ODD-ODD NUCLEI ORGANIC COMPOUNDS P branes Particulate matter PEPTIDE HYDROLASES PHOSPHORUS 32 PHOSPHORUS ISOTOPES Phosphorus Radioisotopes Platelet Platelets PRIMATES PROTEINS RADIOISOTOPES REACTION KINETICS Saponins SERINE PROTEINASES Soybeans Subcellular fractions TRACER TECHNIQUES TRYPSIN Type C Phospholipases - blood VERTEBRATES 550201 -- Biochemistry-- Tracer Techniques |
| title | Specific Binding of [α -32P]GTP to Cytosolic and Membrane-Bound Proteins of Human Platelets Correlates with the Activation of Phospholipase C |
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