A neutrophil GTP-binding protein that regulates cellfree NADPH oxidase activation is located in the cytosolic fraction
The dormant O sub(2) super(-)-generating oxidase in plasma membranes from unstimulated neutrophils becomes activated in the presence of arachidonate and a multicomponent cytosolic fraction. This process is stimulated by nonhydrolyzable GTP analogues and may involve a pertussis toxin insensitive GTP-...
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| Veröffentlicht in: | The Journal of immunology (1950) 1990-08, Vol.145 (3), p.945-951 |
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| container_end_page | 951 |
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| container_issue | 3 |
| container_start_page | 945 |
| container_title | The Journal of immunology (1950) |
| container_volume | 145 |
| creator | GABIG, T. G EKLUND, E. A POTTER, G.B DYKES, J. R |
| description | The dormant O sub(2) super(-)-generating oxidase in plasma membranes from unstimulated neutrophils becomes activated in the presence of arachidonate and a multicomponent cytosolic fraction. This process is stimulated by nonhydrolyzable GTP analogues and may involve a pertussis toxin insensitive GTP-binding protein. Our studies were designed to characterize the putative GTP-binding protein, localizing it to either membrane or cytosolic fraction in this system. We conclude that the GTP-binding protein regulating this cellfree system is located in the cytosolic fraction. The GTP gamma S-liganded form of this protein may be activated or stabilized by arachidonate. |
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G ; EKLUND, E. A ; POTTER, G.B ; DYKES, J. R</creator><creatorcontrib>GABIG, T. G ; EKLUND, E. A ; POTTER, G.B ; DYKES, J. R</creatorcontrib><description>The dormant O sub(2) super(-)-generating oxidase in plasma membranes from unstimulated neutrophils becomes activated in the presence of arachidonate and a multicomponent cytosolic fraction. This process is stimulated by nonhydrolyzable GTP analogues and may involve a pertussis toxin insensitive GTP-binding protein. Our studies were designed to characterize the putative GTP-binding protein, localizing it to either membrane or cytosolic fraction in this system. We conclude that the GTP-binding protein regulating this cellfree system is located in the cytosolic fraction. The GTP gamma S-liganded form of this protein may be activated or stabilized by arachidonate.</description><identifier>ISSN: 0022-1767</identifier><identifier>EISSN: 1550-6606</identifier><identifier>CODEN: JOIMA3</identifier><language>eng</language><publisher>Bethesda, MD: American Association of Immunologists</publisher><subject>Biological and medical sciences ; Fundamental and applied biological sciences. 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R</creatorcontrib><title>A neutrophil GTP-binding protein that regulates cellfree NADPH oxidase activation is located in the cytosolic fraction</title><title>The Journal of immunology (1950)</title><description>The dormant O sub(2) super(-)-generating oxidase in plasma membranes from unstimulated neutrophils becomes activated in the presence of arachidonate and a multicomponent cytosolic fraction. This process is stimulated by nonhydrolyzable GTP analogues and may involve a pertussis toxin insensitive GTP-binding protein. Our studies were designed to characterize the putative GTP-binding protein, localizing it to either membrane or cytosolic fraction in this system. We conclude that the GTP-binding protein regulating this cellfree system is located in the cytosolic fraction. The GTP gamma S-liganded form of this protein may be activated or stabilized by arachidonate.</description><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>guanine nucleotide-binding protein</subject><subject>Immunobiology</subject><subject>Myeloid cells: ontogeny, maturation, markers, receptors</subject><subject>NADPH oxidase</subject><subject>Polynuclears</subject><issn>0022-1767</issn><issn>1550-6606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><recordid>eNotj81KAzEYRYMoWKvvkIW4G0gy-ZlZlqqtULSLuh6-Jpk2kibjJFPs2zvVri4Xzr1wrtCECkEKKYm8RhNCGCuokuoW3aX0RQiRhPEJOs5wsEPuY7d3Hi8262LrgnFhh7s-ZusCznvIuLe7wUO2CWvrfdtbi99nz-sljj_OQLIYdHZHyC4G7BL2UY-wwX9zi_UpxxS907jtz2AM9-imBZ_swyWn6PP1ZTNfFquPxdt8tio6RstcAFAiFGuV3EJtKZi6Ni0VFtqqYkpIqkrKjZKV4URoKnUFY2McuDSGK1VO0dP_72jzPdiUm4NLZwUINg6poaJSvOTVCD5eQEgaRkMI2qWm690B-lPDuaKSluUvS7Nnyw</recordid><startdate>19900801</startdate><enddate>19900801</enddate><creator>GABIG, T. G</creator><creator>EKLUND, E. 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Psychology</topic><topic>Fundamental immunology</topic><topic>guanine nucleotide-binding protein</topic><topic>Immunobiology</topic><topic>Myeloid cells: ontogeny, maturation, markers, receptors</topic><topic>NADPH oxidase</topic><topic>Polynuclears</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GABIG, T. G</creatorcontrib><creatorcontrib>EKLUND, E. A</creatorcontrib><creatorcontrib>POTTER, G.B</creatorcontrib><creatorcontrib>DYKES, J. 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R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A neutrophil GTP-binding protein that regulates cellfree NADPH oxidase activation is located in the cytosolic fraction</atitle><jtitle>The Journal of immunology (1950)</jtitle><date>1990-08-01</date><risdate>1990</risdate><volume>145</volume><issue>3</issue><spage>945</spage><epage>951</epage><pages>945-951</pages><issn>0022-1767</issn><eissn>1550-6606</eissn><coden>JOIMA3</coden><abstract>The dormant O sub(2) super(-)-generating oxidase in plasma membranes from unstimulated neutrophils becomes activated in the presence of arachidonate and a multicomponent cytosolic fraction. This process is stimulated by nonhydrolyzable GTP analogues and may involve a pertussis toxin insensitive GTP-binding protein. Our studies were designed to characterize the putative GTP-binding protein, localizing it to either membrane or cytosolic fraction in this system. We conclude that the GTP-binding protein regulating this cellfree system is located in the cytosolic fraction. The GTP gamma S-liganded form of this protein may be activated or stabilized by arachidonate.</abstract><cop>Bethesda, MD</cop><pub>American Association of Immunologists</pub><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0022-1767 |
| ispartof | The Journal of immunology (1950), 1990-08, Vol.145 (3), p.945-951 |
| issn | 0022-1767 1550-6606 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15874348 |
| source | Alma/SFX Local Collection |
| subjects | Biological and medical sciences Fundamental and applied biological sciences. Psychology Fundamental immunology guanine nucleotide-binding protein Immunobiology Myeloid cells: ontogeny, maturation, markers, receptors NADPH oxidase Polynuclears |
| title | A neutrophil GTP-binding protein that regulates cellfree NADPH oxidase activation is located in the cytosolic fraction |
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