Platelet-activating factor stimulates phosphoinositide turnover in neurohybrid NCB-20 cells: involvement of pertussis toxin-sensitive guanine nucleotide-binding proteins and inhibition by protein kinase C
Platelet-activating factor (PAF) is an unusually potent phospholipid known to be produced by neuronal cells and to modulate cerebral blood flow and metabolism. In previous studies with NCB-20 cells, we reported that PAF induced a significant mobilization of intracellular free Ca2+ ([Ca2+]i), which w...
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| Veröffentlicht in: | Molecular pharmacology 1992-02, Vol.41 (2), p.281-289 |
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| creator | YUE, TL STADEL, JM SARAU, HM FRIEDMAN, E GU, JL POWERS, DA GLEASON, MM FEUERSTEIN, G WANG, HY |
| description | Platelet-activating factor (PAF) is an unusually potent phospholipid known to be produced by neuronal cells and to modulate
cerebral blood flow and metabolism. In previous studies with NCB-20 cells, we reported that PAF induced a significant mobilization
of intracellular free Ca2+ ([Ca2+]i), which was inhibited by PAF antagonists. The increase was the result of release from
intracellular stores and influx from extracellular sources. The present study was designed to characterize further PAF receptor-mediated
cellular signal-transduction mechanisms in myo-[3H]inositol-labeled cells. PAF induced a concentration-dependent increase
in phosphatidylinositol (Pl) metabolism, with EC50 values of 1.96 +/- 0.62 nM and 1.12 +/- 0.50 nM for inositol trisphosphate
(IP3) and inositol monophosphate (IP1) formation, respectively (four experiments). The maximal production of IP3 and IP1 induced
by 50 nM PAF was 254 +/- 34% and 178 +/- 25% over the basal, respectively (four experiments). PAF-induced Pl metabolism was
concentration-dependently inhibited by the PAF antagonist BN50739, with an IC50 value of 6.48 +/- 0.52 nM (four experiments).
The protein kinase C (PKC) activator phorbol 12,13-dibutyrate concentration-dependently inhibited PAF-induced Pl metabolism
and [Ca2+]i mobilization in NCB-20 cells, of NCB-20 cells with pertussis toxin (PTX) resulted in a concentration-dependent
inhibition of PAF-induced IP3 production and intracellular Ca2+ release, with a maximal reduction of 66.9 +/- 3.5% and 63
+/- 6.1%, respectively, at 300 ng/ml PTX. PTX in the presence of [32P]NAD specifically [32P]ADP-ribosylated a 38-kDa protein
in membranes prepared from NCB-20 cells. Pretreatment of the cells with PTX resulted in a concentration-dependent inhibition
of subsequent 32P-labeling of the toxin substrate in the membranes and correlated with the uncoupling of PAF-induced IP3 formation.
PAF (0.01-10 nM) elicited a concentration-related stimulation in guanosine 5'-O-(3-[35S]) triphosphate ([35S]GTP gamma S)
binding to G alpha i(1,2) proteins, which was inhibited by the PAF antagonist BN50739. PAF at 10 nM also increased [35S]GTP
gamma S binding to G alpha s and G alpha o. PAF-evoked activation of G alpha i(1,2) and G alpha o was reduced by preincubation
with PTX. Our results reveal that neuronal cells possess PAF receptors linked through guanine nucleotide-binding proteins
to phospholipase C and receptor-operated Ca2+ channels that are regulated by PKC. Both PTX-sensitive and -insensi |
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cerebral blood flow and metabolism. In previous studies with NCB-20 cells, we reported that PAF induced a significant mobilization
of intracellular free Ca2+ ([Ca2+]i), which was inhibited by PAF antagonists. The increase was the result of release from
intracellular stores and influx from extracellular sources. The present study was designed to characterize further PAF receptor-mediated
cellular signal-transduction mechanisms in myo-[3H]inositol-labeled cells. PAF induced a concentration-dependent increase
in phosphatidylinositol (Pl) metabolism, with EC50 values of 1.96 +/- 0.62 nM and 1.12 +/- 0.50 nM for inositol trisphosphate
(IP3) and inositol monophosphate (IP1) formation, respectively (four experiments). The maximal production of IP3 and IP1 induced
by 50 nM PAF was 254 +/- 34% and 178 +/- 25% over the basal, respectively (four experiments). PAF-induced Pl metabolism was
concentration-dependently inhibited by the PAF antagonist BN50739, with an IC50 value of 6.48 +/- 0.52 nM (four experiments).
The protein kinase C (PKC) activator phorbol 12,13-dibutyrate concentration-dependently inhibited PAF-induced Pl metabolism
and [Ca2+]i mobilization in NCB-20 cells, of NCB-20 cells with pertussis toxin (PTX) resulted in a concentration-dependent
inhibition of PAF-induced IP3 production and intracellular Ca2+ release, with a maximal reduction of 66.9 +/- 3.5% and 63
+/- 6.1%, respectively, at 300 ng/ml PTX. PTX in the presence of [32P]NAD specifically [32P]ADP-ribosylated a 38-kDa protein
in membranes prepared from NCB-20 cells. Pretreatment of the cells with PTX resulted in a concentration-dependent inhibition
of subsequent 32P-labeling of the toxin substrate in the membranes and correlated with the uncoupling of PAF-induced IP3 formation.
PAF (0.01-10 nM) elicited a concentration-related stimulation in guanosine 5'-O-(3-[35S]) triphosphate ([35S]GTP gamma S)
binding to G alpha i(1,2) proteins, which was inhibited by the PAF antagonist BN50739. PAF at 10 nM also increased [35S]GTP
gamma S binding to G alpha s and G alpha o. PAF-evoked activation of G alpha i(1,2) and G alpha o was reduced by preincubation
with PTX. Our results reveal that neuronal cells possess PAF receptors linked through guanine nucleotide-binding proteins
to phospholipase C and receptor-operated Ca2+ channels that are regulated by PKC. Both PTX-sensitive and -insensitive guanine
nucleotide-binding proteins appear to couple the PAF receptor to activation of phospholipase C and the increase in [Ca2+]i.
These results contribute to the further understanding of the mechanisms behind PAF actions on neuronal cells.</description><identifier>ISSN: 0026-895X</identifier><identifier>EISSN: 1521-0111</identifier><identifier>PMID: 1311408</identifier><identifier>CODEN: MOPMA3</identifier><language>eng</language><publisher>BALTIMORE: American Society for Pharmacology and Experimental Therapeutics</publisher><subject>Adenosine Diphosphate - metabolism ; Animals ; Biological and medical sciences ; Brain - cytology ; Brain - drug effects ; Brain - metabolism ; Calcium - metabolism ; Cell physiology ; Cricetinae ; Cricetulus ; Fundamental and applied biological sciences. Psychology ; GTP-Binding Proteins - drug effects ; GTP-Binding Proteins - physiology ; Hybrid Cells - drug effects ; Hybrid Cells - metabolism ; Life Sciences & Biomedicine ; Membrane Proteins - metabolism ; Mice ; Molecular and cellular biology ; Neuroblastoma - drug therapy ; Neuroblastoma - metabolism ; Neuroblastoma - pathology ; Pertussis Toxin ; Pharmacology & Pharmacy ; Phorbol 12,13-Dibutyrate - pharmacology ; Phosphatidylinositols - metabolism ; Platelet Activating Factor - pharmacology ; Protein Kinase C - pharmacology ; Science & Technology ; Signal transduction ; Signal Transduction - drug effects ; Signal Transduction - physiology ; Stimulation, Chemical ; Virulence Factors, Bordetella - pharmacology</subject><ispartof>Molecular pharmacology, 1992-02, Vol.41 (2), p.281-289</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>33</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wosA1992HL47200010</woscitedreferencesoriginalsourcerecordid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27197</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5118795$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1311408$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>YUE, TL</creatorcontrib><creatorcontrib>STADEL, JM</creatorcontrib><creatorcontrib>SARAU, HM</creatorcontrib><creatorcontrib>FRIEDMAN, E</creatorcontrib><creatorcontrib>GU, JL</creatorcontrib><creatorcontrib>POWERS, DA</creatorcontrib><creatorcontrib>GLEASON, MM</creatorcontrib><creatorcontrib>FEUERSTEIN, G</creatorcontrib><creatorcontrib>WANG, HY</creatorcontrib><title>Platelet-activating factor stimulates phosphoinositide turnover in neurohybrid NCB-20 cells: involvement of pertussis toxin-sensitive guanine nucleotide-binding proteins and inhibition by protein kinase C</title><title>Molecular pharmacology</title><addtitle>MOL PHARMACOL</addtitle><addtitle>Mol Pharmacol</addtitle><description>Platelet-activating factor (PAF) is an unusually potent phospholipid known to be produced by neuronal cells and to modulate
cerebral blood flow and metabolism. In previous studies with NCB-20 cells, we reported that PAF induced a significant mobilization
of intracellular free Ca2+ ([Ca2+]i), which was inhibited by PAF antagonists. The increase was the result of release from
intracellular stores and influx from extracellular sources. The present study was designed to characterize further PAF receptor-mediated
cellular signal-transduction mechanisms in myo-[3H]inositol-labeled cells. PAF induced a concentration-dependent increase
in phosphatidylinositol (Pl) metabolism, with EC50 values of 1.96 +/- 0.62 nM and 1.12 +/- 0.50 nM for inositol trisphosphate
(IP3) and inositol monophosphate (IP1) formation, respectively (four experiments). The maximal production of IP3 and IP1 induced
by 50 nM PAF was 254 +/- 34% and 178 +/- 25% over the basal, respectively (four experiments). PAF-induced Pl metabolism was
concentration-dependently inhibited by the PAF antagonist BN50739, with an IC50 value of 6.48 +/- 0.52 nM (four experiments).
The protein kinase C (PKC) activator phorbol 12,13-dibutyrate concentration-dependently inhibited PAF-induced Pl metabolism
and [Ca2+]i mobilization in NCB-20 cells, of NCB-20 cells with pertussis toxin (PTX) resulted in a concentration-dependent
inhibition of PAF-induced IP3 production and intracellular Ca2+ release, with a maximal reduction of 66.9 +/- 3.5% and 63
+/- 6.1%, respectively, at 300 ng/ml PTX. PTX in the presence of [32P]NAD specifically [32P]ADP-ribosylated a 38-kDa protein
in membranes prepared from NCB-20 cells. Pretreatment of the cells with PTX resulted in a concentration-dependent inhibition
of subsequent 32P-labeling of the toxin substrate in the membranes and correlated with the uncoupling of PAF-induced IP3 formation.
PAF (0.01-10 nM) elicited a concentration-related stimulation in guanosine 5'-O-(3-[35S]) triphosphate ([35S]GTP gamma S)
binding to G alpha i(1,2) proteins, which was inhibited by the PAF antagonist BN50739. PAF at 10 nM also increased [35S]GTP
gamma S binding to G alpha s and G alpha o. PAF-evoked activation of G alpha i(1,2) and G alpha o was reduced by preincubation
with PTX. Our results reveal that neuronal cells possess PAF receptors linked through guanine nucleotide-binding proteins
to phospholipase C and receptor-operated Ca2+ channels that are regulated by PKC. Both PTX-sensitive and -insensitive guanine
nucleotide-binding proteins appear to couple the PAF receptor to activation of phospholipase C and the increase in [Ca2+]i.
These results contribute to the further understanding of the mechanisms behind PAF actions on neuronal cells.</description><subject>Adenosine Diphosphate - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Brain - cytology</subject><subject>Brain - drug effects</subject><subject>Brain - metabolism</subject><subject>Calcium - metabolism</subject><subject>Cell physiology</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GTP-Binding Proteins - drug effects</subject><subject>GTP-Binding Proteins - physiology</subject><subject>Hybrid Cells - drug effects</subject><subject>Hybrid Cells - metabolism</subject><subject>Life Sciences & Biomedicine</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Neuroblastoma - drug therapy</subject><subject>Neuroblastoma - metabolism</subject><subject>Neuroblastoma - pathology</subject><subject>Pertussis Toxin</subject><subject>Pharmacology & Pharmacy</subject><subject>Phorbol 12,13-Dibutyrate - pharmacology</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Platelet Activating Factor - pharmacology</subject><subject>Protein Kinase C - pharmacology</subject><subject>Science & Technology</subject><subject>Signal transduction</subject><subject>Signal Transduction - drug effects</subject><subject>Signal Transduction - physiology</subject><subject>Stimulation, Chemical</subject><subject>Virulence Factors, Bordetella - pharmacology</subject><issn>0026-895X</issn><issn>1521-0111</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EZCTM</sourceid><sourceid>EIF</sourceid><recordid>eNqNkc-O0zAQhyMEWrqFR0DyAbisItnOnybclghYpAo47IFbNLEnzUBiF9vJ0nfkoXDUsmcOli193_zGHj9JNqKQIuVCiKfJhnNZplVdfH-eXHv_g3ORFxW_Sq5EJkTOq03y59sIAUcMKahACwQyB9bHs3XMB5rmFXt2HKyPi4z1FEgjC7MzdkHHyDCDs7PDqXOk2ZfmfSo5UziO_l2Eix0XnNAEZnt2RBdm78mzYH-TST2aNW5BdpjBkEFmZjWiXTukHRm9XubobEAynoHRMXCgLpZYw7rTP8R-kgGPrHmRPOth9Pjysm-T-48f7pu7dP_10-fmdp8Osi5DugOeZz0WVQZltuNYiFr3eVmi6mXfdxpqgE5JRMwrrXeR1BpLxKoUIOoy2yZvz7Gx_68ZfWgn8uuLwaCdfStKyesixm-TVxdx7ibU7dHRBO7UXqYf-esLB69g7B0YRf5RK4SodnURteqsPWBne68IjcJH61bUtbzb5zvJ4__yhgKs82nsbEIsvfn_0mi_OdsDHYYHctEcwE2g7GgPpzYXrWxlJbK_Nw_Eqw</recordid><startdate>19920201</startdate><enddate>19920201</enddate><creator>YUE, TL</creator><creator>STADEL, JM</creator><creator>SARAU, HM</creator><creator>FRIEDMAN, E</creator><creator>GU, JL</creator><creator>POWERS, DA</creator><creator>GLEASON, MM</creator><creator>FEUERSTEIN, G</creator><creator>WANG, HY</creator><general>American Society for Pharmacology and Experimental Therapeutics</general><general>Lippincott Williams & Wilkins</general><scope>BLEPL</scope><scope>DTL</scope><scope>EZCTM</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TK</scope></search><sort><creationdate>19920201</creationdate><title>Platelet-activating factor stimulates phosphoinositide turnover in neurohybrid NCB-20 cells: involvement of pertussis toxin-sensitive guanine nucleotide-binding proteins and inhibition by protein kinase C</title><author>YUE, TL ; STADEL, JM ; SARAU, HM ; FRIEDMAN, E ; GU, JL ; POWERS, DA ; GLEASON, MM ; FEUERSTEIN, G ; WANG, HY</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h296t-7a043fe583a6370e519df466ecf2ffbda9aabc2eee48dd74669de6ee861a1963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Adenosine Diphosphate - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Brain - cytology</topic><topic>Brain - drug effects</topic><topic>Brain - metabolism</topic><topic>Calcium - metabolism</topic><topic>Cell physiology</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GTP-Binding Proteins - drug effects</topic><topic>GTP-Binding Proteins - physiology</topic><topic>Hybrid Cells - drug effects</topic><topic>Hybrid Cells - metabolism</topic><topic>Life Sciences & Biomedicine</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Neuroblastoma - drug therapy</topic><topic>Neuroblastoma - metabolism</topic><topic>Neuroblastoma - pathology</topic><topic>Pertussis Toxin</topic><topic>Pharmacology & Pharmacy</topic><topic>Phorbol 12,13-Dibutyrate - pharmacology</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Platelet Activating Factor - pharmacology</topic><topic>Protein Kinase C - pharmacology</topic><topic>Science & Technology</topic><topic>Signal transduction</topic><topic>Signal Transduction - drug effects</topic><topic>Signal Transduction - physiology</topic><topic>Stimulation, Chemical</topic><topic>Virulence Factors, Bordetella - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>YUE, TL</creatorcontrib><creatorcontrib>STADEL, JM</creatorcontrib><creatorcontrib>SARAU, HM</creatorcontrib><creatorcontrib>FRIEDMAN, E</creatorcontrib><creatorcontrib>GU, JL</creatorcontrib><creatorcontrib>POWERS, DA</creatorcontrib><creatorcontrib>GLEASON, MM</creatorcontrib><creatorcontrib>FEUERSTEIN, G</creatorcontrib><creatorcontrib>WANG, HY</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 1992</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Neurosciences Abstracts</collection><jtitle>Molecular pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>YUE, TL</au><au>STADEL, JM</au><au>SARAU, HM</au><au>FRIEDMAN, E</au><au>GU, JL</au><au>POWERS, DA</au><au>GLEASON, MM</au><au>FEUERSTEIN, G</au><au>WANG, HY</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Platelet-activating factor stimulates phosphoinositide turnover in neurohybrid NCB-20 cells: involvement of pertussis toxin-sensitive guanine nucleotide-binding proteins and inhibition by protein kinase C</atitle><jtitle>Molecular pharmacology</jtitle><stitle>MOL PHARMACOL</stitle><addtitle>Mol Pharmacol</addtitle><date>1992-02-01</date><risdate>1992</risdate><volume>41</volume><issue>2</issue><spage>281</spage><epage>289</epage><pages>281-289</pages><issn>0026-895X</issn><eissn>1521-0111</eissn><coden>MOPMA3</coden><abstract>Platelet-activating factor (PAF) is an unusually potent phospholipid known to be produced by neuronal cells and to modulate
cerebral blood flow and metabolism. In previous studies with NCB-20 cells, we reported that PAF induced a significant mobilization
of intracellular free Ca2+ ([Ca2+]i), which was inhibited by PAF antagonists. The increase was the result of release from
intracellular stores and influx from extracellular sources. The present study was designed to characterize further PAF receptor-mediated
cellular signal-transduction mechanisms in myo-[3H]inositol-labeled cells. PAF induced a concentration-dependent increase
in phosphatidylinositol (Pl) metabolism, with EC50 values of 1.96 +/- 0.62 nM and 1.12 +/- 0.50 nM for inositol trisphosphate
(IP3) and inositol monophosphate (IP1) formation, respectively (four experiments). The maximal production of IP3 and IP1 induced
by 50 nM PAF was 254 +/- 34% and 178 +/- 25% over the basal, respectively (four experiments). PAF-induced Pl metabolism was
concentration-dependently inhibited by the PAF antagonist BN50739, with an IC50 value of 6.48 +/- 0.52 nM (four experiments).
The protein kinase C (PKC) activator phorbol 12,13-dibutyrate concentration-dependently inhibited PAF-induced Pl metabolism
and [Ca2+]i mobilization in NCB-20 cells, of NCB-20 cells with pertussis toxin (PTX) resulted in a concentration-dependent
inhibition of PAF-induced IP3 production and intracellular Ca2+ release, with a maximal reduction of 66.9 +/- 3.5% and 63
+/- 6.1%, respectively, at 300 ng/ml PTX. PTX in the presence of [32P]NAD specifically [32P]ADP-ribosylated a 38-kDa protein
in membranes prepared from NCB-20 cells. Pretreatment of the cells with PTX resulted in a concentration-dependent inhibition
of subsequent 32P-labeling of the toxin substrate in the membranes and correlated with the uncoupling of PAF-induced IP3 formation.
PAF (0.01-10 nM) elicited a concentration-related stimulation in guanosine 5'-O-(3-[35S]) triphosphate ([35S]GTP gamma S)
binding to G alpha i(1,2) proteins, which was inhibited by the PAF antagonist BN50739. PAF at 10 nM also increased [35S]GTP
gamma S binding to G alpha s and G alpha o. PAF-evoked activation of G alpha i(1,2) and G alpha o was reduced by preincubation
with PTX. Our results reveal that neuronal cells possess PAF receptors linked through guanine nucleotide-binding proteins
to phospholipase C and receptor-operated Ca2+ channels that are regulated by PKC. Both PTX-sensitive and -insensitive guanine
nucleotide-binding proteins appear to couple the PAF receptor to activation of phospholipase C and the increase in [Ca2+]i.
These results contribute to the further understanding of the mechanisms behind PAF actions on neuronal cells.</abstract><cop>BALTIMORE</cop><pub>American Society for Pharmacology and Experimental Therapeutics</pub><pmid>1311408</pmid><tpages>9</tpages></addata></record> |
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| ispartof | Molecular pharmacology, 1992-02, Vol.41 (2), p.281-289 |
| issn | 0026-895X 1521-0111 |
| language | eng |
| recordid | cdi_pubmed_primary_1311408 |
| source | Web of Science - Science Citation Index Expanded - 1992<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Adenosine Diphosphate - metabolism Animals Biological and medical sciences Brain - cytology Brain - drug effects Brain - metabolism Calcium - metabolism Cell physiology Cricetinae Cricetulus Fundamental and applied biological sciences. Psychology GTP-Binding Proteins - drug effects GTP-Binding Proteins - physiology Hybrid Cells - drug effects Hybrid Cells - metabolism Life Sciences & Biomedicine Membrane Proteins - metabolism Mice Molecular and cellular biology Neuroblastoma - drug therapy Neuroblastoma - metabolism Neuroblastoma - pathology Pertussis Toxin Pharmacology & Pharmacy Phorbol 12,13-Dibutyrate - pharmacology Phosphatidylinositols - metabolism Platelet Activating Factor - pharmacology Protein Kinase C - pharmacology Science & Technology Signal transduction Signal Transduction - drug effects Signal Transduction - physiology Stimulation, Chemical Virulence Factors, Bordetella - pharmacology |
| title | Platelet-activating factor stimulates phosphoinositide turnover in neurohybrid NCB-20 cells: involvement of pertussis toxin-sensitive guanine nucleotide-binding proteins and inhibition by protein kinase C |
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