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Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | European Journal of Biochemistry, 174, 1988, 3, S. 531-535 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
RESINK, Thérèse J. PANCHENKO, Michail P. TKACHUK, Vsevolod A. BÜHLER, Fritz R. RESINK, Thérèse J. PANCHENKO, Michail P. TKACHUK, Vsevolod A. BÜHLER, Fritz R. |
|---|---|
| author |
RESINK, Thérèse J. PANCHENKO, Michail P. TKACHUK, Vsevolod A. BÜHLER, Fritz R. |
| spellingShingle |
RESINK, Thérèse J. PANCHENKO, Michail P. TKACHUK, Vsevolod A. BÜHLER, Fritz R. European Journal of Biochemistry Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes Biochemistry |
| author_sort |
resink, thérèse j. |
| spelling |
RESINK, Thérèse J. PANCHENKO, Michail P. TKACHUK, Vsevolod A. BÜHLER, Fritz R. 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1988.tb14131.x <jats:p>In the presence of 1 μM atrial natriuretic factor (ANF) and low (0.1 mM) Mg<jats:sup>2+</jats:sup> concentrations, the initial rate of binding of [<jats:sup>3</jats:sup>H]guanosine 5′‐[β,γ‐imido)triphosphate ([<jats:sup>3</jats:sup>H]p[NH]ppG) to rat lung plasma membranes was increased twofold to threefold. ANF‐dependent stimulation of the initial rate of [<jats:sup>3</jats:sup>H]p[NH]ppG binding was reduced at high (5 mM) Mg<jats:sup>2+</jats:sup> concentrations. Preincubation of membranes with p[NH]ppG (5 min at 37°C) eliminated the ANF‐dependent effect on [<jats:sup>3</jats:sup>H]p[NH]ppG binding whereas ANF‐dependent [<jats:sup>3</jats:sup>H]p[NH]ppG binding was unaffected by similar pretreatment with guanosine 5′‐[β‐thio]diphosphate (GDP[βS]). An increase in ANF concentration from 10 pM to 1 μM caused a 40% decrease in forskolin‐stimulated or isoproterenol‐stimulated adenylate cyclase activities (IC<jats:sub>50</jats:sub> 5 nM) in rat lung plasma membranes. GTP (100 μM) was obligatory for the ANF‐dependent inhibition of adenylate cyclase, which could be completely overcome by the presence of 100 μM GDP[βS] or the addition of 10 mM Mn<jats:sup>2+</jats:sup>. Reduction of Na<jats:sup>2+</jats:sup> concentration from 120 mM to 20 mM had the same effect. Pertussis toxin eliminated ANF‐dependent inhibition of adenylate cyclase by catalyzing ADP‐ribosylation of membrane‐bound N<jats:sub>i</jats:sub> protein (41‐kDa α subunit of the inhibitory guanyl‐nucleotide‐binding protein of adenylate cyclase). The data support the notion that one of the ANF receptors in rat lung plasma membranes is negatively coupled to a hormone‐sensitive adenylate cyclase complex via the GTP‐binding N<jats:sub>i</jats:sub> protein.</jats:p> Involvement of N<sub>i</sub> protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes European Journal of Biochemistry |
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10.1111/j.1432-1033.1988.tb14131.x |
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Online Free |
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Chemie und Pharmazie |
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Wiley, 1988 |
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Wiley, 1988 |
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0014-2956 1432-1033 |
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0014-2956 1432-1033 |
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resink1988involvementofniproteininthefunctionalcouplingoftheatrialnatriureticfactoranfreceptortoadenylatecyclaseinratlungplasmamembranes |
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1988 |
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European Journal of Biochemistry |
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49 |
| title |
Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_unstemmed |
Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_full |
Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_fullStr |
Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_full_unstemmed |
Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_short |
Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_sort |
involvement of n<sub>i</sub> protein in the functional coupling of the atrial natriuretic factor (anf) receptor to adenylate cyclase in rat lung plasma membranes |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1432-1033.1988.tb14131.x |
| publishDate |
1988 |
| physical |
531-535 |
| description |
<jats:p>In the presence of 1 μM atrial natriuretic factor (ANF) and low (0.1 mM) Mg<jats:sup>2+</jats:sup> concentrations, the initial rate of binding of [<jats:sup>3</jats:sup>H]guanosine 5′‐[β,γ‐imido)triphosphate ([<jats:sup>3</jats:sup>H]p[NH]ppG) to rat lung plasma membranes was increased twofold to threefold. ANF‐dependent stimulation of the initial rate of [<jats:sup>3</jats:sup>H]p[NH]ppG binding was reduced at high (5 mM) Mg<jats:sup>2+</jats:sup> concentrations. Preincubation of membranes with p[NH]ppG (5 min at 37°C) eliminated the ANF‐dependent effect on [<jats:sup>3</jats:sup>H]p[NH]ppG binding whereas ANF‐dependent [<jats:sup>3</jats:sup>H]p[NH]ppG binding was unaffected by similar pretreatment with guanosine 5′‐[β‐thio]diphosphate (GDP[βS]). An increase in ANF concentration from 10 pM to 1 μM caused a 40% decrease in forskolin‐stimulated or isoproterenol‐stimulated adenylate cyclase activities (IC<jats:sub>50</jats:sub> 5 nM) in rat lung plasma membranes. GTP (100 μM) was obligatory for the ANF‐dependent inhibition of adenylate cyclase, which could be completely overcome by the presence of 100 μM GDP[βS] or the addition of 10 mM Mn<jats:sup>2+</jats:sup>. Reduction of Na<jats:sup>2+</jats:sup> concentration from 120 mM to 20 mM had the same effect. Pertussis toxin eliminated ANF‐dependent inhibition of adenylate cyclase by catalyzing ADP‐ribosylation of membrane‐bound N<jats:sub>i</jats:sub> protein (41‐kDa α subunit of the inhibitory guanyl‐nucleotide‐binding protein of adenylate cyclase). The data support the notion that one of the ANF receptors in rat lung plasma membranes is negatively coupled to a hormone‐sensitive adenylate cyclase complex via the GTP‐binding N<jats:sub>i</jats:sub> protein.</jats:p> |
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| author | RESINK, Thérèse J., PANCHENKO, Michail P., TKACHUK, Vsevolod A., BÜHLER, Fritz R. |
| author_facet | RESINK, Thérèse J., PANCHENKO, Michail P., TKACHUK, Vsevolod A., BÜHLER, Fritz R., RESINK, Thérèse J., PANCHENKO, Michail P., TKACHUK, Vsevolod A., BÜHLER, Fritz R. |
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| description | <jats:p>In the presence of 1 μM atrial natriuretic factor (ANF) and low (0.1 mM) Mg<jats:sup>2+</jats:sup> concentrations, the initial rate of binding of [<jats:sup>3</jats:sup>H]guanosine 5′‐[β,γ‐imido)triphosphate ([<jats:sup>3</jats:sup>H]p[NH]ppG) to rat lung plasma membranes was increased twofold to threefold. ANF‐dependent stimulation of the initial rate of [<jats:sup>3</jats:sup>H]p[NH]ppG binding was reduced at high (5 mM) Mg<jats:sup>2+</jats:sup> concentrations. Preincubation of membranes with p[NH]ppG (5 min at 37°C) eliminated the ANF‐dependent effect on [<jats:sup>3</jats:sup>H]p[NH]ppG binding whereas ANF‐dependent [<jats:sup>3</jats:sup>H]p[NH]ppG binding was unaffected by similar pretreatment with guanosine 5′‐[β‐thio]diphosphate (GDP[βS]). An increase in ANF concentration from 10 pM to 1 μM caused a 40% decrease in forskolin‐stimulated or isoproterenol‐stimulated adenylate cyclase activities (IC<jats:sub>50</jats:sub> 5 nM) in rat lung plasma membranes. GTP (100 μM) was obligatory for the ANF‐dependent inhibition of adenylate cyclase, which could be completely overcome by the presence of 100 μM GDP[βS] or the addition of 10 mM Mn<jats:sup>2+</jats:sup>. Reduction of Na<jats:sup>2+</jats:sup> concentration from 120 mM to 20 mM had the same effect. Pertussis toxin eliminated ANF‐dependent inhibition of adenylate cyclase by catalyzing ADP‐ribosylation of membrane‐bound N<jats:sub>i</jats:sub> protein (41‐kDa α subunit of the inhibitory guanyl‐nucleotide‐binding protein of adenylate cyclase). The data support the notion that one of the ANF receptors in rat lung plasma membranes is negatively coupled to a hormone‐sensitive adenylate cyclase complex via the GTP‐binding N<jats:sub>i</jats:sub> protein.</jats:p> |
| doi_str_mv | 10.1111/j.1432-1033.1988.tb14131.x |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTg4LnRiMTQxMzEueA |
| imprint | Wiley, 1988 |
| imprint_str_mv | Wiley, 1988 |
| institution | DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4 |
| issn | 0014-2956, 1432-1033 |
| issn_str_mv | 0014-2956, 1432-1033 |
| language | English |
| last_indexed | 2024-03-01T15:43:42.56Z |
| match_str | resink1988involvementofniproteininthefunctionalcouplingoftheatrialnatriureticfactoranfreceptortoadenylatecyclaseinratlungplasmamembranes |
| mega_collection | Wiley (CrossRef) |
| physical | 531-535 |
| publishDate | 1988 |
| publishDateSort | 1988 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | European Journal of Biochemistry |
| source_id | 49 |
| spelling | RESINK, Thérèse J. PANCHENKO, Michail P. TKACHUK, Vsevolod A. BÜHLER, Fritz R. 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1988.tb14131.x <jats:p>In the presence of 1 μM atrial natriuretic factor (ANF) and low (0.1 mM) Mg<jats:sup>2+</jats:sup> concentrations, the initial rate of binding of [<jats:sup>3</jats:sup>H]guanosine 5′‐[β,γ‐imido)triphosphate ([<jats:sup>3</jats:sup>H]p[NH]ppG) to rat lung plasma membranes was increased twofold to threefold. ANF‐dependent stimulation of the initial rate of [<jats:sup>3</jats:sup>H]p[NH]ppG binding was reduced at high (5 mM) Mg<jats:sup>2+</jats:sup> concentrations. Preincubation of membranes with p[NH]ppG (5 min at 37°C) eliminated the ANF‐dependent effect on [<jats:sup>3</jats:sup>H]p[NH]ppG binding whereas ANF‐dependent [<jats:sup>3</jats:sup>H]p[NH]ppG binding was unaffected by similar pretreatment with guanosine 5′‐[β‐thio]diphosphate (GDP[βS]). An increase in ANF concentration from 10 pM to 1 μM caused a 40% decrease in forskolin‐stimulated or isoproterenol‐stimulated adenylate cyclase activities (IC<jats:sub>50</jats:sub> 5 nM) in rat lung plasma membranes. GTP (100 μM) was obligatory for the ANF‐dependent inhibition of adenylate cyclase, which could be completely overcome by the presence of 100 μM GDP[βS] or the addition of 10 mM Mn<jats:sup>2+</jats:sup>. Reduction of Na<jats:sup>2+</jats:sup> concentration from 120 mM to 20 mM had the same effect. Pertussis toxin eliminated ANF‐dependent inhibition of adenylate cyclase by catalyzing ADP‐ribosylation of membrane‐bound N<jats:sub>i</jats:sub> protein (41‐kDa α subunit of the inhibitory guanyl‐nucleotide‐binding protein of adenylate cyclase). The data support the notion that one of the ANF receptors in rat lung plasma membranes is negatively coupled to a hormone‐sensitive adenylate cyclase complex via the GTP‐binding N<jats:sub>i</jats:sub> protein.</jats:p> Involvement of N<sub>i</sub> protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes European Journal of Biochemistry |
| spellingShingle | RESINK, Thérèse J., PANCHENKO, Michail P., TKACHUK, Vsevolod A., BÜHLER, Fritz R., European Journal of Biochemistry, Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes, Biochemistry |
| title | Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_full | Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_fullStr | Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_full_unstemmed | Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_short | Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| title_sort | involvement of n<sub>i</sub> protein in the functional coupling of the atrial natriuretic factor (anf) receptor to adenylate cyclase in rat lung plasma membranes |
| title_unstemmed | Involvement of Ni protein in the functional coupling of the atrial natriuretic factor (ANF) receptor to adenylate cyclase in rat lung plasma membranes |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1111/j.1432-1033.1988.tb14131.x |