Effect of guanine nucleotides on [3H]glutamate binding and on adenylate cyclase activity in rat brain membranes. 1997

M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
Departamento de Quimica, Centro de Ciências Naturais e Exatas, Universidade Federal de Santa Maria, RS, Brasil.

GMP-PNP, a non-hydrolyzable analog of GTP binds tightly to G-protein in the presence of Mg2+, so that the binding is stable even after exhaustive washings. This property was exploited to prepare membrane samples of rat brain where G-protein GTP-binding sites were saturated with GMP-PNP. Experiments carried out with these membranes showed that GTP, GMP-PNP, GDP-S and GMP (1 mM) inhibit the sodium-independent [3H]glutamate binding by 30-40% [F(4,40) = 5.9; p < .001], whereas only GMP-PNP activates adenylate cyclase activity [F(6,42) = 3.56; p < .01]. The inhibition of sodium-independent [3H]glutamate binding occurred in the absence of Mg2+. These findings suggest that guanine nucleotides may inhibit glutamate binding and activate adenylate cyclase through distinct mechanisms by acting on different sites.

UI MeSH Term Description Entries
D008274 Magnesium A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
D008297 Male Males
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D006150 Guanine Nucleotides Guanine Nucleotide,Guanosine Phosphates,Nucleotide, Guanine,Nucleotides, Guanine,Phosphates, Guanosine
D006153 Guanosine Diphosphate A guanine nucleotide containing two phosphate groups esterified to the sugar moiety. GDP,Guanosine 5'-Diphosphate,Guanosine 5'-Trihydrogen Diphosphate,5'-Diphosphate, Guanosine,5'-Trihydrogen Diphosphate, Guanosine,Diphosphate, Guanosine,Diphosphate, Guanosine 5'-Trihydrogen,Guanosine 5' Diphosphate,Guanosine 5' Trihydrogen Diphosphate
D006157 Guanosine Monophosphate A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature. 5'-Guanylic Acid,Guanosine 5'-Monophosphate,5'-GMP,Guanylic Acid,5' Guanylic Acid,5'-Monophosphate, Guanosine,Acid, 5'-Guanylic,Acid, Guanylic,Guanosine 5' Monophosphate,Monophosphate, Guanosine
D006160 Guanosine Triphosphate Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety. GTP,Triphosphate, Guanosine
D006165 Guanylyl Imidodiphosphate A non-hydrolyzable analog of GTP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It binds tightly to G-protein in the presence of Mg2+. The nucleotide is a potent stimulator of ADENYLYL CYCLASES. GMP-PNP,GMP-P(NH)P,Gpp(NH)p,Guanosine 5'-(Beta,Gamma-Imido)Triphosphate,Guanyl-5'-Imidodiphosphate,P(NH)PPG,Guanyl 5' Imidodiphosphate,Imidodiphosphate, Guanylyl
D000262 Adenylyl Cyclases Enzymes of the lyase class that catalyze the formation of CYCLIC AMP and pyrophosphate from ATP. Adenyl Cyclase,Adenylate Cyclase,3',5'-cyclic AMP Synthetase,Adenylyl Cyclase,3',5' cyclic AMP Synthetase,AMP Synthetase, 3',5'-cyclic,Cyclase, Adenyl,Cyclase, Adenylate,Cyclase, Adenylyl,Cyclases, Adenylyl,Synthetase, 3',5'-cyclic AMP

Related Publications

M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
January 1980, European journal of pharmacology,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
July 1983, Pediatric research,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
January 1987, European journal of biochemistry,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
June 1977, The Journal of biological chemistry,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
September 1997, Biochemistry and molecular biology international,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
February 1990, Biochemical and biophysical research communications,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
February 1978, European journal of biochemistry,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
January 1981, Recent progress in hormone research,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
November 1994, FEBS letters,
M A Rubin, and A C Medeiros, and P C Rocha, and C B Livi, and G Ramirez, and D O Souza
February 1983, Journal of immunology (Baltimore, Md. : 1950),
Copied contents to your clipboard!