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1.
Cell Signal ; 13(11): 835-9, 2001 Nov.
Article in English | MEDLINE | ID: mdl-11583919

ABSTRACT

We cloned MafG-2, a novel splice variant of MafG, from rat brain by RT-PCR method. MafG-2 differs from the previously published MafG by an insertion of 27 amino acids. Sequence analysis of the cDNA-encoded MafG-2 showed that MafG-2 contains basic domain and basic leucine zipper (bZip) motif. Transient transfection studies with GFP-MafG-2 chimera protein indicate that MafG-2 is localized in the nuclei of transfected COS-7 cells. To determine whether gene expression of mafG-2 mRNA is induced by an increase in extracellular protons, we analyzed expression of the mRNA in PC12 cells after an increase in extracellular proton concentration. We found that the mafG-2 mRNA expression increased when extracellular pH was decreased gradually from 7.40 to 7.20 and that there was a significant correlation between extracellular pH value and the expression of mafG-2 mRNA. These results suggest that an increase in extracellular proton may induce the expression of mafG-2 mRNA and MafG-2 may be involved in signal transduction of extracellular of H(+).


Subject(s)
DNA-Binding Proteins/genetics , Nuclear Proteins/genetics , Protons , Repressor Proteins/genetics , Transcription Factors/genetics , Transcriptional Activation , Amino Acid Sequence , Animals , Base Sequence , COS Cells , Cloning, Molecular , DNA-Binding Proteins/biosynthesis , Extracellular Space/physiology , Hydrogen-Ion Concentration , MafG Transcription Factor , Mice , Molecular Sequence Data , Nuclear Proteins/biosynthesis , PC12 Cells , Phylogeny , RNA, Messenger/biosynthesis , Rats , Repressor Proteins/biosynthesis , Sequence Homology, Amino Acid , Transcription Factors/biosynthesis
2.
Regul Pept ; 99(2-3): 87-92, 2001 Jun 15.
Article in English | MEDLINE | ID: mdl-11384769

ABSTRACT

Apelin is an endogenous ligand of the human orphan receptor APJ. We detected apelin-like immunoreactivity in the adipocytes, gastric mucosa, and Kupffer cells in the liver. We also detected apelin-like immunoreactivity localized within the endothelia of small arteries in various organs. Further, it was found that mean arterial pressure after the administration of apelin-12, apelin-13, and apelin-36 at a dose of 10 nmol/kg in anaesthetized rats was reduced by 26+/-5, 11+/-4, and 5+/-4 mm Hg, respectively. In the presence of a nitric oxide (NO) synthase inhibitor, the effect of apelin-12 on blood pressure was abolished. Furthermore, the administration of apelin-12 (10 nmol/kg) in rats produced a transitory elevation of the plasma nitrite/nitrate concentration from a basal level of 21.4+/-1.6 to 27.0+/-1.5 microM. Thus, apelin may lower blood pressure via a nitric oxide-dependent mechanism.


Subject(s)
Antihypertensive Agents/administration & dosage , Blood Pressure/drug effects , Carrier Proteins/physiology , Nitric Oxide/physiology , Peptides/physiology , Receptors, G-Protein-Coupled , Animals , Antihypertensive Agents/chemical synthesis , Apelin , Apelin Receptors , Carrier Proteins/administration & dosage , Carrier Proteins/chemical synthesis , Enzyme Inhibitors/administration & dosage , Enzyme Inhibitors/pharmacology , In Vitro Techniques , Injections, Intraperitoneal , Injections, Intravenous , Intercellular Signaling Peptides and Proteins , Ligands , Male , NG-Nitroarginine Methyl Ester/administration & dosage , NG-Nitroarginine Methyl Ester/pharmacology , Nitrates/blood , Nitric Oxide/blood , Nitric Oxide Synthase/antagonists & inhibitors , Nitric Oxide Synthase/metabolism , Nitric Oxide Synthase Type III , Nitrites/blood , Organ Specificity , Peptides/administration & dosage , Peptides/chemical synthesis , Rats , Rats, Wistar , Receptors, Dopamine D2/metabolism
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