High impact information on Vipr1

• This study demonstrates that the transcriptional repressor sequence of the rat vasoactive intestinal peptide receptor (VIPR) gene constitutes a 42-base pair core element that is the binding site for a nuclear protein [1].
• Transfection of VIP-RP expression vector into Cos cells resulted in transcriptional repression of a reporter construct containing multiple copies of the VIPR repressor element [1].
• Direct evidence for functional coupling of the vasoactive intestinal peptide receptor to Gi3 in native lung membranes [2].
• Identification of vasoactive intestinal peptide receptor subtypes in the lacrimal gland and their signal-transducing components [3].
• Solubilization and hydrodynamic characterization of guanine nucleotide sensitive vasoactive intestinal peptide-receptor complexes from rat intestine [4].

Biological context of Vipr1

• Promoter analysis of the 5'-flanking region of Vipr1 using a luciferase gene reporter system revealed that the isolated 5'-flanking region has functional promoter activity [5].
• The gene (Vipr1) is more than 16 kb in length and is divided into 13 exons [5].
• The differential sensitivity to guanylyl-imidodiphosphate suggests the existence of at least two vasoactive intestinal peptide receptor subtypes in brain, with distinct regional distribution, and may reflect differential coupling to second messenger systems [6].
• Differential effect of arachidonic acid on the vasoactive intestinal peptide receptor/effector system in rat prostatic epithelium during sexual maturation [7].
• Among them, the genes for the inducible nitric oxide synthase (Nos2) and for a vasoactive intestinal peptide receptor (Vipr) are potential candidates for genetic regulation of blood pressure and were localized to rat Chromosomes (Chrs) 10 and 8 respectively [8].

Anatomical context of Vipr1

• Vasoactive intestinal peptide receptor on liver plasma membranes: characterization as a glycoprotein [9].
• Characterization of the vasoactive intestinal peptide receptor in rat submandibular gland: radioligand binding assay in membrane preparations [10].
• Tumor-promoting phorbol esters interfere with the vasoactive intestinal peptide receptor/effector system in rat prostatic epithelial cells [11].
• Vasoactive intestinal peptide receptor antagonists in rat seminal vesicle membranes [12].
• Vasoactive intestinal peptide receptor localization in rat forebrain by autoradiography [13].

Associations of Vipr1 with chemical compounds

• The effect of streptozotocin diabetes on the vasoactive intestinal peptide receptor/effector system in membranes from rat ventral prostate [14].
• The pressor response was not antagonized by prior injection of the PACAP type II receptor antagonist PACAP6-38 (0.5 nmol), but was significantly attenuated by prior intravenous administration of phentolamine (1 mg/kg) [15].
• Lindane effect upon the vasoactive intestinal peptide receptor/effector system in rat enterocytes [16].
• Effects of chronic ethanol ingestion on the vasoactive intestinal peptide receptor-effector system from rat seminal vesicle membranes [17].
• Effects of GTP analogs and dithiothreitol on the binding properties of the vascular vasoactive intestinal peptide receptor [18].

Physical interactions of Vipr1

• The ED50 for vasoactive intestinal peptide-stimulated mucin release was 0.12 +/- 0.05 nM, thus suggesting an activation anomaly in the vasoactive intestinal peptide receptor-coupled signal transduction pathway at a point between cyclic AMP production and mucin release [19].

Regulatory relationships of Vipr1

• The PACAP-induced catecholamine output responses were inhibited by the PACAP type I receptor antagonist PACAP- (6-38) (30-3,000 nM) but were resistant to the PACAP type II receptor antagonist [Lys1,Pro2,5,Ara3,4,Tyr6]-vasoactive intestinal peptide (LPAT-VIP; 30-3,000 nM) [20].

Analytical, diagnostic and therapeutic context of Vipr1

• Southwestern blot analysis indicated that the VIPR repressor element interacts specifically with a nuclear protein of about 72 kDa [1].
• Molecular cloning of a novel transcriptional repressor protein of the rat type 1 vasoactive intestinal peptide receptor gene [1].
• Influence of castration and testosterone treatment on the vasoactive intestinal peptide receptor/effector system in rat prostatic epithelial cells [21].

References