Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fine regulation of water reabsorption by the antidiuretic hormone [8-arginine]vasopressin (AVP) occurs in principal cells of the collecting duct and is largely dependent on regulation of the aquaporin-2 (AQP2) water channel. AVP-inducible long term AQP2 expression was investigated in immortalized mouse cortical collecting duct principal cells. Combined RNase protection assay, Western blot, and immunofluorescence analyses revealed that physiological concentrations of AVP added to the basal side, but not to the apical side, of cells grown on filters induced both AQP2 mRNA and apical protein expression. The stimulatory effect of AVP on AQP2 expression followed a V(2) receptor-dependent pathway because [deamino-8-d-arginine]vasopressin (dDAVP), a specific V(2) receptor agonist, produced the same effect as AVP, whereas the V(2) antagonist SR121463B antagonized action of both AVP and dDAVP. Moreover, forskolin and cyclic 8-bromo-AMP fully reproduced the effects of AVP on AQP2 expression. Analysis of protein degradation pathways showed that inhibition of proteasomal activity prevented synthesis of AVP-inducible AQP2 mRNA and protein. Once synthesized, AQP2 protein was quickly degraded, a process that involves both the proteasomal and lysosomal pathways. This is the first study that delineates induction and degradation mechanisms of AQP2 endogenously expressed by a renal collecting duct principal cell line.
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PMID:Long term regulation of aquaporin-2 expression in vasopressin-responsive renal collecting duct principal cells. 1178 89

In the renal collecting duct (CD) the major physiological role of aldosterone is to promote Na+ reabsorption. In addition, aldosterone may also influence CD water permeability elicited by vasopressin (AVP). We have previously shown that endogenous expression of the aquaporin-2 (AQP2) water channel in immortalized mouse cortical CD principal cells (mpkCCDC14) grown on filters is dramatically increased by administration of physiological concentrations of AVP. In the present study, we investigated the influence of aldosterone on AQP2 expression in mpkCCDC14 cells by RNase protection assay and Western blot analysis. Aldosterone reduced AQP2 mRNA and protein expression when administered together with AVP for short periods of time (< or =24 h). For longer periods of time, however, aldosterone increased AQP2 protein expression despite sustained low expression levels of AQP2 mRNA. Both events were dependent on mineralocorticoid receptor occupancy because they were both induced by a low concentration of aldosterone (10-9 m) and were abolished by the mineralocorticoid receptor antagonist canrenoate. Inhibition of lysosomal AQP2 protein degradation increased AQP2 protein expression in AVP-treated cells, an effect that was potentiated by aldosterone. Finally, both aldosterone and actinomycin D delayed AQP2 protein decay following AVP washout, but in a non-cumulative manner. Taken together, our data suggest that aldosterone tightly modulates AQP2 protein expression in cultured mpkCCDC14 cells by increasing AQP2 protein turnover while maintaining low levels of AQP2 mRNA expression.
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PMID:Dual influence of aldosterone on AQP2 expression in cultured renal collecting duct principal cells. 1266 Feb 45

Abstract An ontogenic series of chick embryo brains (4, 6, 9,12,14,16 and 18 days of incubation, hatching day: 21) was coronally or saggitally sectioned and investigated for expression of the arginine vasotocin (AVT)/mesotocin (MT) gene. To this end a 39mer oligonucleotide recognizing the AVT/MT encoding sequence of their respective mRNAs was constructed employing optimized codon usage and was used for in situ hybridization. AVT/MT mRNA-expressing neurons were first detected on embryonal day (E) 6 adjacent to the third ventricle. By E9 the periventricular nucleus had expanded in size but the hybridization signal was weaker. These results suggest a migration of cells in all directions away from the third ventricle into the diencephalon; some perikarya were even observed at the lateral pial surface above the optic chiasm. By E12, brain differentiation had advanced to distinct hypothalamo-neurohypophyseal nuclei (supraoptic and paraventricular nuclei) as well as to accessory groups expressing AVT/MT mRNA. Two cell types were then distinguishable in the paraventricular nucleus; the specific mRNA was expressed either as a weak or a strong hybridization signal. Comparison with other studies suggested that differentiation had almost attained adult level though cell growth and differentiation of supraoptic and paraventricular nuclei still occurred. This was complete by E18 when individual cells were larger and the intensity of the hybridization signal became very strong. RNase pretreatment depressed the signal by 100%. Northern blot hybridization of RNA extracted from newly hatched chicks verified the specificity of the probe. A single band was evident, indicating an mRNA of approximately 700 bases, which is only found in hypothalamus and not in muscle, liver or extra-hypothalamic brain, and corresponds in size closely with mammalian vasopressin mRNA. The data demonstrate a very early development (E6) of neurohypophyseal hormone gene expression in the chick embryo brain with important differentiation around E9. At E12 magnocellular neuronal arrangement resembled adult neurons but the gene expression signal increased in intensity until E18.
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PMID:Embryonal development of arginine vasotocin/mesotocin gene expression in the chicken brain. 1921 Apr 19

A new multiple fluorescence in situ hybridization method based on hybridization chain reaction was recently reported, enabling simultaneous mapping of multiple target mRNAs within intact zebrafish and mouse embryos. With this approach, DNA probes complementary to target mRNAs trigger chain reactions in which metastable fluorophore-labeled DNA hairpins self-assemble into fluorescent amplification polymers. The formation of the specific polymers enhances greatly the sensitivity of multiple fluorescence in situ hybridization. In this study we describe the optimal parameters (hybridization chain reaction time and temperature, hairpin and salt concentration) for multiple fluorescence in situ hybridization via amplification of hybridization chain reaction for frozen tissue sections. The combined use of fluorescence in situ hybridization and immunofluorescence, together with other control experiments (sense probe, neutralization and competition, RNase treatment, and anti-sense probe without initiator) confirmed the high specificity of the fluorescence in situ hybridization used in this study. Two sets of three different mRNAs for oxytocin, vasopressin and somatostatin or oxytocin, vasopressin and thyrotropin releasing hormone were successfully visualized via this new method. We believe that this modified protocol for multiple fluorescence in situ hybridization via hybridization chain reaction would allow researchers to visualize multiple target nucleic acids in the future.
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PMID:A modified protocol for the detection of three different mRNAs with a new-generation in situ hybridization chain reaction on frozen sections. 2772 91


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