Isoproterenol-induced intramembrane particle aggregation and water flux in toad epidermis

Brown, Dennis; Grosso, A.; Sousa, R. C. de

doi:10.1016/0005-2736(80)90181-9

Cited by 34 publications

(6 citation statements)

References 21 publications

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“…The binding to luminal membranes may represent an 'internalization' process of a receptor-peptide complex in the kidney (Brown, Grosso & DeSousa, 1980) and toad urinary bladder (Muller, Kachadorian & Discala, 1980). Vasopressin also stimulates forma¬ tion of intramembrane particle (IMP) aggregates, which are transferred from the cytoplasm to luminal membranes (Wade, Guckian & Koeppen, 1984).…”

Section: Discussionmentioning

confidence: 98%

Immunocytochemical localization of vasopressin-binding sites in the rat kidney

Ravid¹,

Swaab²,

Pool³

1985

Journal of Endocrinology

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The rat kidney and brain are major target organs for vasopressin (VP). A procedure was developed for immunocytochemical staining of VP and its binding sites in the kidney. This procedure involved preincubation of kidney sections with the ligand, followed by immunocytochemical detection of VP. The staining in renal tubules from Wistar rats was enhanced by preincubation of tissue sections with increasing concentrations of VP (6-6000 nmol/l). Staining was present in the epithelium of distal convolutions and collecting ducts (medullary and cortical portions) and more pronounced in the apical zone of the tubular epithelium. With high concentrations of VP in the preincubation, staining was also obtained in the thick ascending limb of the loop of Henle. There was no staining under any circumstances in proximal tubules. In the kidney of the Brattleboro rat homozygous for hypothalamic diabetes insipidus (DI) which congenitally lacks VP but responds to the peptide, exactly the same staining pattern was observed after preincubation with VP, but the maximal staining was less intense. The VP binding to the DI rat kidney, after 2 weeks treatment with VP (using Accurel implants), reached levels seen in the Wistar kidney after in-vitro preincubation with high doses of VP.

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Section: Discussionmentioning

confidence: 98%

Immunocytochemical localization of vasopressin-binding sites in the rat kidney

Ravid¹,

Swaab²,

Pool³

1985

Journal of Endocrinology

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“…Water permeability in the pelvic skin of frogs is considered to be regulated by at least two systems: the first is via the AVT V2 receptor, and the other is via the -adrenergic receptor (Brown et al, 1980;De Sousa and Grosso, 1982). Our group has shown that both AQP-h2 and AQP-h3 proteins are translocated in response to AVT to the apical plasma membrane of principal cells in the outermost granular layer [i.e.…”

Section: Introductionmentioning

confidence: 99%

Correlation between aquaporin and water permeability in response to vasotocin, hydrin and β-adrenergic effectors in the ventral pelvic skin of the tree frogHyla japonica

Ogushi

Kitagawa

Hasegawa

et al. 2010

Journal of Experimental Biology

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SUMMARYThe ventral pelvic skin of the tree frog Hyla japonica expresses two kinds of arginine vasotocin (AVT)-stimulated aquaporins (AQP-h2 and AQP-h3), which affect the capacity of the frog's skin to absorb water. As such, it can be used as a model system for analyzing the molecular mechanisms of water permeability. We investigated AQP dynamics and water permeability in the pelvic skin of H. japonica following challenge with AVT, hydrins (intermediate peptides of pro-AVT) and -adrenergic effectors. In the in vivo experiment, both AQP-h2 and AQP-h3 proteins were translocated to the apical plasma membrane in the principal cells of the first-reacting cell (FRC) layer in the pelvic skin following challenge with AVT, hydrin 1 and hydrin 2, thereby increasing the water permeability of the pelvic skin. The -adrenergic receptor agonist isoproterenol (IP) and its anatagonist propranolol (PP) in combination with AVT or hydrins were used as challenge in the in vitro experiment. IP increased water permeability whereas PP inhibited it, and both events were well correlated with the translocation of the AQPs to the apical membrane. In the PP+AVT-treated skins, labels for AQP-h2 and AQP-h3 were differentially visible among the principal cells; the apical plasma membrane of some cells was labeled while others were not, indicating that the response of PP or AVT is different from cell to cell. These results provide morphological evidence that the principal cells of the FRC layers may have two kinds of receptors: a V2 receptor and -adrenergic receptor.

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“…The terminal step in the vasopressin-induced pathway is a structural change in the luminal membrane. In mammalian collecting ducts, preformed membrane segments (intramembranous particle aggregates) are inserted into the luminal membrane of collecting duct cells (Harmanci et al 1978(Harmanci et al , 1980; Brown & Orci 1983). Similar structural changes have been reported in amphibian urinary bladder (Bourguet et al 1976; Kachadorian et al 1977) and amphibian skin (Brown et af.…”

Section: Introductionmentioning

confidence: 71%

EFFECT OF pH ON VASOPRESSIN‐INDUCED WATER PERMEABILITY IN COLLECTING DUCTS OF ISOLATED RAT PAPILLAE

Fitzgibbon

Morgan

1988

Clin Exp Pharma Physio

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1. The effects of basolateral and luminal pH on diffusional water permeability of microperfused collecting ducts of isolated rat papillae were examined in the presence and absence of vasopressin at two concentrations. 2. In the absence of vasopressin, collecting duct diffusional water permeabilities did not differ when the pH of the luminal fluid was varied. Similarly, in the absence of vasopressin, collecting duct diffusional water permeabilities did not differ when the bath pH was varied. 3. In the presence of 50 microU/ml vasopressin, increases in diffusional water permeability of collecting ducts perfused with solutions at pH 5.0, 7.4 or 9.0 did not differ significantly. Similarly, increases in diffusional water permeability induced by 200 microU/ml vasopressin were not different when collecting ducts were perfused with solutions at pH 5.0, 7.4 or 9.0. 4. The presence of vasopressin (50 microU/ml) in the bathing medium at pH 6.4, 7.4 and 8.4 induced increments in diffusional water permeability of 0.40 +/- 0.21 (n = 14, P greater than 0.05), 1.56 +/- 0.27 (n = 27, P less than 0.001) and 1.67 +/- 0.24 (n = 12, P less than 0.001) microns/s, respectively. The increment in water permeability at pH 6.4 was significantly less than that at pH 7.4 (P less than 0.001). 5. The presence of vasopressin (200 microU/ml) in the bathing medium at pH 6.4, 7.4 and 8.4 induced increments in diffusional water permeability of 2.16 +/- 0.54 (n = 9, P less than 0.01), 2.55 +/- 0.51 (n = 17, P less than 0.001) and 0.98 +/- 0.34 (n = 11, P less than 0.05) microns/s respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

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Isoproterenol-induced intramembrane particle aggregation and water flux in toad epidermis

Cited by 34 publications

References 21 publications

Immunocytochemical localization of vasopressin-binding sites in the rat kidney

Immunocytochemical localization of vasopressin-binding sites in the rat kidney

Correlation between aquaporin and water permeability in response to vasotocin, hydrin and β-adrenergic effectors in the ventral pelvic skin of the tree frogHyla japonica

EFFECT OF pH ON VASOPRESSIN‐INDUCED WATER PERMEABILITY IN COLLECTING DUCTS OF ISOLATED RAT PAPILLAE

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