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)

Long-term (24 h) pretreatment of cultured rat vascular smooth muscle cells with 100 nM angiotensin and 1 microM vasopressin induced a marked reduction of the maximal binding capacity of atrial natriuretic peptide (ANP) receptors in a fashion similar to that induced by phorbol ester. The down-regulation of the receptors induced by vasoconstrictors and phorbol ester was concomitantly associated with an attenuation of ANP-stimulated cGMP accumulation. These data suggest that vasoconstrictor-induced activation of protein kinase C is involved in the mechanism of heterologous down-regulation of vascular ANP receptors.
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PMID:Vasoconstrictor-induced heterologous down-regulation of vascular atrial natriuretic peptide receptor. 254 76

An increase in the water permeability of the frog urinary bladder due to vasopressin, correlates with an increase of cAMP content in the bladder tissue. The osmotic permeability reached its maximum in 15-20 min. The sharp increase of inositol triphosphate content was observed within 20 sec after vasopressin administration, whereas cGMP content significantly decreased within 5 min. The augmentation of cAMP content seems to lead to a rise in water permeability white inositol triphosphate and cGMP acted, probably, as modulators of the vasopressin effect.
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PMID:[Effect of vasopressin on the osmotic permeability of the bladder wall in the frog and its content of cAMP, cGMP and inositol triphosphate]. 254 97

The L-arginine antagonist NG-monomethyl-L-arginine has been shown to inhibit nitric oxide formation from L-arginine in endothelial cells. In the present study NG-monomethyl-L-arginine was used to assess the role of L-arginine for cyclic GMP stimulation by vasopressin in a kidney epithelial cell line (LLC-PK1). Preincubation of cells with 1 mumol/l, 10 mumol/l and 100 mumol/l NG-monomethyl-L-arginine decreased cyclic GMP stimulation at 1 mumol/l vasopressin by 25%, 71% and 90%, respectively. This inhibition by NG-monomethyl-L-arginine was markedly reduced by L-arginine (2 mmol/l) but not D-arginine (2 mmol/l). Cyclic GMP stimulation by the calcium ionophore A23187 was also inhibited by NG-monomethyl-L-arginine and enantioselectively restored by L-arginine. However, NG-monomethyl-L-arginine did not affect cyclic GMP stimulation by sodium nitroprusside that spontaneously releases nitric oxide. These results suggest that, in kidney epithelial cells, vasopressin induces nitric oxide formation from L-arginine leading to activation of soluble guanylate cyclase. It is concluded that nitric oxide formation from L-arginine is not only responsible for endothelium-dependent relaxation but may be a more general pathway with regulatory function for intracellular guanylate cyclase activity.
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PMID:Cyclic GMP stimulation by vasopressin in LLC-PK1 kidney epithelial cells is L-arginine-dependent. 255 24

Treatment of intact adipocytes with either or both insulin and adrenaline stimulated membrane cyclic AMP phosphodiesterase activity only in the endoplasmic reticulum subfraction. The cyclic GMP-inhibited cyclic AMP phosphodiesterase activity was also found in this fraction. Quantitative Western blotting using a specific polyclonal antibody, raised against the homogeneous 'dense-vesicle' cyclic AMP phosphodiesterase from rat liver, identified a single 63 kDa species which was localized in the adipocyte endoplasmic reticulum fraction. The ability of adrenaline to stimulate adipocyte membrane cyclic AMP phosphodiesterase was shown to be mediated via beta-adrenoceptors and not alpha 1-adrenoceptors. Membrane cyclic AMP phosphodiesterase was stimulated by glucagon but not by vasopressin, A23187 or 12-O-tetradecanoylphorbol 13-acetate (TPA). Treatment of adipocytes with either chloroquine or dansyl cadaverine failed to affect the ability of insulin to stimulate cyclic AMP phosphodiesterase activity. Treatment of an isolated adipocyte endoplasmic reticulum membrane fraction with purified protein kinase A increased its cyclic AMP phosphodiesterase activity some 2-fold. When this fraction was treated with purified protein kinase A and [32P]ATP, label was incorporated into a 63 kDa protein which was specifically immunoprecipitated with the antiserum against the liver 'dense-vesicle' cyclic AMP phosphodiesterase.
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PMID:Subcellular localization and hormone sensitivity of adipocyte cyclic AMP phosphodiesterase. 255 12

The secretion of corticotropin by perfused rat anterior pituitary cell columns was studied. Forty-one residue corticotropin releasing factor, vasopressin and high extracellular KC1 all stimulated the secretion of corticotropin. The hormonal response to corticotropin-releasing factor (10(-10) mol/l), vasopressin (10(-9) mol/l) as well as KC1 (48 mmol/l) was reduced by membrane permeant analogs of cGMP, such as 8-BrcGMP and dibutyryl-cGMP. The 8-BrcGMP analog (10(-5) mol/l) inhibited corticotropin release in response to corticotropin-releasing factor by 30%, that to vasopressin by 70%, and that to KCl by 50%. Atriopeptin1-28 (10(-8) and 10(-7) mol/l), a peptide known to activate membrane-bound guanylate cyclase in the anterior pituitary gland, decreased the release of corticotropin induced by vasopressin to about 30% of control. Similarly, activators of soluble guanylate cyclase, such as glyceryltrinitrate and sodium nitroprusside (10(-5) mol/l) inhibited vasopressin-stimulated corticotropin release by 60%. In conclusion, the data show that purported activators of particulate and soluble guanylate cyclase, as well as derivatives of cGMP itself are strong inhibitors of secretagogue-induced corticotropin release by corticotroph cells of the anterior pituitary gland.
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PMID:Guanosine 3':5'cyclic monophosphate and activators of guanylate cyclase inhibit secretagogue-induced corticotropin release by rat anterior pituitary cells. 256 41

Rat thoracic aortic smooth-muscle cells (A-10; A.T.C.C. CRL 1476) displays a high density of vasopressin and atrial-natriuretic-factor (ANF) receptors and a low density of beta-adrenergic receptors. ANF stimulates cGMP (cyclic GMP) accumulation in a time- and dose-dependent fashion. Pretreatment of these cells with phorbol dibutyrate (PDBu), a known activator of protein kinase C, attenuated ANF-stimulated cGMP accumulation without affecting basal cGMP concentrations. This effect was concentration-dependent and was observed as early as 2 min after treatment. 4 alpha-Phorbol 12, 13-didecanoate (alpha PDD), which does not activate protein kinase C, did not inhibit the cGMP accumulation. PDBu pretreatment did not affect the density and affinity of ANF receptors. These data suggest that PDBu, presumably via activation of protein kinase C, might stimulate phosphorylation of a key regulatory protein in the ANF/cGMP pathway.
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PMID:An activator of protein kinase C (phorbol dibutyrate) attenuates atrial-natriuretic-factor-stimulated cyclic GMP accumulation in smooth-muscle cells. 282 9

Atrial natriuretic peptide (ANP) III stimulated the formation of intracellular cGMP in renal epithelial cells (LLC-PK1) dose dependently. Incubation of LLC-PK1 cells with [Arg8]vasopressin resulted in an increase in intracellular cAMP levels. The stimulatory effect of ANP III on the cyclic cGMP system was inhibited by coincubation with [Arg8]vasopressin in a dose-dependent manner.
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PMID:Modulation of atrial natriuretic peptide-induced cGMP accumulation by [Arg8]vasopressin in the cultured renal epithelial cell line, LLC-PK1. 283 11

Specific high-affinity binding sites (dissociation constant 100 pmol/l) for atrial natriuretic peptide (ANP) have been identified in the clone D384 derived from the human astrocytoma cell line G-CCM. Unrelated peptides such as angiotensin II, vasopressin and bradykinin did not compete for these sites. Of the atrial natriuretic peptides studied, both the human and rat ANP competed equally, while peptides with either C- or N-terminal residue missing or with no internal -S-S-bond either competed less effectively or did not compete at all. Human ANP stimulated the cells to increase their intracellular level of cyclic GMP in a time- and dose-dependent manner with maximum stimulation being approached but not reached at concentrations of 1 mumol/l. These results support both the notion that ANP has an important functional role within the brain and the concept of neurotransmitter/neuromodulator communication between neurones and glia.
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PMID:Specific binding of atrial natriuretic peptide increases cyclic GMP levels in human astrocytoma cells. 283 28

Atrial natriuretic factor (ANF) is actively involved in the control of blood pressure and fluid homeostasis as a physiological antagonist of the renin-angiotensin system. To evaluate a possible interaction between ANF and angiotensin II (Ang-II) receptors, we investigated the effect of long term pretreatment (18 h) of rat cultured vascular smooth muscle cells with Ang-II. Binding of 125I-labeled ANF and cyclic GMP production induced by ANF were measured. After preincubation of the cells with Ang-II (1, 10, and 100 nM), the number of ANF binding sites (Bmax) was decreased by 30, 59, and 71%, respectively, with a slight decrease of the Kd values. Sar1-Ile8-Ang-II (100 nM), a specific Ang-II receptor antagonist, totally inhibited the down-regulation induced by Ang-II (10 nM). Moreover, the regulatory effect of Ang-II on ANF receptors appeared more slowly as compared to ANF homologous receptor regulation. Ang-II pretreatment did not desensitize but increased cyclic GMP production elicited by ANF, implying that only the number of non-guanylate cyclase-coupled receptors was affected. These findings, which were not observed with 100 nM of epinephrine, norepinephrine, histamine, serotonin, and Arg-vasopressin, demonstrate a specific and functional link between ANF and Ang-II receptors. This study also shows that the regulation of ANF receptors is heterogeneous, providing new evidence of multiple classes of ANF receptors.
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PMID:Regulation of atrial natriuretic factor receptors by angiotensin II in rat vascular smooth muscle cells. 284 14

Vasopressin has been shown previously to lower the glucagon-induced increase of cyclic AMP levels in isolated rat hepatocytes by way of an enhanced phosphodiesterase (EC 3.1.4.17) activity. Five phosphodiesterase inhibitors were tested for their ability to prevent vasopressin from lowering cyclic AMP levels in intact hepatocytes and for their inhibitory effect in vitro on soluble and particulate phosphodiesterase activities partially purified from hepatocytes. Three soluble activities have been separated by DEAE-cellulose chromatography: a phosphodiesterase hydrolyzing both cyclic AMP and cyclic GMP, a form stimulated by cyclic GMP and a cyclic AMP-specific activity. The absence of any statistically significant correlation between the in vivo (in intact cells) and the in vitro (on isolated phosphodiesterases) potencies of the inhibitors does not support a role for the cytosolic phosphodiesterases in mediating the vasopressin-induced decrease in cyclic AMP levels. No statistically significant correlation was observed between the inhibition of the vasopressin effect on cyclic AMP accumulation and the inhibition of phosphodiesterase activity either associated with the native plasma membranes or solubilized from these membranes with 0.4 M NaCl. In contrast, a statistically significant correlation was observed between the degree of inhibition of the vasopressin effect in the intact cells and the degree of inhibition of the intrinsic phosphodiesterase still associated with the plasma membranes after high-salt treatment. These data indicate that a phosphodiesterase activity integral to the plasma membrane is very likely involved in the negative control of cyclic AMP levels by vasopressin.
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PMID:Involvement of a plasma membrane phosphodiesterase in the negative control of cyclic AMP levels by vasopressin in rat hepatocytes. 284 89


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