scholarly journals Response of cortical collecting ducts from remnant kidneys to arginine vasopressin

1992 ◽  
Vol 41 (5) ◽  
pp. 1150-1154 ◽  
Author(s):  
Melvin Bonilla-Felix ◽  
L. Lee Hamm ◽  
John Herndon ◽  
V. Matti Vehaskari
Keyword(s):  
Arginine Vasopressin ◽  
Collecting Ducts

Urea transport in MDCK cells that are stably transfected with UT-A1

2004 ◽  
Vol 286 (6) ◽  
pp. C1264-C1270 ◽  
Author(s):  
Otto Fröhlich ◽  
Janet D. Klein ◽  
Pauline M. Smith ◽  
Jeff M. Sands ◽  
Robert B. Gunn
Keyword(s):  
Epithelial Cell ◽  
Cell Line ◽  
Arginine Vasopressin ◽  
Cell Biology ◽  
Mdck Cells ◽  
Epithelial Cell Line ◽  
Urea Transport ◽  
Urea Transporter ◽  
Collecting Ducts ◽  
Single Clone

Progress in understanding the cell biology of urea transporter proteins has been hampered by the lack of an appropriate cell culture system. The goal of this study was to create a polarized epithelial cell line that stably expresses the largest of the rat renal urea transporter UT-A isoforms, UT-A1. The gene for UT-A1 was cloned into pcDNA5/FRT and transfected into Madin-Darby canine kidney (MDCK) cells with an integrated Flp recombination target site. The cells from a single clone were grown to confluence on collagen-coated membranes until the resistance was >1,500 Ω·cm2. Transepithelial [14C]urea fluxes were measured at 37°C in a HCO3−/CO2 buffer, pH 7.4, with 5 mM urea. The baseline fluxes were not different between unstimulated UT-A1-transfected MDCK cells and nontransfected or sham-transfected MDCK cells. However, only in the UT-A1-transfected cells was UT-A1 protein expressed (as measured by Western blot analysis) and urea transport stimulated by forskolin or arginine vasopressin. Forskolin and arginine vasopressin also increased the phosphorylation of UT-A1. Thionicotinamide, dimethylurea, and phloretin inhibited the forskolin-stimulated [14C]urea fluxes in the UT-A1-transfected MDCK cells. These characteristics mimic those seen in rat terminal inner medullary collecting ducts. This new polarized epithelial cell line stably expresses UT-A1 and reproduces several of the physiological responses observed in rat terminal inner medullary collecting ducts.

scholarly journals Apelin Counteracts Vasopressin-Induced Water Reabsorption via Cross Talk Between Apelin and Vasopressin Receptor Signaling Pathways in the Rat Collecting Duct

Endocrinology ◽  
2014 ◽  
Vol 155 (11) ◽  
pp. 4483-4493 ◽  
Author(s):  
Annette Hus-Citharel ◽  
Laurence Bodineau ◽  
Alain Frugière ◽  
Fanny Joubert ◽  
Nadine Bouby ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Cross Talk ◽  
Arginine Vasopressin ◽  
Blood Circulation ◽  
Direct Action ◽  
Collecting Duct ◽  
Urine Osmolality ◽  
Water Reabsorption ◽  
Collecting Ducts ◽  
Antagonist Effect

Abstract Apelin receptors (ApelinRs) are expressed along an increasing cortico-medullary gradient in collecting ducts (CDs). We showed here that iv injection of apelin 17 (K17F) in lactating rats characterized by increases in both synthesis and release of arginine vasopressin (AVP) increased diuresis concomitantly with a significant decrease in urine osmolality and no change in Na+ and K+ excretion. Under these conditions, we also observed a significant decrease in apical aquaporin-2 immunolabeling in CD, with a cortico-medullary gradient, suggesting that K17F-induced diuresis could be linked to a direct action of apelin on CD. We then examined the potential cross talk between V1a AVP receptor (V1a-R), V2 AVP receptor (V2-R) and ApelinR signaling pathways in outer medullary CD (OMCD) and inner medullary CD microdissected rat CD. In OMCD, expressing the 3 receptors, K17F inhibited cAMP production and Ca2+ influx induced by 1-desamino-8-D-arginine vasopressin a V2-R agonist. Similar effects were observed in inner medullary CD expressing only V2-R and ApelinR. In contrast, in OMCD, K17F increased by 51% the Ca2+ influx induced by the stimulation of V1a-R by AVP in the presence of the V2-R antagonist SR121463B, possibly enhancing the physiological antagonist effect of V1a-R on V2-R. Thus, the diuretic effect of apelin is not only due to a central effect by inhibiting AVP release in the blood circulation as previously shown but also to a direct action of apelin on CD, by counteracting the antidiuretic effect of AVP occurring via V2-R.

cAMP-dependent effects of vasopressin and calcitonin on cytosolic calcium in rat CCD

1994 ◽  
Vol 267 (3) ◽  
pp. F354-F365 ◽  
Author(s):  
E. Siga ◽  
A. Champigneulle ◽  
M. Imbert-Teboul
Keyword(s):  
Adenylate Cyclase ◽  
Arginine Vasopressin ◽  
Cytosolic Calcium ◽  
Camp Production ◽  
Fura 2 ◽  
Fluorescence Measurements ◽  
A Value ◽  
Intracellular Release ◽  
Collecting Ducts ◽  
Luminal Calcium

Fura 2 fluorescence measurements were carried out on microperfused rat cortical collecting ducts (CCD) to investigate the effect of adenosine 3',5'-cyclic monophosphate (cAMP) and adenylate cyclase-stimulating hormones on free cytosolic calcium ([Ca2+]i). Forskolin, 3-isobutyl-1-methylxanthine, and 8-(4-chlorophenylthio)-cAMP (CPT-cAMP) all triggered marked and sustained [Ca2+]i variations. Maximal increases elicited by 100 microM CPT-cAMP amounted to 101 +/- 11 nM (mean +/- SE, n = 18). This effect was mostly dependent on the presence of basolateral calcium and totally independent of luminal calcium. It remained unchanged in CCD perfused with sodium-free luminal fluid (82 +/- 10 nM, n = 5), pretreated with 1 mM bath ouabain (113 +/- 20, n = 4), or superfused with sodium-free bath in the presence of ouabain (82 +/- 22, n = 5). The V2 agonist 1-desamino-8-D-arginine vasopressin (DDAVP, 10 nM) increased [Ca2+]i by 57 +/- 5 nM (n = 27), a value 40% lower than that achieved with 10 nM AVP (141 +/- 7, n = 34) but similar to that observed with AVP + a V1a antagonist (57 +/- 6, n = 6). Significant effects could also be obtained with 200 pM DDAVP (31 +/- 6, n = 8) and arginine vasopressin (AVP) (72 +/- 6, n = 16). Rat calcitonin also raised [Ca2+]i by 43 +/- 10 (n = 8) and 66 +/- 8 nM (n = 17) at 1 and 10 nM, respectively, and its effect was not additive to that of CPT-cAMP. Calcitonin and DDAVP effects, like those of CPT-cAMP and forskolin, were nearly abolished in Ca(2+)-free bath, but AVP action on intracellular release persisted. These results show that, in rat CCD, cAMP effects on [Ca2+]i mainly result from basolateral calcium entry. In contrast to rabbit CCD the mechanism is independent on Na reabsorption and basolateral Na+/Ca2+ exchange. Calcitonin and DDAVP effects on [Ca2+]i are probably secondary to increased cAMP production.

COMPARATIVE EXPERIMENTS ON THE URINARY EXCRETION OF EXOGENOUS OXYTOCIN AND VASOPRESSIN

1973 ◽  
Vol 73 (4) ◽  
pp. 643-650 ◽  
Author(s):  
Svend Erik Jensen ◽  
Per Frandsen ◽  
Aage Theil Nielsen
Keyword(s):  
Steady State ◽  
Urinary Excretion ◽  
Continuous Infusion ◽  
Glomerular Filtration ◽  
Blood Level ◽  
Intravenous Injection ◽  
Arginine Vasopressin ◽  
Plasma Proteins ◽  
Renal Handling ◽  
Collecting Ducts

ABSTRACT The urinary excretion of oxytocin (milk-ejecting activity) and arginine vasopressin (antidiuretic activity) in water-loaded rabbits was measured following simultaneous intravenous injection of 1–9 IU of oxytocin and 0.1–0.3 IU of vasopressin per animal. The percentage excretion of vasopressin was 2–10 times that of oxytocin. Experiments with a steady state blood level of vasopressin and oxytocin maintained by continuous infusion showed, that the vasopressin/oxytocin ratio increased 2–6 times, when the hormones passed from the blood into the urine. This indicates a difference in the renal handling of the hormones with regard to the mechanism of the urinary excretion. The urinary clearance of vasopressin was about the same as that of inulin, consistent with the hypothesis, that vasopressin is excreted mainly by glomerular filtration. The clearance of oxytocin was lower than that of vasopressin and inulin, indicating that oxytocin is filtered at a lower rate (binding to plasma proteins) or partly re-absorbed or inactivated in the tubules and/or collecting ducts.

Vasopressin regulation of inner medullary collecting ducts and compensatory changes in mice lacking adenosine A1 receptors

2008 ◽  
Vol 294 (3) ◽  
pp. F638-F644 ◽  
Author(s):  
Timo Rieg ◽  
Kanishka Pothula ◽  
Jana Schroth ◽  
Joseph Satriano ◽  
Hartmut Osswald ◽  
...  
Keyword(s):  
Arginine Vasopressin ◽  
Free Water ◽  
Urinary Flow ◽  
Free Water Clearance ◽  
Water Excretion ◽  
Water Loading ◽  
Collecting Ducts ◽  
Camp Formation

Activation of adenosine A1 receptors (A1R) can inhibit arginine vasopressin (AVP)-induced cAMP formation in isolated cortical and medullary collecting ducts. To assess the in vivo consequences of the absence of A1R, we performed experiments in mice lacking A1R (A1R−/−). We assessed the effects of the vasopressin V2 receptor (V2R) agonist 1-desamino-8-d-arginine vasopressin (dDAVP) on cAMP formation in isolated inner medullary collecting ducts (IMCD) and on water excretion in conscious water-loaded mice. dDAVP-induced cAMP formation in isolated IMCD was significantly greater (∼2-fold) in A1R−/− compared with wild-type mice (WT) and, in contrast to WT, was not inhibited by the A1R agonist N6-cyclohexyladenosine. A1R−/− and WT had similar basal urinary excretion of vasopressin, expression of aquaporin-2 protein in renal cortex and medulla, and acute increases in urinary flow rate and electrolyte-free water clearance in response to the V2R antagonist SR121463 or acute water loading; the latter increased inner medullary A1R expression in WT. Dose dependence of dDAVP-induced antidiuresis after acute water loading was not different between the genotypes. However, A1R−/− had greater inner medullary expression of cyclooxygenase-1 under basal conditions and of the P2Y2 and EP3 receptor in response to water loading compared with WT mice. Thus vasopressin-induced cAMP formation is enhanced in isolated IMCD of mice lacking A1R, but the adenosine-A1R/V2R interaction demonstrated in vitro is likely compensated in vivo by multiple mechanisms, a number of which can be “uncovered” by water loading.

scholarly journals Combo effect of hypomagnesemia and hypokalaemia inducing nephrogenic diabetes insipidus in a patient with type 1 diabetes mellitus

2021 ◽  
Author(s):  
Esmail Sangey ◽  
Kishan Chudasama ◽  
Ahmad Mwinyi
Keyword(s):  
Diabetes Mellitus ◽  
Type 1 Diabetes ◽  
Diabetes Insipidus ◽  
Type 1 Diabetes Mellitus ◽  
Arginine Vasopressin ◽  
Nephrogenic Diabetes Insipidus ◽  
Water Channels ◽  
Aquaporin 2 ◽  
Collecting Ducts

NDI is rarely considered versus diabetes mellitus in the situation of polyuria. It is well known that hypokalaemia and hypercalcemia induce NDI through decreased activity of arginine vasopressin and downregulation of Aquaporin-2 water channels in the collecting ducts. However, not much is known whether hypomagnesemia can directly induce NDI.

Pharmacological characterization of V1a vasopressin receptors in the rat cortical collecting duct

1992 ◽  
Vol 262 (4) ◽  
pp. F546-F553 ◽  
Author(s):  
A. Ammar ◽  
S. Roseau ◽  
D. Butlen
Keyword(s):  
Arginine Vasopressin ◽  
Rank Order ◽  
Collecting Duct ◽  
Free Ligand ◽  
Arginine Vasotocin ◽  
Cortical Collecting Duct ◽  
Pharmacological Characterization ◽  
Collecting Ducts ◽  
Vasopressin Receptors ◽  
V2 Vasopressin Receptors

Vasopressin receptors in distal segments of the rat nephron were identified in isolated tubules using two labeled ligands: the [1-(beta-mercapto-beta,beta-cyclopentamethylenepropionic acid), 2-(O-methyl)tyrosine,4-threonine,8-ornithine,9-125I-tyrosylamide]- vasotocin [125I-d(CH2)5[Tyr(Me)2,Thr4,Tyr-NH2(9)]OVT] and the linear analogue, Phaa1,D-Tyr(Me)2,Phe3,Gln4,Asn5,Arg6, Pro7,Arg8,125I-Tyr-NH2(9) [125I-Tyr-NH2(9)-linear antagonist (LA)-V1a)]. Specific 125I-d(CH2)5[Tyr(Me)2,Thr4,Tyr-NH2(9)]-OVT binding to cortical collecting ducts (CCD) was saturable with incubation time and dose, reversible after elimination of free ligand, and characterized by the following rank order for recognition of vasopressin analogues: desGly9-d-(CH2)5-[Tyr(Et)2,Val4]arginine vasopressin (AVP) greater than or equal to d(CH2)5[Tyr-(ET)2,Val4]AVP greater than or equal to AVP greater than or equal to d(CH2)5[Tyr(Me)2]AVP = 1-desamino-8-D-arginine vasopressin (DDAVP) greater than or equal to Tyr-NH2(9)-LA-V1a greater than [8-arginine]vasotocin (AVT) greater than d(CH2)5[Tyr(Me)2, Thr4,Tyr-NH2(9)]OVT greater than oxytocin (OT) greater than [Phe2,Orn8]VT much greater than [Thr4,Gly7]-OT. Scatchard plots of dose-dependent 125I-Tyr-NH2(9)-LA-V1a binding to medullary thick ascending limbs (MTAL), CCD, and outer medullary collecting ducts (OMCD) revealed the presence of high- and low-affinity binding sites corresponding to V1a and V2 vasopressin receptors, respectively; the densities of V1a receptors are approximately 20% of the total number of vasopressin receptors in CCD and 5% in MTAL and OMCD.

cAMP mediates the increase in apical membrane Na+ conductance produced in rat CCD by vasopressin

1990 ◽  
Vol 259 (5) ◽  
pp. F823-F831 ◽  
Author(s):  
J. A. Schafer ◽  
S. L. Troutman
Keyword(s):  
Arginine Vasopressin ◽  
Apical Membrane ◽  
Basolateral Membrane ◽  
Transepithelial Resistance ◽  
Bathing Solution ◽  
Dibutyryl Camp ◽  
Cyclic Monophosphate ◽  
Collecting Ducts ◽  
Transepithelial Voltage ◽  
Stimulation Of

Experiments were conducted to determine if adenosine 3',5'-cyclic monophosphate (cAMP) mediates the stimulation of Na+ absorption by arginine vasopressin (AVP) in isolated perfused cortical collecting ducts (CCD) from rats treated with deoxycorticosterone pivalate (5 mg im) 5-9 days before study. AVP (220 pM) in the bathing solution hyperpolarized the transepithelial voltage (PDT) from -4.0 +/- 0.8 (SE) to -15.1 +/- 1.4 mV (n = 9, P less than 0.001) and decreased the transepithelial resistance (RT) from 40 +/- 8 to 33 +/- 6 omega.cm2 (n = 5, P less than 0.025). Bath addition of 0.2 mM dibutyryl cAMP (DBcAMP), 0.1 mM isobutylmethylxanthine (IBMX), 0.1 mM DBcAMP plus 0.1 mM IBMX, and 10 or 50 microM forskolin produced the same effects, reversibly hyperpolarizing PDT by 7.0-11.5 mV and decreasing RT by 6-12 omega.cm2. Addition of 10 microM amiloride to the luminal perfusate reduced PDT from -0.9 to +2.0 mV and increased RT in the presence or absence of any of the test agents. Addition of DBcAMP + IBMX or 50 microM forskolin to the bathing solution also reversibly depolarized the basolateral membrane voltage of principal cells by 1-2 mV and decreased the apical membrane fractional resistance from 0.82-0.84 to 0.72-0.77. Both effects were reversed by addition of amiloride to the luminal perfusate. These results demonstrate that cAMP is the intracellular mediator of the increase in apical membrane Na+ conductance produced by AVP in the rat CCD.

N-ethylmaleimide causes aquaporin-2 trafficking in the renal inner medullary collecting duct by direct activation of protein kinase A

2005 ◽  
Vol 288 (4) ◽  
pp. F832-F839 ◽  
Author(s):  
Stephen Shaw ◽  
David Marples
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Arginine Vasopressin ◽  
Water Permeability ◽  
Collecting Duct ◽  
Direct Activation ◽  
Aquaporin 2 ◽  
Collecting Ducts ◽  
Kinase A

The antidiuretic hormone arginine vasopressin increases the osmotic water permeability of the renal collecting ducts by inducing the shuttling of aquaporin-2 (AQP2) water channels from intracellular vesicles to the apical plasma membrane of the principal cells. This process has been demonstrated to be dependent on the cytoskeleton and protein kinase A (PKA). Previous studies in the toad urinary bladder, a functional homologue of the renal collecting duct, have demonstrated that the sulfhydryl reagent N-ethylmaleimide (NEM) is also able to activate the vasopressin-sensitive water permeability pathway in this tissue. The aim of the present study was to investigate the effects of NEM on AQP2 trafficking in a mammalian system. We show that NEM causes translocation of AQP2 from the cytosol to the plasma membrane in rat inner medullary collecting ducts; like the response to arginine vasopressin, this action was also dependent on an intact cytoskeleton and PKA. This effect is not mediated by cAMP but results from direct activation of PKA by NEM.

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