Stimulation of Aquaporin-Mediated Fluid Transport by Cyclic GMP in Human Retinal Pigment Epithelium In Vitro

Baetz, Nicholas W.; Stamer, W. Daniel; Yool, Andrea J.

doi:10.1167/iovs.11-8471

Cited by 14 publications

(11 citation statements)

References 45 publications

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“…Previous studies have shown that ANP and cGMP alone can stimulate the pumping activity of the RPE and increase the rate of reabsorption of subretinal fluid (Marmor and Negi, 1986;Baetz et al, 2012). These data provide evidence that the activation of the cGMP-PKG pathway is important for maintaining the functional integrity of the RPE and removal of fluid from the subretinal environment.…”

Section: Discussionsupporting

confidence: 61%

C-Type Natriuretic Peptide Protects the Retinal Pigment Epithelium against Advanced Glycation End Product–Induced Barrier Dysfunction

Dahrouj

Alsarraf

Liu

et al. 2013

The Journal of Pharmacology and Experimental Therapeutics

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In diabetic retinopathy, vision loss is usually secondary to macular edema, which is thought to depend on the functional integrity of the blood-retina barrier. The levels of advanced glycation end products in the vitreous correlate with the progression of diabetic retinopathy. Natriuretic peptides (NP) are expressed in the eye and their receptors are present in the retinal pigment epithelium (RPE). Here, we investigated the effect of glycated-albumin (Glyc-alb), an advanced glycation end product model, on RPE-barrier function and the ability of NP to suppress this response. Transepithelial electrical resistance (TEER) measurements were used to assess the barrier function of ARPE-19 and human fetal RPE (hfRPE) monolayers. The monolayers were treated with 0

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Section: Discussionsupporting

confidence: 61%

C-Type Natriuretic Peptide Protects the Retinal Pigment Epithelium against Advanced Glycation End Product–Induced Barrier Dysfunction

Dahrouj

Alsarraf

Liu

et al. 2013

The Journal of Pharmacology and Experimental Therapeutics

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“…35,36 Other data have indicated a stimulatory role of cGMP on AQP1-dependent water transport in the eye. 37 Our findings suggest that the signaling molecules cAMP and cGMP promote trafficking of AQP1 into the BBM of proximal tubular cells, and among the stimulated groups, no significant differences between the effects of the two nucleotides were evident. Because highly divergent findings of cAMP-and cGMPtriggered pathways have been reported with respect to other proximal tubular membrane proteins, such as NHE3, which among other characteristics, revealed a dose-dependent biphasic (i.e., partly inhibited and partly stimulated) response on protein kinase A activation, 38 it is currently impossible to adequately assign our data to the detail of defined signaling cascades stimulating AQP1, and more work needs to be done in this respect.…”

Section: Discussionmentioning

confidence: 52%

Short-Term Functional Adaptation of Aquaporin-1 Surface Expression in the Proximal Tubule, a Component of Glomerulotubular Balance

Pohl

Shan

Petsch

et al. 2015

Journal of the American Society of Nephrology

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Transepithelial water flow across the renal proximal tubule is mediated predominantly by aquaporin-1 (AQP1). Along this nephron segment, luminal delivery and transepithelial reabsorption are directly coupled, a phenomenon called glomerulotubular balance. We hypothesized that the surface expression of AQP1 is regulated by fluid shear stress, contributing to this effect. Consistent with this finding, we found that the abundance of AQP1 in brush border apical and basolateral membranes was augmented .2-fold by increasing luminal perfusion rates in isolated, microperfused proximal tubules for 15 minutes. Mouse kidneys with diminished endocytosis caused by a conditional deletion of megalin or the chloride channel ClC-5 had constitutively enhanced AQP1 abundance in the proximal tubule brush border membrane. In AQP1-transfected, cultured proximal tubule cells, fluid shear stress or the addition of cyclic nucleotides enhanced AQP1 surface expression and concomitantly diminished its ubiquitination. These effects were also associated with an elevated osmotic water permeability. In sum, we have shown that luminal surface expression of AQP1 in the proximal tubule brush border membrane is regulated in response to flow. Cellular trafficking, endocytosis, an intact endosomal compartment, and controlled protein stability are the likely prerequisites for AQP1 activation by enhanced tubular fluid shear stress, serving to maintain glomerulotubular balance.

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“…The contribution of AQP1 to this inhibition was not confirmed directly, although Cd 2+ , which was shown to inhibit cGMP-induced cation conduction of AQP1, reversed the inhibition of fluid transport [150]. ANP and a cGMP analogue were also shown to upregulate apical-tobasal fluid transport in cultured retinal pigment epithelial cells, but this was reversed by an inhibitor of AQP1 water permeability [151].…”

Section: Ion Permeability Of Aqps: An Unresolved Controversymentioning

confidence: 95%

Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

Kitchen

Day

Salman

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

131

115

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BACKGROUND: Aquaporin (AQP) water channels are best known as passive transporters of water that are vital for water homeostasis. SCOPE OF REVIEW:AQP knockout studies in whole animals and cultured cells, along with naturally occurring human mutations suggest that the transport of neutral solutes through AQPs has important physiological roles. Emerging biophysical evidence suggests that AQPs may also facilitate gas (CO2) and cation transport. AQPs may be involved in cell signalling for volume regulation and controlling the subcellular localization of other proteins by forming macromolecular complexes. This review examines the evidence for these diverse functions of AQPs as well their physiological relevance. MAJOR CONCLUSIONS:As well as being crucial for water homeostasis, AQPs are involved in physiologically important transport of molecules other than water, regulation of surface expression of other membrane proteins, cell adhesion, and signalling in cell volume regulation. GENERAL SIGNIFICANCE:Elucidating the full range of functional roles of AQPs beyond the passive conduction of water will improve our understanding of mammalian physiology in health and disease. The functional variety of AQPs makes them an exciting drug target and could provide routes to a range of novel therapies.3

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Stimulation of Aquaporin-Mediated Fluid Transport by Cyclic GMP in Human Retinal Pigment Epithelium In Vitro

Cited by 14 publications

References 45 publications

C-Type Natriuretic Peptide Protects the Retinal Pigment Epithelium against Advanced Glycation End Product–Induced Barrier Dysfunction

C-Type Natriuretic Peptide Protects the Retinal Pigment Epithelium against Advanced Glycation End Product–Induced Barrier Dysfunction

Short-Term Functional Adaptation of Aquaporin-1 Surface Expression in the Proximal Tubule, a Component of Glomerulotubular Balance

Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

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