Actin filaments and vasopressin-stimulated water flow in toad urinary bladder

Pearl, M.; Taylor, Ann

doi:10.1152/ajpcell.1983.245.1.c28

Cited by 47 publications

(20 citation statements)

References 39 publications

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“…Previous studies using toad bladders have demonstrated the involvement of the F-actin cytoskeleton in AVP-mediated increases in osmotic water permeability (13,14). In addition, the reorganization of the F-actin cytoskeleton by AVP is a consistent finding in both amphibian urinary bladder epithelia and mammalian renal principal cells (2,16).…”

Section: Discussionmentioning

confidence: 74%

“…Microtubule-disrupting drugs like colchicine and nocodazole inhibit AVP-mediated increases in osmotic water permeability in renal collecting ducts by 65 and 72%, respectively (10 -13). Disruption of the F-actin cytoskeleton by cytochalasin B or dihydrocytochalasin B inhibits the AVP-induced increase in osmotic water permeability in toad bladder epithelium by 25-50% (13,14). The F-actin cytoskeleton also undergoes rearrangements after stimulation of cells with cAMP-elevating agents.…”

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confidence: 99%

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An Inhibitory Role of Rho in the Vasopressin-mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells

Klussmann

Tamma

Lorenz

et al. 2001

Journal of Biological Chemistry

152

160

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Vasopressin regulates water reabsorption in renal collecting duct principal cells by a cAMP-dependent translocation of the water channel aquaporin-2 (AQP2) from intracellular vesicles into the cell membrane. In the present work primary cultured inner medullary collecting duct cells were used to study the role of the proteins of the Rho family in the translocation of AQP2. Clostridium difficile toxin B, which inhibits all members of the Rho family, Clostridium limosum C3 toxin, which inactivates only Rho, and the Rho kinase inhibitor, Y-27632, induced both depolymerization of actin stress fibers and AQP2 translocation in the absence of vasopressin. The data suggest an inhibitory role of Rho in this process, whereby constitutive membrane localization is prevented in resting cells. Expression of constitutively active RhoA induced formation of actin stress fibers and abolished AQP2 translocation in response to elevation of intracellular cAMP, confirming the inhibitory role of Rho. Cytochalasin D induced both depolymerization of the F-actin cytoskeleton and AQP2 translocation, indicating that depolymerization of F-actin is sufficient to induce AQP2 translocation. Thus Rho is likely to control the intracellular localization of AQP2 via regulation of the F-actin cytoskeleton.The antidiuretic hormone arginine-vasopressin (AVP) 1 regulates water reabsorption in renal collecting duct principal cells by inducing the translocation of the water channel aquaporin-2 (AQP2) from intracellular vesicles primarily into the apical cell membrane (shuttle hypothesis; Refs. 1 and 2). The molecular targets of AVP on the surface of principal cells are heptahelical vasopressin V2 receptors coupled to the G s /adenylyl cyclase system. Activation of this system by the hormone raises the level of intracellular cAMP and results in the activation of protein kinase A (PKA) which then phosphorylates its substrates, one of which is AQP2.The phosphorylation of AQP2 by PKA and also the anchoring of PKA to subcellular compartments via protein kinase A anchoring proteins are prerequisites for AQP2 translocation to the cell membrane (2-5). In addition, the involvement of a heterotrimeric G protein of the G i family in the AQP2 translocation has been demonstrated in CD8 cells (6).The cytoskeleton consists of various components, including microtubules and F-actin, both of which are involved in AVPmediated changes of osmotic water permeability (2, 7-9). Microtubule-disrupting drugs like colchicine and nocodazole inhibit AVP-mediated increases in osmotic water permeability in renal collecting ducts by 65 and 72%, respectively (10 -13). Disruption of the F-actin cytoskeleton by cytochalasin B or dihydrocytochalasin B inhibits the AVP-induced increase in osmotic water permeability in toad bladder epithelium by 25-50% (13, 14). The F-actin cytoskeleton also undergoes rearrangements after stimulation of cells with cAMP-elevating agents. After stimulation with vasopressin, total F-actin decreases in toad bladders by 20 -30% (15) and apical F-actin in rat coll...

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Section: Discussionmentioning

confidence: 74%

mentioning

confidence: 99%

An Inhibitory Role of Rho in the Vasopressin-mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells

Klussmann

Tamma

Lorenz

et al. 2001

Journal of Biological Chemistry

152

160

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“…Alternatively, vesicles containing ENaC could be trafficked or held in place by the cortical actin cytoskeleton. In the toad urinary bladder, the cortical actin cytoskeleton forms a meshwork of short filaments just under the apical surface when observed with an electron microscope (40); this is probably true for cortical collecting duct cells in the mammalian kidney. This would in turn lend support to previously reported observations that demonstrated that short actin filaments had an effect on ENaC by increasing the channel's open probability and decreasing its conductance (4,6).…”

Section: Discussionmentioning

confidence: 95%

The Carboxyl Terminus of the α-Subunit of the Amiloride-sensitive Epithelial Sodium Channel Binds to F-actin

Mazzochi

Bubien

Smith

et al. 2006

Journal of Biological Chemistry

102

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The activity of the amiloride-sensitive epithelial sodium channel (ENaC) is modulated by F-actin. However, it is unknown if there is a direct interaction between ␣-ENaC and actin. We have investigated the hypothesis that the actin cytoskeleton directly binds to the carboxyl terminus of ␣-ENaC using a combination of confocal microscopy, co-immunoprecipitation, and protein binding studies. Confocal microscopy of Madin-Darby canine kidney cell monolayers stably transfected with wild type, rat isoforms of ␣-, ␤-, and ␥-ENaC revealed co-localization of ␣-ENaC with the cortical F-actin cytoskeleton both at the apical membrane and within the subapical cytoplasm. F-actin was found to co-immunoprecipitate with ␣-ENaC from whole cell lysates of this cell line. Gel overlay assays demonstrated that F-actin specifically binds to the carboxyl terminus of ␣-ENaC. A direct interaction between F-actin and the COOH terminus of ␣-ENaC was further corroborated by F-actin co-sedimentation studies. This is the first study to report a direct and specific biochemical interaction between F-actin and ENaC.The amiloride-sensitive epithelial sodium channel (ENaC) 2 is a member of the degenerin/epithelial sodium channel superfamily of ion channels. ENaC is expressed at the apical surface of polarized epithelia and is in part responsible for maintaining proper salt and water homeostasis in the body. A great deal of information is known about the biophysical properties of ENaC once it is inserted into the apical surface of an epithelial cell plasma membrane. However, less is known about the proteins that interact with ENaC. Data from the literature indicate an interaction between ENaC and components of the apical membrane cytoskeleton. A partially purified ENaC complex from bovine renal epithelia copurifies with ankyrin, spectrin, and actin (1), suggesting that these cytoskeletal proteins may be associated with ENaC. In addition, ␣-rENaC has been shown to bind to ␣-spectrin, and this is mediated through direct interaction between the ␣-spectrin Src homology 3 domain and the second proline-rich region in the COOH terminus of ␣-rENaC (2). Electrophysiological data provide further support for an interaction between ENaC and the actin-based cytoskeleton. In cellattached patches of A6 renal epithelial cells treated with the actin filament disrupter cytochalasin D, an induction of ENaC activity was observed (3), thereby suggesting that changes in the actin cytoskeleton affect the activity of ENaC. ENaC activation was also observed when short F-actin filaments were added to excised patches, and this effect was increased with the addition of cytochalasin D and/or ATP. These effects were reversed by the addition of the G-actin binding protein, DNase I. In planar lipid bilayers, short F-actin filaments were demonstrated to increase the open probability of rENaC (4), whereas application of DNase I prevented the activation of rENaC. The application of gelsolin, a Ca 2ϩ -activated protein that severs actin filaments and caps the plus end of the actin fi...

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“…In the case ofglucose transport, microfilament disruption with cytochalasin B resulted in impaired glucose transporter trafficking and diminished glucose uptake (50-53). Toad bladder studies have revealed that water transport is dependent upon water channel movement through the cytoskeleton, since water transport was inhibited after disruption of either microfilaments (54)(55)(56)(57) or microtubules (54,55,57). Although endocytosis through cytoskeletal domains appears to be required for a number of AP functions, there is little information about the role of the cytoskeleton in receptor-mediated signal transduction.…”

Section: Discussionmentioning

confidence: 99%

Cytoskeleton-dependent endocytosis is required for apical type 1 angiotensin II receptor-mediated phospholipase C activation in cultured rat proximal tubule cells.

Schelling

Hanson²,

Marzec³

et al. 1992

J. Clin. Invest.

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Renal proximal tubule sodium reabsorption is enhanced by apical or basolateral angiotensin II (All). Although All activates phospholipase C (PLC) in other tissues, All coupling to PLC on either apical or basolateral surfaces of proximal tubule cells is unclear. To determine if All causes PLC activation, and the differences between apical and basolateral All receptor function, receptors were unilaterally activated in rat proximal tubule cells cultured on permeable, collagen-coated supports. Apical All incubation resulted in concentration-and time-dependent inositol trisphosphate (IP3) formation. Basolateral All caused greater IP3 responses. Apical AII-induced IP3 generation was inhibited by DuP 753, suggesting that the type 1 All receptor subtype mediated proximal tubule PLC activation. Apical All signaling did not result from paracellular ligand leak to basolateral receptors since AII-induced PLC activation occurred when basolateral All receptors were occupied by SarLeu All or DuP 753. Inhibition of endocytosis with phenylarsine oxide prevented apical (but not basolateral) AII-induced IP3 formation. Cytoskeletal disruption with colchicine or cytochalasin D also prevented apical All-induced IP3 generation. These results demonstrate that in cultured rat proximal tubule cells, All is coupled to PLC via type 1 All receptors and cytoskeleton-dependent endocytosis is required for apical (but not basolateral) All receptor-mediated PLC activation. (J. Clin. Invest. 1992.90:2472-2480

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Actin filaments and vasopressin-stimulated water flow in toad urinary bladder

Cited by 47 publications

References 39 publications

An Inhibitory Role of Rho in the Vasopressin-mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells

An Inhibitory Role of Rho in the Vasopressin-mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells

The Carboxyl Terminus of the α-Subunit of the Amiloride-sensitive Epithelial Sodium Channel Binds to F-actin

Cytoskeleton-dependent endocytosis is required for apical type 1 angiotensin II receptor-mediated phospholipase C activation in cultured rat proximal tubule cells.

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