Current understanding of the cellular biology and molecular structure of the antidiuretic hormone-stimulated water transport pathway.

Harris, H. W.; Strange, Kevin; Zeidel, Mark L.

doi:10.1172/jci115263

Cited by 112 publications

(63 citation statements)

References 44 publications

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“…It is tempting to speculate that such ac tivation might involve stimulated fusion of vesicles con taining membrane-bounci Ca2* influx channels with the plasma membrane. A similar mechanism has been pro posed for the stimulatory effects of AVP on transepithelial Na* and water transport [9,17,25,30]. Surprisingly, dDAVP transiently increased when added in the complete absence of external Ca2*.…”

Section: Discussionsupporting

confidence: 57%

Vasopressin-stimulated Ca 2+ reabsorption in rabbit cortical collecting system: effects on cAMP and cytosolic Ca 2+

Baal

Raber

Slegte

et al. 1996

Pfl�gers Archiv European Journal of Physiology

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The effect of arginine vasopressin (AVP) on transepithelial Ca2+ transport in primary cultures of rabbit cortical collecting system cells was examined. Addition of AVP to the basolateral side of the monolayer dose-dependently (ECM ) = 0.7 nM) increased active Ca2+ reab sorption from a basal value of 85 ± 2 nm oM r'-cnr2 to a maximum value of 124 ± 3 nniol-lr^cnr2. This was par alleled by a dose-dependent (ECi0 =1.1 nM ) increase in cellular adenosine ¿'^'-cyclic monophosphate (cAMP) content. Both effects of AVP were mimicked by the V 2 agonist deamino-Cys,D-Arg8-vasopressin (dDAVP) and forskolin. Addition of either AVP or dDAVP to the baso lateral side evoked a sustained increase in cytosolic free Ca2+ concentration, which resulted from both Ca2* entry and release from internal stores. Only the effect on Ca2+ entry was mimicked by forskolin, demonstrating that cAMP acts by activating a Ca2* influx pathway. The pres ent findings demonstrate that AVP stimulates transeellular Ca2'1 * transport in the cortical collecting system through activation of basolateral V 2 receptors coupled to adenylyl cyclase to increase the cellular cAM P content.

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Section: Discussionsupporting

confidence: 57%

Vasopressin-stimulated Ca 2+ reabsorption in rabbit cortical collecting system: effects on cAMP and cytosolic Ca 2+

Baal

Raber

Slegte

et al. 1996

Pfl�gers Archiv European Journal of Physiology

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“…These two functions are hormonally controlled by the antidiuretic hormone (ADH) and the mineralocorticosteroid aldosterone. The permeability of the apical membrane of the granular cell to water is very low, unless this cell has been stimulated by ADH (DiBona et al, 1969;Harris et al, 1991). This low permeability has been related to the presence of only a few particles on the P face of the apical membrane (Bourguet et al, 1976), which in turn may reflect an unusual composition H. Bartels and I. C. Potter 3454 or arrangement of lipids in the exoplasmic half of this membrane (Harris et al, 1991).…”

Section: The Pavement Cellmentioning

confidence: 99%

“…The permeability of the apical membrane of the granular cell to water is very low, unless this cell has been stimulated by ADH (DiBona et al, 1969;Harris et al, 1991). This low permeability has been related to the presence of only a few particles on the P face of the apical membrane (Bourguet et al, 1976), which in turn may reflect an unusual composition H. Bartels and I. C. Potter 3454 or arrangement of lipids in the exoplasmic half of this membrane (Harris et al, 1991). Since this unusual and highly specialised membrane structure is shared by the pavement cell in the lamprey gill epithelium, the apical membrane of the latter cell is likewise assumed to be relatively impermeable to water.…”

Section: The Pavement Cellmentioning

confidence: 99%

Cellular composition and ultrastructure of the gill epithelium of larval and adult lampreys

Bartels

Potter

2004

Journal of Experimental Biology

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SUMMARY Lampreys, one of the only two surviving groups of agnathan (jawless)vertebrates, contain several anadromous species that, during their life cycle,thus migrate from fresh to seawater and back to freshwater. Lampreys have independently evolved the same overall osmoregulatory mechanisms as the gnathostomatous (jawed) and distantly related teleost fishes. Lamprey gills thus likewise play a central role in taking up and secreting monovalent ions. However, the ultrastructural characteristics and distribution of their epithelial cell types [ammocoete mitochondria-rich (MR) cell, intercalated MR cell, chloride cell and pavement cell] differ in several respects from those of teleosts. The ultrastructural characteristics of these cells are distinctive and closely resemble those of certain ion-transporting epithelia in other vertebrates, for which the function has been determined. The data on each cell type, together with the stage in the life cycle at which it is found, i.e. whether in fresh or seawater, enable the following proposals to be made regarding the ways in which lampreys use their gill epithelial cells for osmoregulating in hypo- and hypertonic environments. In freshwater, the intercalated MR cell takes up Cl– and secretes H+,thereby facilitating the uptake of Na+ through pavement cells. In seawater, the chloride cell uses a secondarily active transcellular transport of Cl– to provide the driving force for the passive movement of Na+ through leaky paracellular pathways between these cells.

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“…CHIP28 exists in membranes of erythrocytes and renal tubules and therefore may be related to the protein channels through which facilitated permeability of water occurs (31,32). IfCHIP28 is a water channel, it is logical to speculate that it may be clinically important in settings such as erythrocyte dehydration in sickle cell disease and in the perturbations of water and electrolyte balance found in various renal diseases.…”

mentioning

confidence: 99%

Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.

Preston

Agre

1991

Proc. Natl. Acad. Sci. U.S.A.

728

407

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CHIP28 is a 28-kDa integral membrane protein with similarities to membrane chanch and Is found in erythrocytes and renal tubules. A cDNA for CHIP28 was isolated from human fetal liver cDNA template by a the-step polymerase chain reaction (PCR) Analysis of the deduced amino acid sequence sugss that CHEIP28 protein contains six bilayer-sannin domains, two exofacial potential N-glycosylation sites, and intraceflular N and C termini. Search of the DNA sequence data bas revealed a strong homology with the major intrinsic protein of bovine lens, which is the prototype of an ancient but recently recognized family of membrane channels. These proteins are believed to form channels permeable to water and possibly other small molecules. CHIP28 shares homology with all known members of this channel family, and it is speculated that CHIP28 has a similar function.The erythrocyte membrane has proven to be an accessible source of new proteins with structural or metabolic functions and a useful model with general relevance to plasma membranes (for reviews, see refs. 1 and 2). During isolation of the 32-kDa Rh polypeptides from human erythrocytes, a 28-kDa integral membrane protein copurified and was considered a breakdown product (3, 4). The 28-kDa protein was later shown to be a unique molecule that is abundant in erythrocytes and renal tubules, and a subpopulation is N-glycosy-The function of the 28-kDa protein is not yet known, but several observations suggest that it is a membrane channel. The 28-kDa protein behaves as a tetramer when solubilized in Triton X-100, and the N-terminal amino acid sequence of the purified 28-kDa protein (6) is related to that of MIP26, the 26-kDa major intrinsic protein of bovine lens fiber cells (7). When reconstituted into planar lipid bilayers, MIP26 forms tetrameric channels with voltage-regulated conductance (8,9), and MIP26 appears to function as a channel through which lens fiber cells absorb interstitial fluid (8). MMP26 is the prototype of a family of membrane proteins recently identified in diverse species (10). This report describes isolation of the cDNA* for the 28-kDa protein, which has homology with all known members of the MIP channel family and is referred to as

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Current understanding of the cellular biology and molecular structure of the antidiuretic hormone-stimulated water transport pathway.

Cited by 112 publications

References 44 publications

Vasopressin-stimulated Ca 2+ reabsorption in rabbit cortical collecting system: effects on cAMP and cytosolic Ca 2+

Vasopressin-stimulated Ca 2+ reabsorption in rabbit cortical collecting system: effects on cAMP and cytosolic Ca 2+

Cellular composition and ultrastructure of the gill epithelium of larval and adult lampreys

Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.

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