Structural-functional relationships along the distal nephron

Madsen, Kirsten; Tisher, C. Craig

doi:10.1152/ajprenal.1986.250.1.f1

Cited by 142 publications

(70 citation statements)

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“…collecting duct which contains two cell types (15,22). The results establish a cell-specific and Ca 2ϩ -dependent inhibition on either the AVP-or the glucagon-dependent cAMP content.…”

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confidence: 56%

“…It is striking to note that all the structures that expressed more than one AC type (i.e. glomerulus, CCD, OMCD) are known to contain several cell types (15,22). In several segments, types IV and V AC mRNAs were not or barely detectable (Ͻ100 molecules per mm, Table II).…”

Section: Ca 2ϩ -Inhibitable Adenylyl Cyclases Along the Rat Nephronmentioning

confidence: 99%

“…The expression of several AC types in these structures might be due to the presence of different cell types (15,22). A localization at the cellular level of these AC mRNAs cannot be accurately studied by using in situ hybridization due to the small size of the renal tubule cells ( -inhibitable AC proteins was investigated by studying the regulation of hormone-dependent cAMP content.…”

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confidence: 99%

“…(i) Morphological studies have described two cell types in this segment, the principal cell and the type A intercalated cell (15,22). (ii) Biochemical studies have established that ␣ 2 -adrenergic agonists inhibit AVP-but not glucagon-stimulated cAMP synthesis (25).…”

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confidence: 99%

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Localization of mRNAs Encoding Ca2+-inhibitable Adenylyl Cyclases along the Renal Tubule

Chabardès

Firsov

Aarab

et al. 1996

Journal of Biological Chemistry

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Expression of Ca2؉ -inhibitable types V and VI adenylyl cyclases was studied by reverse transcription-polymerase chain reaction in rat renal glomeruli and nephron segments isolated by microdissection. Quantitation of each mRNA was achieved using a mutant cRNA which differed from the wild type by substituting two bases to create a new restriction site in the corresponding cDNA. Type VI mRNA was present all along the nephron but was more abundant in distal than in proximal segments. The expression of type V mRNA was restricted to the glomerulus and to the initial portions of the collecting duct. Expression of the Ca 2؉ -insensitive type IV mRNA studied on the same samples was evidenced only in the glomerulus. The functional relevance of the expression of Ca 2؉ -inhibitable isoforms was studied by measuring cAMP content in the microdissected outer medullary collecting duct which expressed both type V mRNA (2367 ؎ 178 molecules/mm tubular length; n ‫؍‬ 8) and type VI mRNA (5658 ؎ 543 molecules/mm, n ‫؍‬ 8). Agents known to increase intracellular Ca 2؉ in this segment induced a Ca 2؉ -dependent inhibition on either arginine vasopressin-or glucagon-stimulated cAMP level. The characteristics of these inhibitions suggest a functional and differential expression of types V and VI adenylyl cyclases in two different cell types of the rat outer medullary collecting duct.In the past few years, the control of cAMP content in mammalian cells has become more intricate by the description of several types of adenylyl cyclase with different regulatory properties (1-3). Among the eight isoforms of adenylyl cyclase cloned up to date, the type V and the type VI are characterized by an activity negatively regulated by sub-micromolar concentrations of Ca 2ϩ . This property, established in vitro on membrane preparations (4 -7), has been observed also on the cAMP content measured on cultured cells from different tissues that express Ca 2ϩ -inhibitable AC 1 isoforms (4, 8 -13). These results demonstrate therefore that type V and type VI adenylyl cyclases can be inhibited in intact cells in response to a rise in [Ca 2ϩ ] i . Northern blot analyses have demonstrated that types V and VI AC mRNAs are expressed in the rat kidney (8,14). The renal tissue is, however, structurally highly heterogeneous and includes, in addition to the nephron epithelial cells, other cell types such as interstitial and vascular cells (15). The main functions of the kidney are achieved by the glomerulus and the different segments of the nephron, and many of these physiological processes, including the maintenance of Ca 2ϩ homeostasis (16), are regulated by the cAMP and/or the phospholipase C pathway. In addition, recent data demonstrated the expression of an extracellular Ca 2ϩ receptor in the rat kidney that might participate in Ca 2ϩ -sensitive regulations in some segments of the nephron (17). In this context, the presence of Ca 2ϩ -inhibitable AC mRNAs in the rat kidney (8,14) suggests that these isoforms might contribute to the regulation of physiological ...

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“…collecting duct which contains two cell types (15,22). The results establish a cell-specific and Ca 2ϩ -dependent inhibition on either the AVP-or the glucagon-dependent cAMP content.…”

mentioning

confidence: 56%

Section: Ca 2ϩ -Inhibitable Adenylyl Cyclases Along the Rat Nephronmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Localization of mRNAs Encoding Ca2+-inhibitable Adenylyl Cyclases along the Renal Tubule

Chabardès

Firsov

Aarab

et al. 1996

Journal of Biological Chemistry

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“…Indeed, water permeability in this membrane was at least 3-fold reduced in cortical collecting ducts of AQP3 null mice. The residual water permeability after AQP3 deletion is probably accounted for by lipid-mediated water transport across the convolved basolateral membrane surface (26,31,32). Although the in vivo findings are a consequence of AQP3 deletion in collecting duct, a number of compensatory changes and physiological issues must be considered.…”

Section: Discussionmentioning

confidence: 99%

Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels

Song

Yang

et al. 2000

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

360

246

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Aquaporin-3 (AQP3) is a water channel expressed at the basolateral plasma membrane of kidney collecting-duct epithelial cells. The mouse AQP3 cDNA was isolated and encodes a 292-amino acid water͞glycerol-transporting glycoprotein expressed in kidney, large airways, eye, urinary bladder, skin, and gastrointestinal tract. The mouse AQP3 gene was analyzed, and AQP3 null mice were generated by targeted gene disruption. The growth and phenotype of AQP3 null mice were grossly normal except for polyuria. AQP3 deletion had little effect on AQP1 or AQP4 protein expression but decreased AQP2 protein expression particularly in renal cortex. Fluid consumption in AQP3 null mice was more than 10-fold greater than that in wild-type litter mates, and urine osmolality (<275 milliosmol) was much lower than in wild-type mice (>1,200 milliosmol). After 1-desamino-8-D-arginine-vasopressin administration or water deprivation, the AQP3 null mice were able to concentrate their urine partially to Ϸ30% of that in wild-type mice. Osmotic water permeability of cortical collecting-duct basolateral membrane, measured by a spatial filtering optics method, was >3-fold reduced by AQP3 deletion. To test the hypothesis that the residual concentrating ability of AQP3 null mice was due to the inner medullary collecting-duct water channel AQP4, AQP3͞AQP4 double-knockout mice were generated. The double-knockout mice had greater impairment of urinary-concentrating ability than did the AQP3 single-knockout mice. Our findings establish a form of nephrogenic diabetes insipidus produced by impaired water permeability in collecting-duct basolateral membrane. Basolateral membrane aquaporins may thus provide blood-accessible targets for drug discovery of aquaretic inhibitors.water transport ͉ AQP3 ͉ kidney ͉ urinary-concentrating mechanism ͉ polyuria A quaporin-3 (AQP3, originally called glycerol intrinsic protein, GLIP, based on its glycerol-transport function) was cloned from rat kidney by our laboratory (1) as well as by Ishibashi et al. (2) and Echevarria et al. (3). AQP3 is a relatively weak transporter of water but functions as an efficient glycerol transporter (4). Reflection coefficient measurements (5) and mutagenesis studies (6) suggested that water and glycerol share a common pathway through the AQP3 protein, although inhibition experiments were interpreted as suggesting different pathways (7). Immunocytochemistry in rat showed AQP3 protein expression in basolateral membrane of kidney collecting duct and large airways, as well as in several tissues that are thought not to have an important water-transporting role including urinary bladder, conjunctiva, and epidermis (8-11). Recent studies report strong AQP3 expression in various regions of the gastrointestinal tract including small intestine (12). Another unique feature of AQP3 is its gene structure, which is different from the water-selective mammalian aquaporins (13). AQP3, AQP7, and AQP9 have been called ''aquaglyceroporins'' because of their relatively broad solute specificity and sequence ho...

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Regulation of Transport in the Connecting Tubule and Cortical Collecting Duct

Staruschenko

2012

Comprehensive Physiology

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The central goal of this overview article is to summarize recent findings in renal epithelial transport, focusing chiefly on the connecting tubule (CNT) and the cortical collecting duct (CCD). Mammalian CCD and CNT are involved in fine tuning of electrolyte and fluid balance through reabsorption and secretion. Specific transporters and channels mediate vectorial movements of water and solutes in these segments. Although only a small percent of the glomerular filtrate reaches the CNT and CCD, these segments are critical for water and electrolyte homeostasis since several hormones, e.g. aldosterone and arginine vasopressin, exert their main effects in these nephron sites. Importantly, hormones regulate the function of the entire nephron and kidney by affecting channels and transporters in the CNT and CCD. Knowledge about the physiological and pathophysiological regulation of transport in the CNT and CCD and particular roles of specific channels/transporters has increased tremendously over the last two decades. Recent studies shed new light on several key questions concerning the regulation of renal transport. Precise distribution patterns of transport proteins in the CCD and CNT will be reviewed, and their physiological roles and mechanisms mediating ion transport in these segments will be also covered. Special emphasis will be given to pathophysiological conditions appearing as a result of abnormalities in renal transport in the CNT and CCD.

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Structural-functional relationships along the distal nephron

Cited by 142 publications

References 0 publications

Localization of mRNAs Encoding Ca2+-inhibitable Adenylyl Cyclases along the Renal Tubule

Localization of mRNAs Encoding Ca2+-inhibitable Adenylyl Cyclases along the Renal Tubule

Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels

Regulation of Transport in the Connecting Tubule and Cortical Collecting Duct

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