Effect of nocodazole on the water permeability response to vasopressin in rabbit collecting tubules perfused in vitro.

Phillips, Matthew E.; Taylor, Ann

doi:10.1113/jphysiol.1989.sp017588

Cited by 39 publications

(37 citation statements)

References 33 publications

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“…Table 12C shows the transcripts corresponding to the microtubule proteins and microtubule-associated proteins, including molecular motors that are expressed above background on the arrays. Microtubule disruption with colchicine and other agents reduces the hydroosmotic action of vasopressin in collecting ducts (61) through effects on AQP2 trafficking (67). In addition, it has been shown that both dyneins (microtubule-based molecular motors) and dynactin in the inner medulla were associated with trafficking of AQP2-containing vesicles to the apical plasma membrane (49).…”

Section: Resultsmentioning

confidence: 99%

Transcriptional profiling of native inner medullary collecting duct cells from rat kidney

Uawithya

Pisitkun

Ruttenberg

et al. 2008

Physiological Genomics

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pressin acts on the inner medullary collecting duct (IMCD) in the kidney to regulate water and urea transport. To obtain a "parts list" of gene products expressed in the IMCD, we carried out mRNA profiling of freshly isolated rat IMCD cells using Affymetrix Rat 230 2.0 microarrays with ϳ31,000 features; 7,913 annotated transcripts were found to be expressed above background in the IMCD cells. We have created a new online database (the "IMCD Transcriptome Database;" http://dir.nhlbi.nih.gov/papers/lkem/imcdtr/) to make the results publicly accessible. Among the 30 transcripts with the greatest signals on the arrays were 3 water channels: aquaporin-2, aquaporin-3, and aquaporin-4, all of which have been reported to be targets for regulation by vasopressin. In addition, the transcript with the greatest signal among members of the solute carrier family of genes was the UT-A urea transporter (Slc14a2), which is also regulated by vasopressin. The V2 vasopressin receptor was strongly expressed, but the V1a and V1b vasopressin receptors did not produce signals above background. Among the 200 protein kinases expressed, the serumglucocorticoid-regulated kinase (Sgk1) had the greatest signal intensity in the IMCD. WNK1 and WNK4 were also expressed in the IMCD with a relatively high signal intensity, as was protein kinase A (␤-catalytic subunit). In addition, a large number of transcripts corresponding to A kinase anchoring proteins and 14-3-3 proteins (phospho-S/T-binding proteins) were expressed. Altogether, the results combine with proteomics studies of the IMCD to provide a framework for modeling complex interaction networks responsible for vasopressin action in collecting duct cells. oligonucleotide array; vasopressin; aquaporin-2; urea transport; kinases THE INNER MEDULLARY COLLECTING DUCT (IMCD) is the terminal portion of the collecting duct system of the kidney. The collecting duct system represents the final site of adjustment of urinary composition and volume and therefore is critical for extracellular fluid homeostasis. An important regulator of collecting duct transport function is vasopressin, which controls both water and urea transport (21,53).To address the mechanisms of vasopressin signaling in the renal IMCD, we have been following a "systems-biology" approach consisting of identification of the component proteins via protein mass spectrometry-based analysis (2,29,30,62,71,102) and antibody-based quantification of protein abundance (41) coupled to computational analysis of the identified proteins to discover signaling networks involved in IMCD regulation (30).

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Section: Resultsmentioning

confidence: 99%

Transcriptional profiling of native inner medullary collecting duct cells from rat kidney

Uawithya

Pisitkun

Ruttenberg

et al. 2008

Physiological Genomics

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“…In particular, the microtubular network has been implicated in this process, since chemical disruption of microtubules inhibits the increase in permeability both in the toad bladder and in the mammalian collecting duct (189,190). Because microtubule-disruptive agents inhibit the development of the hydrosmotic response to vasopressin, but have no effect on the maintenance of an established response, and because they have been reported to slow the development of the response without affecting the final permeability in toad bladders (230), it has been deduced that microtubules appear to be involved in the coordinated delivery of water channels, without being involved in the actual insertion process, or in recycling of water channels.…”

Section: Role Of the Cytoskeletonmentioning

confidence: 99%

Aquaporins in the Kidney: From Molecules to Medicine

Nielsen

Frøkiær

Marples

et al. 2002

Physiological Reviews

1,131

1,022

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The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical question of how water specifically crosses biological membranes. In the kidney, at least seven aquaporins are expressed at distinct sites. AQP1 is extremely abundant in the proximal tubule and descending thin limb and is essential for urinary concentration. AQP2 is exclusively expressed in the principal cells of the connecting tubule and collecting duct and is the predominant vasopressin-regulated water channel. AQP3 and AQP4 are both present in the basolateral plasma membrane of collecting duct principal cells and represent exit pathways for water reabsorbed apically via AQP2. Studies in patients and transgenic mice have demonstrated that both AQP2 and AQP3 are essential for urinary concentration. Three additional aquaporins are present in the kidney. AQP6 is present in intracellular vesicles in collecting duct intercalated cells, and AQP8 is present intracellularly at low abundance in proximal tubules and collecting duct principal cells, but the physiological function of these two channels remains undefined. AQP7 is abundant in the brush border of proximal tubule cells and is likely to be involved in proximal tubule water reabsorption. Body water balance is tightly regulated by vasopressin, and multiple studies now have underscored the essential roles of AQP2 in this. Vasopressin regulates acutely the water permeability of the kidney collecting duct by trafficking of AQP2 from intracellular vesicles to the apical plasma membrane. The long-term adaptational changes in body water balance are controlled in part by regulated changes in AQP2 and AQP3 expression levels. Lack of functional AQP2 is seen in primary forms of diabetes insipidus, and reduced expression and targeting are seen in several diseases associated with urinary concentrating defects such as acquired nephrogenic diabetes insipidus, postobstructive polyuria, as well as acute and chronic renal failure. In contrast, in conditions with water retention such as severe congestive heart failure, pregnancy, and syndrome of inappropriate antidiuretic hormone secretion, both AQP2 expression levels and apical plasma membrane targetting are increased, suggesting a role for AQP2 in the development of water retention. Continued analysis of the aquaporins is providing detailed molecular insight into the fundamental physiology and pathophysiology of water balance and water balance disorders.

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“…On the basis of earlier evidence from amphibian model systems, isolated perfused collecting ducts, and in vivo studies, it was proposed that VP acted by stimulating water channel insertion into the apical plasma membrane by VP-induced exocytosis of cytoplasmic vesicles (29,45,48,57,100,141). While a modeling study in 1993 proposed that both the exocytotic and the endocytotic arms of the pathway were likely to be involved in the process leading to membrane accumulation of water channels (64), most attention was focused on the exocytotic pathway as the main regulatory event in the onset of VP action (141).…”

Section: Role Of Both Exocytosis and Endocytosis In Aqp2 Membrane Accmentioning

confidence: 99%

New insights into the dynamic regulation of water and acid-base balance by renal epithelial cells

Brown

Bouley

Păunescu

et al. 2012

American Journal of Physiology-Cell Physiology

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Maintaining tight control over body fluid and acid-base homeostasis is essential for human health and is a major function of the kidney. The collecting duct is a mosaic of two cell populations that are highly specialized to perform these two distinct processes. The antidiuretic hormone vasopressin (VP) and its receptor, the V2R, play a central role in regulating the urinary concentrating mechanism by stimulating accumulation of the aquaporin 2 (AQP2) water channel in the apical membrane of collecting duct principal cells. This increases epithelial water permeability and allows osmotic water reabsorption to occur. An understanding of the basic cell biology/physiology of AQP2 regulation and trafficking has informed the development of new potential treatments for diseases such as nephrogenic diabetes insipidus, in which the VP/V2R/AQP2 signaling axis is defective. Tubule acidification due to the activation of intercalated cells is also critical to organ function, and defects lead to several pathological conditions in humans. Therefore, it is important to understand how these "professional" proton-secreting cells respond to environmental and cellular cues. Using epididymal proton-secreting cells as a model system, we identified the soluble adenylate cyclase (sAC) as a sensor that detects luminal bicarbonate and activates the vacuolar proton-pumping ATPase (V-ATPase) via cAMP to regulate tubular pH. Renal intercalated cells also express sAC and respond to cAMP by increasing proton secretion, supporting the hypothesis that sAC could function as a luminal sensor in renal tubules to regulate acid-base balance. This review summarizes recent advances in our understanding of these fundamental processes. aquaporin 2; vacuolar ATPase; intercalated cell; principal cell; kidney; epididymis IT HAS BEEN KNOWN FOR MANY years that the major functions of collecting duct principal cells and intercalated cells (Fig. 1) can be regulated by the recycling of aquaporin 2 (AQP2) and the vacuolar H ϩ -ATPase (V-ATPase), respectively, between cytoplasmic vesicles and the plasma membrane (1,26,28,40,54,67,85,142). A considerable amount of the earlier data illuminating these processes was generated using readily accessible model epithelial systems such as the toad urinary bladder (48,83,140) and the turtle bladder (3,127,128), in which cellular function and morphology could be correlated with measurements of water flux and acid-base transport. More recently, a variety of in vitro cell culture models have replaced the toad bladder as an experimental system for water channel trafficking and function. This review will show how cell cultures have provided novel and important information on aquaporin 2 trafficking that has been translatable to the in vivo situation and has allowed the development of strategies to bypass the vasopressin (VP)/vasopressin type 2 receptor (V2R) signaling axis that is defective in nephrogenic diabetes insipidus (NDI). We will go on to demonstrate how the epididymis and vas deferens (from the male reproductive tract) ha...

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Effect of nocodazole on the water permeability response to vasopressin in rabbit collecting tubules perfused in vitro.

Cited by 39 publications

References 33 publications

Transcriptional profiling of native inner medullary collecting duct cells from rat kidney

Transcriptional profiling of native inner medullary collecting duct cells from rat kidney

Aquaporins in the Kidney: From Molecules to Medicine

New insights into the dynamic regulation of water and acid-base balance by renal epithelial cells

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