Localization of pendrin in mouse kidney.

@article{Wall2003LocalizationOP,
  title={Localization of pendrin in mouse kidney.},
  author={Susan M. Wall and Kathryn A. Hassell and Ines E. Royaux and Eric D. Green and Judy Yi-Huei Chang and Gregory L. Shipley and Jill W. Verlander},
  journal={American journal of physiology. Renal physiology},
  year={2003},
  volume={284 1},
  pages={
          F229-41
        },
  url={https://api.semanticscholar.org/CorpusID:22831140}
}
  • S. WallK. Hassell J. Verlander
  • Published in 2003
  • Biology, Medicine
  • American journal of physiology. Renal physiology
Pendrin is expressed in the mouse distal convoluted tubule, CCD, and CNT along the apical plasma membrane of non-A-non-B intercalated cells and in subapical cytoplasmic vesicles of type B intercalate cells.

Figures and Tables from this paper

Origin and fate of pendrin-positive intercalated cells in developing mouse kidney.

It is determined that selective proliferation of pendrin-positive intercalated cells does not occur; instead, these cells may arise from undifferentiated precursor cells from separate foci, one in the connecting tubule and two in the collecting duct.

The Renal Physiology of Pendrin-Positive Intercalated Cells.

How aldosterone and angiotensin II-induced signaling regulate pendrin and the contribution of pendrin-positive ICs in the kidney to distal nephron function and blood pressure is described.

Pendrin regulation in mouse kidney primarily is chloride-dependent.

The results of this study suggest that factors that are associated with changes in distal chloride delivery govern pendrin expression in the connecting tubule and cortical collecting duct.

Pendrin protein abundance in the kidney is regulated by nitric oxide and cAMP.

It is concluded that NO acts through cAMP to reduce pendrin total protein abundance by enhancing cAMP degradation.

Pendrin localizes to the adrenal medulla and modulates catecholamine release.

It is concluded that pendrin is expressed in the adrenal medulla, where it blunts stress-induced catecholamine release.

The role of pendrin in blood pressure regulation.

The signaling mechanisms that regulate pendrin abundance and function are summarized as well as the contribution of pendrin to distal nephron function, which may modulate blood pressure partly through its extrarenal effects.

The multiple roles of pendrin in the kidney.

It is demonstrated that pendrin and the Na-Cl cotransporter (NCC; SLC12A3) cross compensate for the loss of each other, therefore masking the role that each transporter plays in salt reabsorption under baseline conditions.

The Anion Exchanger Pendrin (SLC26A4) and Renal Acid-base Homeostasis

A review of recent findings on the role and regulation of pendrin in the context of the kidneys role in acid-base homeostasis in health and disease concludes that pendrin is the apical bicarbonate extruding pathway.

The role of pendrin in renal physiology.

Pendrin modulates aldosterone-induced Na(+) absorption by changing ENaC abundance and function through a kidney-specific mechanism that does not involve changes in the concentration of a circulating hormone.
...

Pendrin: an apical Cl-/OH-/HCO3- exchanger in the kidney cortex.

The results demonstrate that pendrin mRNA expression in the rat kidney is abundant and limited to the cortex, and pendrin is an apical Cl-/base exchanger in the kidney proximal tubule and CCD and mediates Cl- /OH, Cl/HCO3, and Cl--/formate exchange.

Intercalated cell subtypes in connecting tubule and cortical collecting duct of rat and mouse.

It is concluded that striking differences exist in the prevalence and distribution of the different types of intercalated cells in the CNT, ICT, and CCD of rat and mouse.

Pendrin, encoded by the Pendred syndrome gene, resides in the apical region of renal intercalated cells and mediates bicarbonate secretion

Immunolocalization studies indicate that pendrin is an apical anion transporter in intercalated cells of CCDs and has an essential role in renal bicarbonate secretion.

Localization of the thiazide sensitive Na-Cl cotransporter, rTSC1 in the rat kidney.

In situ hybridization showed rTSC1 transcripts were localized to short, convoluted tubule segments in the kidney cortex and Ultrastructural studies by immunoelectron microscopy showed the cotransporter protein to be localized predominately on apical microvilli of the distal convoluted tubules cells.

Localization of a proton-pumping ATPase in rat kidney.

It is demonstrated that subpopulations of cortical intercalated cells have opposite polarities of an H+ATPase, consistent with the presence of both proton- and bicarbonate-secreting cells, and suggested a role for the H+ ATPase in acid/base regulation or H+ transport in segments other than the collecting duct and the proximal tubule.

Activation of acid-secreting intercalated cells in rabbit collecting duct with ammonium chloride loading.

It is suggested that rabbits respond to acid loading via enhancement of both electrogenic proton secretion and Cl-/HCO3- exchange in intercalated cells in the inner CCD and the OMCDo and morphometric analysis demonstrated an increase in the amount of basolateral plasma membrane in these intercalations.

Subtypes of intercalated cells in rat kidney collecting duct defined by antibodies against erythroid band 3 and renal vacuolar H+-ATPase.

Results demonstrate the coexpression of H+-ATPase and band 3 in opposite plasma membrane domains of a subpopulation of intercalated cells that are probably the acid-excreting (type A) cells and probably include the bicarbonate-exCreting ( type B) cells.

Colocalization of H(+)-ATPase and band 3 anion exchanger in rabbit collecting duct intercalated cells.

The possibility of hybrid cells that might combine alpha- and beta-cell transport proteins suggests a mechanism for functional reversal of collecting duct IC polarity.

Identification of distinct subpopulations of intercalated cells in the mouse collecting duct.

It is concluded that three morphologically and immunologically distinct types of intercalated cells are present in the mouse kidney.