Literature DB >> 3039855

Three distinct cell populations in rat kidney collecting duct.

H Holthöfer, B A Schulte, G Pasternack, G J Siegel, S S Spicer.   

Abstract

The morphologically heterogeneous cell populations in the collecting ducts of the rat kidney were studied using immunocytochemical detection of Na+-K+-ATPase and the anion channel (band 3) glycoprotein. Both enzymes were localized to the basal aspect of separate and morphologically distinct subpopulations of cells in various segments of the collecting duct. Na+-K+-ATPase appeared to be present exclusively in principal cells as identified by their morphology, whereas band 3 antibodies reacted only with intercalated cells. However, 5-20% of cells with the morphological characteristics of intercalated cells failed to react with either antisera in various segments of collecting ducts. As band 3 glycoprotein serves in exchanging intracellular bicarbonate for chloride, it is highly likely that the cells positive for this antigen secrete protons. The method introduced here appears thus useful for distinguishing between principal and intercalated cells by differences in their enzyme content and further for revealing two subpopulations of intercalated cells. This method promises to provide a useful approach for studying the principal and intercalated cell populations in various metabolic states.

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Year:  1987        PMID: 3039855     DOI: 10.1152/ajpcell.1987.253.2.C323

Source DB:  PubMed          Journal:  Am J Physiol        ISSN: 0002-9513


  18 in total

1.  Quantitative immunogold localization of Na, K-ATPase along rat nephron.

Authors:  T Takada; A Yamamoto; K Omori; Y Tashiro
Journal:  Histochemistry       Date:  1992-10

2.  Electrophysiological identification of alpha- and beta-intercalated cells and their distribution along the rabbit distal nephron segments.

Authors:  S Muto; K Yasoshima; K Yoshitomi; M Imai; Y Asano
Journal:  J Clin Invest       Date:  1990-12       Impact factor: 14.808

3.  Shear stress-induced volume decrease in C11-MDCK cells by BK-alpha/beta4.

Authors:  J David Holtzclaw; Liping Liu; P Richard Grimm; Steven C Sansom
Journal:  Am J Physiol Renal Physiol       Date:  2010-06-24

4.  Renal carbonic anhydrase in the quail Coturnix coturnix japonica: I. Activity and distribution in male and female metanephros.

Authors:  M G Gabrielli; P Palatroni; S Vincenzetti
Journal:  Histochem J       Date:  1990-11

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

Authors:  S L Alper; J Natale; S Gluck; H F Lodish; D Brown
Journal:  Proc Natl Acad Sci U S A       Date:  1989-07       Impact factor: 11.205

Review 6.  [Regulation of ion conductance in the cortical collecting duct].

Authors:  E Schlatter
Journal:  Klin Wochenschr       Date:  1991-09-03

7.  Intercalated cell BK-alpha/beta4 channels modulate sodium and potassium handling during potassium adaptation.

Authors:  J David Holtzclaw; P Richard Grimm; Steven C Sansom
Journal:  J Am Soc Nephrol       Date:  2010-03-18       Impact factor: 10.121

8.  Basolateral membrane sodium-independent Cl-/HCO3- exchanger in rat inner medullary collecting duct cell.

Authors:  R A Star
Journal:  J Clin Invest       Date:  1990-06       Impact factor: 14.808

9.  Renal intercalated cells are rather energized by a proton than a sodium pump.

Authors:  Régine Chambrey; Ingo Kurth; Janos Peti-Peterdi; Pascal Houillier; Jeffrey M Purkerson; Françoise Leviel; Moritz Hentschke; Anselm A Zdebik; George J Schwartz; Christian A Hübner; Dominique Eladari
Journal:  Proc Natl Acad Sci U S A       Date:  2013-04-22       Impact factor: 11.205

10.  Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus of the protein to the cytoplasmic side of the red cell membrane and distribution of the protein in some human tissues.

Authors:  S D Wainwright; M J Tanner; G E Martin; J E Yendle; C Holmes
Journal:  Biochem J       Date:  1989-02-15       Impact factor: 3.857

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