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

V. L. Schuster, G. Fejes-Toth, A. Naray-Fejes-Toth, S. Gluck

Research output: Contribution to journalArticle

80 Scopus citations

Abstract

Two major types of intercalated cells (IC) have been previously defined in rabbit collecting duct: α-cells have a basolateral band 3-like anion exchanger and secrete H+, whereas β-cells bind peanut agglutinin (PNA) apically and are believed to secrete HCO3-. To further define IC types, we double-labeled kidney sections with anti-H+-ATPase antibodies and with either an anti-band 3 antibody or PNA. We found four patterns of staining: 1) IC with apical H+-ATPase and basal band 3, a configuration consistent with ongoing H+ secretion, which prevailed in the inner stripe of outer medulla (OMCD(i)); 2) diffuse H+-ATPase labeling across the cell and basal band 3, which was most numerous in the outer stripe of outer medulla (OMCD(o)); 3) IC with ''bright'' apical peanut lectin, diffuse H+-ATPase, and no band 3, which was abundant in the cortical collecting duct (CCD) and probably represents HCO3--secreting cells; and 4) ''hybrid'' cells with various staining combinations (e.g., apical lectin binding and apical H+-ATPase), which although they are uncommon, were seen in the CCD. Consistent with this immunocytochemical finding of hybrid cells, cell-sorting studies on isolated CCD IC showed that 6-18% of PNA-positive cells also stained positively for band 3. We conclude that 1) band 3-positive IC in the OMCD vary axially. Most OMCD(i) IC are probably active proton secretors, whereas up to one-half of OMCD(o) IC may be latent H+ secretors. 2) The diffuse H+-ATPase pattern in putative β-cells differs from comparable results in the rat and is not consistent with a ''reversed'' α-cell. HCO3- secretion by β-cells may be driven by an H+ extrusion mechanism other than the α-cell pump re-sorted to the basolateral membrane. 3) The possibility of hybrid cells that might combine α- and β-cell transport proteins suggests a mechanism for functional reversal of collecting duct IC polarity.

Original languageEnglish (US)
Pages (from-to)F506-F517
JournalAmerican Journal of Physiology - Renal Fluid and Electrolyte Physiology
Volume260
Issue number4 29/4
DOIs
StatePublished - 1991

Keywords

  • Acid
  • Acidification
  • Alkalinization
  • Alkalosis
  • Antiport
  • Bicarbonate Chloride
  • Epithelial polarity
  • Fluorescence-activated cell sorting
  • Immunocytochemistry
  • Lectins
  • Mitochondria

ASJC Scopus subject areas

  • Physiology

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