Aldosterone-induced proteins: Purification and localization of GP65,70

H. M. Szerlip, L. Weisberg, M. Clayman, E. Neilson, J. B. Wade, M. Cox

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Aldosterone stimulates sodium transport in responsive epithelia by inducing 'effector' proteins that control or modulate transcellular sodium flux. We have previously identified a group of electrophoretically microheterogeneous (pI 5.8-6.2) and polymorphic (M(r) 65 and 70) glycoproteins that are specifically induced by aldosterone in toad urinary bladders (TUBs) and cultured toad kidney cells (A6 cell line). We raised a series of monoclonal antibodies (MAb) to these proteins and, using light and electron immunohistochemistry, localized the higher M(r) glycoproteins (GP70) to the apical plasma membrane and subapical granules of the sodium-transporting cell of the TUB epithelium, the granular cell. GP70 appears to be discharged into the bladder lumen; this process is increased by phorbol myristate acetate, an agent known to induce granule exocytosis. These findings are consistent with the possibility that GP70 represent components or modulators of the 'high-resistance' renal epithelial sodium channel. MAbs reactive against GP65 did not identify these glycoproteins within TUB epithelial cells; these lower M(r) aldosterone-induced proteins may be incompletely processed forms of GP70.

Original languageEnglish (US)
Pages (from-to)25/4
JournalAmerican Journal of Physiology - Cell Physiology
Issue number4
StatePublished - 1989

ASJC Scopus subject areas

  • Physiology
  • Cell Biology


Dive into the research topics of 'Aldosterone-induced proteins: Purification and localization of GP65,70'. Together they form a unique fingerprint.

Cite this