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Salt stress increases abundance and glycosylation of CFTR localized at apical surfaces of salt gland secretory cells.

Publication ,  Journal Article
Ernst, SA; Crawford, KM; Post, MA; Cohn, JA
Published in: Am J Physiol
October 1994

Osmotic stress elicits hypertonic NaCl secretion and promotes structural and biochemical differentiation in avian salt glands. In addition to cholinergic control, Cl- secretion is stimulated by vasoactive intestinal peptide (VIP), suggesting that the cystic fibrosis transmembrane conductance regulator (CFTR) may be present and that its expression may be regulated by chronic salt stress. Anion efflux, assayed by 6-methoxy-N-(3-sulfopropyl)quinolinium fluorescence changes in single cells, was stimulated by VIP or 8-(4-chlorophenylthio)adenosine 3',5'-cyclic monophosphate. Immunoblots with a COOH-terminal peptide antibody to human CFTR revealed approximately 170- and approximately 180-kDa bands in lysates from control and salt-stressed glands, respectively. Both variants reduced to approximately 140 kDa after N-glycanase digestion and gave identical tryptic phosphopeptide maps after immunoprecipitation and phosphorylation by protein kinase A. CFTR was localized to apical membranes by immunofluorescence and, additionally, to subapical vesicles by immunoelectron microscopy. Salt stress induced an approximately twofold increase in CFTR abundance/cell protein (approximately 5-fold/cell) and intensified apical membrane immunofluorescence. For comparison, Na+ pump expression increased approximately fourfold per cell protein with little change in actin. Thus differentiation induced by salt stress is accompanied by alteration in CFTR abundance and glycosylation. Upregulation of CFTR likely contributes to increased efficiency of Cl- secretion.

Duke Scholars

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

October 1994

Volume

267

Issue

4 Pt 1

Start / End Page

C990 / 1001

Location

United States

Related Subject Headings

  • Tissue Distribution
  • Sodium Chloride
  • Salt Gland
  • Phosphoproteins
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Peptide Mapping
  • Osmotic Pressure
  • Membrane Proteins
  • Immunohistochemistry
  • Glycosylation
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Ernst, S. A., Crawford, K. M., Post, M. A., & Cohn, J. A. (1994). Salt stress increases abundance and glycosylation of CFTR localized at apical surfaces of salt gland secretory cells. Am J Physiol, 267(4 Pt 1), C990-1001. https://doi.org/10.1152/ajpcell.1994.267.4.C990
Ernst, S. A., K. M. Crawford, M. A. Post, and J. A. Cohn. “Salt stress increases abundance and glycosylation of CFTR localized at apical surfaces of salt gland secretory cells.Am J Physiol 267, no. 4 Pt 1 (October 1994): C990-1001. https://doi.org/10.1152/ajpcell.1994.267.4.C990.
Ernst SA, Crawford KM, Post MA, Cohn JA. Salt stress increases abundance and glycosylation of CFTR localized at apical surfaces of salt gland secretory cells. Am J Physiol. 1994 Oct;267(4 Pt 1):C990-1001.
Ernst, S. A., et al. “Salt stress increases abundance and glycosylation of CFTR localized at apical surfaces of salt gland secretory cells.Am J Physiol, vol. 267, no. 4 Pt 1, Oct. 1994, pp. C990-1001. Pubmed, doi:10.1152/ajpcell.1994.267.4.C990.
Ernst SA, Crawford KM, Post MA, Cohn JA. Salt stress increases abundance and glycosylation of CFTR localized at apical surfaces of salt gland secretory cells. Am J Physiol. 1994 Oct;267(4 Pt 1):C990-1001.

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

October 1994

Volume

267

Issue

4 Pt 1

Start / End Page

C990 / 1001

Location

United States

Related Subject Headings

  • Tissue Distribution
  • Sodium Chloride
  • Salt Gland
  • Phosphoproteins
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Peptide Mapping
  • Osmotic Pressure
  • Membrane Proteins
  • Immunohistochemistry
  • Glycosylation