CFTR protein expression in primary and cultured epithelia

Pamela L. Zeitlin, Isabelle Crawford, Luo Lu, Sybille Woel, Michael E. Cohen, Mark Donowitz, Marshall H. Montrose, Ada Hamosh, Garry R. Cutting, Dieter Gruenert, Richard Huganir, Peter Maloney, William B. Guggino

Research output: Contribution to journalArticlepeer-review

Abstract

The gene responsible for the lethal disorder cystic fibrosis encodes a 1480-amino acid glycoprotein, CFTR. Using polyclonal antibodies directed against separate phosphorylation sites in the pre-nucleotide-binding fold (exon 9) and the R domain (exon 13), we have identified a 165-kDa protein in Xenopus laevis oocytes injected with recombinant CFTR cRNA transcribed from the full-length CFTR plasmid pBQ4.7. A protein of the same mobility was also detected with Western blotting techniques in whole cell extracts of cells that express CFTR mRNA (T84, FHTE, HT-29), including biopsied human nasal and bronchial tissue. Immunodetectable 165-kDa protein was concentrated in the apical membrane fraction of ileal villus tissue. We also report that the 165-kDa protein levels can be modulated pharmacologically, and these levels are appropriately correlated with second-messenger-regulated Cl- efflux. Thus, native or recombinant CFTR can be recognized by these anti-CFTR peptide polyclonal antibodies.

Original languageEnglish (US)
Pages (from-to)344-347
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number1
DOIs
StatePublished - 1992

Keywords

  • Chloride channel
  • Cystic fibrosis transmembrane conductance regulator

ASJC Scopus subject areas

  • General

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