Channelopathies of inwardly rectifying potassium channels

M. Roselle Abraham, Arshad Jahangir, Alexey E. Alekseev, Andre Terzic

Research output: Contribution to journalReview articlepeer-review

Abstract

Mutations in genes encoding ion channels have increasingly been identified to cause disease conditions collectively termed channelopathies. Recognizing the molecular basis of an ion channel disease has provided new opportunities for screening, early diagnosis, and therapy of such conditions. This synopsis provides an overview of progress in the identification of molecular defects in inwardly rectifying potassium (Kir) channels. Structurally and functionally distinct from other channel families, Kir channels are ubiquitously expressed and serve functions as diverse as regulation of resting membrane potential, maintenance of K+ homeostasis, control of heart rate, and hormone secretion. In humans, persistent hyperinsulinemic hypoglycemia of infancy, a disorder affecting the function of pancreatic β cells, and Bartter's syndrome, characterized by hypokalemic alkalosis, hypercalciuria, increased serum aldosterone, and plasma renin activity, are the two major diseases linked so far to mutations in a Kir channel or associated protein. In addition, the weaver phenotype, a neurological disorder in mice, has also been associated with mutations in a Kir channel subtype. Further genetic linkage analysis and full understanding of the consequence that a defect in a Kir channel would have on disease pathogenesis are among the priorities in this emerging field of molecular medicine.

Original languageEnglish (US)
Pages (from-to)1901-1910
Number of pages10
JournalFASEB Journal
Volume13
Issue number14
StatePublished - Nov 17 1999

Keywords

  • Bartter's syndrome
  • Ion channel disease
  • Persistent hyperinsulinemic hypoglycemia of infancy
  • Weaver phenotype

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Fingerprint Dive into the research topics of 'Channelopathies of inwardly rectifying potassium channels'. Together they form a unique fingerprint.

Cite this