Localization of a potassium channel gene (kcne1) to 21q22.1-q22.2 by insitu hybridization and somatic-cell hybridization
Abstract
K+ channels form a diverse family of membrane-spanning proteins that exhibit various electrophysiological and pharmacological properties (5). They play a prominent role in a wide variety ofbiological functions such as cell growth, osmotic reg-ulation, hormonal secretion, and excitability (5). Among the various K + channel proteins characterized, the KCNEl pro-tein is distinct from the Shaker-type channels in its structure and biophysical properties (for review, see 6). It consists of 129-130 amino acid residues with a single putative transmem-brane domain and directs the expression of a very slow activat-ing voltage-dependent K + current (4, 7), when expressed in Xenopus oocytes. Originally characterized in epithelial cells (7), KCNEl has also been cloned from neonatal heart, uterus, and human Band T lymphocytes (1-3). Its presence in human T lymphocytes suggested that the KCNEl protein could be involved in the T cell activation process (1). In the present work, we mapped the KCNEl gene by in situ hybridization on human metaphase chromosomes and Southern blot analysis of human-Chinese hamster cell hybrids.
Domains
Microbiology and Parasitology
Origin : Publication funded by an institution