Selectable mutations altering two mechanisms of mammalian K+ transport are dominant

Author:

Gargus J. J.

Abstract

Somatic cell mutants with altered K+ transport have previously been isolated from mutagenzied LMTK- cells for their ability to grow at subthreshold low-potassium concentrations (0.2 mM). These mutants fall into two classes: one class, LTK-5, possesses a functionally altered furosemide-sensitive Na+-K+-Cl- cotransport system and the other, LTK-1, an altered K+-conducting channel. Somatic cell hybrids have been formed between each of these cell lines and a wild-type L-cell line, making use of complementing selectable marker mutations carried by these parents, to establish the dominance of the K+ transport mutations. Hybrids were isolated and studied in two ways: clonal hybrid cell lines were selected in a manner unbiased toward their K+ transport phenotype, which was later assayed; and the number of independent hybrids arising in this single-selective condition was compared with the number arising in a condition which is double selective for the mutant phenotype as well. By both assays, hybrids formed with LTK-1 or LTK-5 as a parent uniformly exhibited the mutant phenotype by growth and cloning, whereas control hybrids with LMTK- as parent never did. This demonstrates both transport mutations to be dominant and thus potentially isolatable.

Publisher

American Physiological Society

Subject

Cell Biology,Physiology

Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. The Role of a PDGF-Activated Nonselective Cation Channel in the Proliferative Response;Nonselective Cation Channels;1993

2. Ion Transport in Mutant Cell Lines: Possibilities for Analysis;Epithelial Secretion of Water and Electrolytes;1990

3. PROPERTIES AND DIVERSITY OF (NA-K-C1) COTRANSPORTERS;ANNU REV PHYSIOL;1989

4. Gene transfer of a putative mammalian K+ channel gene from genomic and cosmid DNA;American Journal of Physiology-Cell Physiology;1988-07-01

5. Mutant isolation and gene transfer as tools in study of transport proteins;American Journal of Physiology-Cell Physiology;1987-05-01

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