The plasma-membrane component is the primary site of action of alloxan on ATP-driven Ca2+ transport in vascular-muscle microsomal fractions

Author:

Kwan C Y1

Affiliation:

1. Smooth Muscle Research Program and Department of Biomedical Sciences, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.

Abstract

The direct effects of alloxan in vitro on the handling of Ca2+ by microsomal fractions from dog aortic smooth muscle were investigated. Preincubation of the vascular-muscle microsomal membranes with alloxan showed a suppression of both binding of Ca2+ (in the absence of ATP) and ATP-driven Ca2+ transport. Alloxan substantially inhibited the microsomal ATP-driven Ca2+ transport stimulated by Pi, but not that stimulated by oxalate. Studies using subfractions isolated from the microsomal membranes on a sucrose density gradient indicated that plasma membrane is the primary site of action of alloxan on the ATP-driven Ca2+ transport.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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. Effects of Free Radicals on Coronary Artery;Medical Principles and Practice;2003

2. The role of plasma membrane CA2+ Pumps (PMCAs) in pathologies of mammalian cells;Frontiers in Bioscience;2002

3. Ca2+ pumps in smooth muscle cells;Journal of Muscle Research and Cell Motility;1993-04

4. Inhibition of the transepithelial potential difference and short circuit current in the isolated frog skin by alloxan;Comparative Biochemistry and Physiology Part C: Comparative Pharmacology;1992-05

5. Alloxan inhibits ligand binding to adrenoceptors of vascular smooth muscle microsomes;Biochemical Journal;1990-08-15

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