Possible involvement of a calmodulin regulated Ca2+‐ATPase in exocytosis performance in Paramecium tetraurelia cells

FEBS Letters

Tiggemann, R.¹  Plattner, H.¹ 

[1] Faculty of Biology, University of Konstanz, PO Box 5560, D-7750 Konstanz, FROG

关键词: Adenosinetriphosphatase;    Calcium;    Calmodulin;    Exocytosis;    Membrane fusion;    Paramecium;   

DOI  :  10.1016/0014-5793(82)80812-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Surface membrane fractions from Paramecium tetraurelia cells contain a calmodulin-stimulated Ca²⁺-ATPase responding to low levels of free Ca²⁺ and with features characteristic of a membrane-bound ATPase responding to low levels of free Ca²⁺ and with features characteristics of a membrane-bound ATPase. Among the different strains analyzed this enzyme was practically absent selectively from the ‘non-discharge” mutant nd9—28°C (from J. Beisson); if cultured at a permissive temperature (18°C), this strain showed identical values of calmodulin-stimulated Ca²⁺-ATPase activity as wild-type cells (7S) or strains with mutations which do not affect exocytosis performance. We conclude that this calmodulin-stimulated Ca²⁺-activated ATPase might be a prerequisite for membrane fusion in the course of exocytosis performance.

【 授权许可】

Unknown