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Functional aspects of calmodulin in protozoa

Published online by Cambridge University Press:  19 September 2011

Yoshinori Nozawa
Affiliation:
Department of Biochemistry, Gifu University School of Medicine, Tsuksamachi-40, Gifu, Japan
Seiji Nagao
Affiliation:
Department of Biochemistry, Gifu University School of Medicine, Tsuksamachi-40, Gifu, Japan
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Abstract

Calmodulin is a ubiquitous endogenous calcium receptor in eukaryotic cells and is involved in many different physiological functions. The presence of calmodulins in protozoa has been reported for Tetrahymena and Paramecium. Calmodulin purified from T. pyriformis is composed of 147 amino acids and the amino-terminal is acetylated.Compared to bovine brain calmodulin, there are 11 substitutions and 1 deletion of amino acid residue(s). Besides such structural specificity, Tetrahymena calmodulin (T-CaM) is highly unique in that it has a potential ability to activate the pellicle-bound guanylate cyclase in a calcium-dependent manner. This stimulatory effect is also observed in Paramecium calmodulin (P-CaM). Bovine brain calmodulin represses the T-CaM-dependent activation of guanylate cyclase, indicating that bovine brain CaM exerts its inhibitory influence by interfering with the calmodulin-binding site of this enzyme. The 14S and 30S dyneins extracted from demembranated cilia with EDTA contai ATPase activities which are potentiated by addition of calmodulin. Taken together with its location in cilia, T-CaM appears to regulate the ciliary movement. Moreover, evidence has been provided that calmodulin may be implicated in the glycoprotein biosynthesis. The phosphorylated derivatives of the long chain polyisoprenoid alcohols (dolichol phosphates) are known to act as coenzymes, and the microsomal enzyme involving dolichol phosphorylation is calcium-requiring CTP-dependent and activated by calmodulin. A role for calmodulin in the control of cell growth is postulated by the concerted fluctuations of calmodulin contentand guanylate cyclase activity during the cell cycle in synchronized Tetrahymena cells. In addition, some other possible functions for calmodulin can be considered in protozoa.

Résumé

La calmoduline est un récepteur endogène et ubiquite du calcium dans les cellules eucaryotes et est impliquée dans de nombreuses fonctions physiologiques différentes. La présence de calmodulines chez les Protozoaires a été rapportée pour Tetrahymena et Paramecium. La calmoduline purifiée à partir de T. pyriformis est composée de 147 amino acides et l'aminoacide terminal est acétylé. Par comparaison avec la calmoduline de cerveau de bovin, il y a 11 substitutions et 1 délétion de résidu(s) acide aminé(s). A côté d'une telle spéciflcité structurale, la calmoduline de Tetrahymena (T-CaM) est unique en ce qu'elle a la capacité potentielle d'activer d'une manière calcium-dépendante la guanylate cyclase liée à la pellicule. Cet effet de stimulation est également observé avec la calmoduline de Paramecium (P-CaM). La calmoduline de cerveau de bovin réprime l'activation T-CaM-dépendante de la guanylate cyclases, indiquant que la CaM de cerveau de bovin exerce son influence inhibitrice en interférant avec les sites de fixation de la calmoduline de cette enzyme. Les dyneines 14S et 30S, extraites des cils débarassés de leur membrane par l'EDTA présentent des activités ATPasiques qui sont renforcées par l'addition de calmoduline. En considérant ègalement sa localisation dans les cils, la T-CaM paraît réguler le mouvement cilaire. Deplus, des preuves ont été fournies en ce qui concerne la possible implication dela calmoduline dans la biosynthése des glycoprotéines. Les dérivés phosphorylés des longues chaînes d'alcools polyisoprenoides (phosphates de dolichol) sont connus pour agir comme coenzymes, et l'enzyme microsomale impliquant la phosphorylation des dolichols est calcium-dépendante et CTP-dépendante, et, activée par la calmoduline. On peut postuler un rôle particulier de la calmoduline dans la croissance cellulaire en raison de fluctuations corrélées du contenu en calmoduline et de l'activité de la guanylate cyclase au cours du cycle cellulaire chez les cellules synchronisés de Tetrahymena. De plus, quelques autres fonctions possibles peuvent être considérées chez les protozoaires.

Type
Research Article
Copyright
Copyright © ICIPE 1986

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