Calcium-dependent protein phosphorylation in Babesia bovis and its role in growth regulation

Intracellular growth of protozoan parasite Babesia bovis has been followed to study the effect of some chemical agents on growth regulation. Using an in vitro parasite culture system we present evidence that the normal growth of the parasite is dependent upon available calcium and a Ca2+-binding pro...

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Bibliographic Details
Published in:The Journal of parasitology 1990-04, Vol.76 (2), p.153-161
Main Authors: Ray, A. (University of Missouri, Columbia, MO), Quade, J, Carson, C.A, Ray, B.K
Format: Article
Language:English
Subjects:
Animals
BABESIA
Babesia - enzymology
Babesia - growth & development
Babesia - metabolism
Babesia bovis
Biochemistry
Biochemistry. Physiology. Immunology. Molecular biology
Biological and medical sciences
CALCIO
CALCIUM
Calcium - pharmacology
CALMODULIN
Calmodulin - antagonists & inhibitors
Calmodulin - pharmacology
Cell growth
Culture Media
Erythrocytes
ESTIMULANTES DEL CRECIMIENTO
FOSFORILACION
Fundamental and applied biological sciences. Psychology
Histones
Imidazoles - pharmacology
Invertebrates
Merozoites
Parasites
Parasitism
Phosphoproteins
PHOSPHORYLATION
PLANT GROWTH SUBSTANCES
PROTEIN KINASE
Protein Kinases - metabolism
PROTEINAS
PROTEINE
PROTEINS
Protozoa
Protozoan Proteins - metabolism
SUBSTANCE DE CROISSANCE VEGETALE
Threonine - metabolism
TRANSFERASAS
TRANSFERASE
TRANSFERASES
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Description
Summary:Intracellular growth of protozoan parasite Babesia bovis has been followed to study the effect of some chemical agents on growth regulation. Using an in vitro parasite culture system we present evidence that the normal growth of the parasite is dependent upon available calcium and a Ca2+-binding protein, calmodulin, because sequestration of either of these 2 components from the culture medium causes inhibition of parasitic growth. Further studies demonstrate that the parasite contains a protein kinase that can phosphorylate a 40-kDa parasitic protein and its activity is regulated by calcium and calmodulin. Both the enzyme and its substrate are present in the membrane of the parasite. In addition, the parasite also contains a highly active protein kinase C activity that is documented by phosphorylating histone, a known substrate for protein kinase C. These findings suggest a possible correlation between the growth of parasite and calcium/calmodulin-dependent protein phosphorylation activity.
ISSN:0022-3395
1937-2345
DOI:10.2307/3283006