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Hormonal Regulation of Glycogen Synthase and Phosphorylase Activities in Human Polymorphonuclear Leukocytes by Yoshinori Ohtsuka; Takahito Kondo; Yoshikazu Kawakami is a Medicine article available to read on EtoBox.

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Hormonal regulation of glycogen synthase and phosphorylase activities were studied in human polymorphonuclear leukocytes. Polymorphonuclear leukocytes from normal subjects were incubated with glucose, insulin, ΑΖ,-isoproterenol and L-thyroxine, either independently or in different combinations, and changes of the enzyme activity ratios of glycogen synthase (active form (I) / total activity (T)) and glycogen phosphorylase (active form (a) / total activity (T)) were assessed. Neither glucose nor insulin changed the glycogen synthase activity ratio. However, the proportion of the active form (I) of glycogen synthase was increased by the simultaneous addition of glucose and insulin to the incubation mixture, but D,L-isoproterenol or L-thyroxine diminished this effect and caused a decrease in the proportion of the active form of glycogen synthase. Insulin had no effect on the glycogen phosphorylase activity ratio. Glucose decreased the proportion of phosphorylase in the a form. The simultaneous addition of glucose and insulin caused no further changes, whereas in the presence of AL-isoproterenol or L-thyroxine, this glucose effect was abolished and the proportion of phosphorylase a incr

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Author

Yoshinori Ohtsuka; Takahito Kondo; Yoshikazu Kawakami

Published

1988

Language

EN

Field

Medicine (Health Sciences)