Calcium-dependent action of hypertrehalosemic hormone on activation of glycogen phosphorylase in cockroach fat body.

Abstract:

:Signaling mechanisms for Blaberus discoidalis hypertrehalosemic hormone (Bld-HrTH)-dependent glycogen phosphorylase activation were investigated in vitro using fat body of the tropical cockroach, B. discoidalis. Brief treatment of fat bodies with Bld-HrTH in the absence of extracellular Ca2+ showed a significant activation of phosphorylase. Although extracellular Ca2+ was required for a full activation of phosphorylase by Bld-HrTH, stimulation in the absence of extracellular Ca2+ suggested that intracellular Ca2+ was also involved in Bld-HrTH signal transduction. Thapsigargin and thimerosal mobilize Ca2+ from intracellular stores by different mechanisms, and both chemicals stimulated phosphorylase activities as effectively as a maximum dose of Bld-HrTH. Bld-HrTH likely induces intracellular Ca2+ release followed by extracellular Ca2+ entry across the plasma membrane. Inositol-1,4,5-trisphosphate (InsP3) levels were greatly increased by Bld HrTH in a time- and dose-dependent manner, suggesting that InsP3 might be a Ca(2+)-mobilizing intracellular second messenger for Bld-HrTH.

journal_name

Mol Cell Endocrinol

authors

Park JH,Keeley LL

doi

10.1016/0303-7207(95)03715-2

subject

Has Abstract

pub_date

1996-02-05 00:00:00

pages

199-205

issue

2

eissn

0303-7207

issn

1872-8057

pii

0303720795037152

journal_volume

116

pub_type

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