Cordycepin-Enriched WIB801C from Cordyceps militaris Inhibits Collagen-Induced [Ca(2+)]i Mobilization via cAMP-Dependent Phosphorylation of Inositol 1, 4, 5-Trisphosphate Receptor in Human Platelets.

In this study, we prepared cordycepin-enriched (CE)-WIB801C, a n-butanol extract of Cordyceps militaris-hypha, and investigated the effect of CE-WIB801C on collagen-induced human platelet aggregation. CE-WIB801C dose-dependently inhibited collagen-induced platelet aggregation, and its IC50 value was 175 μg/ml. CE-WIB801C increased cAMP level more than cGMP level, but inhibited collagen-elevated [Ca(2+)]i mobilization and thromboxane A2 (TXA2) production.

The opposite correlation between calcium ion and cyclic-AMP regarding the activation of microsomal triglyceride transfer protein in rat liver.

In this study, the effects of Ca(2+) and cyclic adenosine monophosphate (cAMP) on microsomal triglyceride (TG) transfer protein (MTP) activity were investigated in rat liver. MTP activity was high when liver contained low levels of cAMP, which was induced by administration of glucose, or high levels of total Ca(2+) and TG. However, MTP activity increased by high levels of Ca(2+) and TG was reduced in a dose-dependent manner by treatment with dibutyryl-cAMP (db-cAMP), a cAMP analogue.

Augmentation of Ca2+-induced microsomal triglyceride transfer protein activity by glucose supply enhances hypertriglyceridemia in vivo.

We have investigated possible roles of intra-glucose supply on microsomal triglyceride (TG) transfer protein (MTP) in the secretion of TG-rich very low-density lipoprotein (VLDL) from the liver. Due to the activation of MTP, TG and apolipoprotein B (apoB) in the liver are assembled into VLDL and then the VLDL is transferred into the blood stream. High MTP activity can increase the release of VLDL into the blood stream, and this would lead high levels of TG and apoB in the blood.

The possible role of Ca2+ on the activation of microsomal triglyceride transfer protein in rat hepatocytes.

Microsomal triglyceride (TG) transfer protein (MTP) is involved in the secretion of TG-rich very low-density lipoprotein (VLDL), a process which leads to the generation of hypertriglyceridemia and atherosclerosis. We investigated the possible role of Ca(2+) on MTP activity in hepatocytes. Exogenous CaCl(2) and calmodulin increased MTP activity dose-dependently, and calcium ionophore A23187 (A23187) also increased total Ca(2+) level and MTP activity in hepatocytes.