The effects of phenothiazines and other calmodulin antagonists on the sarcoplasmic and endoplasmic reticulum Ca(2+) pumps.

The effects of a number of phenothiazines and other calmodulin antagonists on the Ca(2+)-ATPase activity of sarcoplasmic reticulum (SR) and endoplasmic reticulum (ER) were investigated. The drugs used in this study were trifluoperazine, calmidazolium, fluphenazine, chlorpromazine, W-7, and calmodulin-binding peptide. Our results showed that calmidazolium and calmodulin-binding peptide were the most potent inhibitors of skeletal muscle SR Ca(2+)-ATPase activity (isoform SERCA 1) (IC(50) values of 0.

The mycotoxin paxilline inhibits the cerebellar inositol 1,4, 5-trisphosphate receptor.

Paxilline, a tremorgenic alkaloid mycotoxin produced by Penicillium paxilline, is a reversible inhibitor of the cerebellar inositol 1,4, 5-trisphophate (InsP(3)) receptor. It inhibits the amount or extent of InsP(3)-induced Ca(2+) release (IICR), at sub-maximal concentrations of InsP(3), in a biphasic manner consistent with two inhibition constants (K(i)'s 6.7 and > or =400 microM).

Critical evaluation of ECV304 as a human endothelial cell model defined by genetic analysis and functional responses: a comparison with the human bladder cancer derived epithelial cell line T24/83.

Early reports indicated that ECV304 was a spontaneously-transformed line derived from a Japanese human umbilical vein endothelial cells (HUVEC) culture. Many morphological, immunochemical, and genetic studies provided further evidence that ECV304 was a valuable biomedical research tool and could be used to study processes that include angiogenesis in vitro and signal transduction by a variety of G protein-coupled receptors. However, several distinct differences between ECV304 and HUVEC are now apparent and recent reports have indicated genetic similarity between ECV304 and T24/83, a human bladder cancer cell line.

The mechanism of inhibition of the Ca2+-ATPase by mastoparan. Mastoparan abolishes cooperative ca2+ binding.

The amphiphilic peptide mastoparan, isolated from wasp venom, is a potent inhibitor of the sarcoplasmic reticulum Ca2+-ATPase. At pH 7. 2, ATPase activity is inhibited with an inhibitory constant (Ki) of 1 +/- 0.

Biochemical mechanisms of calcium mobilisation induced by mastoparan and chimeric hormone-mastoparan constructs.

Ca2+ efflux, Ca(2+)-ATPase, and membrane permeability measurements were used to investigate the biochemical mechanisms of Ca2+ release induced by mastoparan (MP) and the chimeric hormone-MP constructs incorporating galanin (galparan) or vasopressin antagonist (M375 and M391) moieties. Comparative studies utilised preparations of porcine cerebellar microsomes and rabbit skeletal muscle sarcoplasmic reticulum (SR). MP and chimeric peptides galparan, M375 and M391 induce Ca2+ release over a range of concentrations from 0.