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2019/02/18
Toxicological Evaluation of SiO2 Nanoparticles by Zebrafish Embryo Toxicity Test

2018/12/27
Increased susceptibility to oxidative stress-induced toxicological evaluation by genetically modified nrf2a-deficient zebrafish.

2018/01/18
EGF receptor kinase suppresses ciliogenesis through activation of USP8 deubiquitinase

2017/11/23
Chemokines protect vascular smooth muscle cells from cell death induced by cyclic mechanical stretch.

2017/07/29
New photic stimulating system with white light-emitting diodes to elicit electroretinograms from zebrafish larvae.

tCa2+-dependent Inhibition of Actin-activated Myosin Atpase Activity by S100C(S100A11), A Novel Member of the S100 Protein Family.

                     
2000/01/01

Xiao Qing Zhao, Michiko Naka and Toshio Tanaka
Biochem. Biophys. Res. Commun. 267 77-79 2000

Abstract

S100C (S100A11, calgizzarin) inhibits the actin-activated myosin Mg(2+)-ATPase activity of smooth muscle in a dose-dependent manner: its half-maximal effect occurs at a S100C/actin molar ratio of 0.05 and its maximal effect occurs at a ratio of 0.20. Furthermore, S100C was found to bind to actin with a stoichiometry of 1:6-7 in the presence of Ca(2+), with an affinity of 1 x 10(-6) M determined by cosedimentation assays. Other Ca(2+)-binding proteins such as S100A1, S100A2, S100B, and calmodulin did not inhibit actin-activated myosin Mg(2+)-ATPase activity. Calmodulin, S100A1, and S100B reversed the inhibitory effect of calponin in a Ca(2+)-dependent manner, S100A2 had no effect, and S100C had additional inhibitory effects. The results suggest that S100C might be involved in the regulation of actin-activated myosin Mg(2+)-ATPase activity through its Ca(2+)-dependent interaction with actin filaments.

Copyright 2000 Academic Press.