2019/03/18
Zebrafish yolk sac microinjection of thalidomide for assessment of developmental toxicology
2019/02/18
Toxicological Evaluation of SiO2 Nanoparticles by Zebrafish Embryo Toxicity Test
2018/01/18
EGF receptor kinase suppresses ciliogenesis through activation of USP8 deubiquitinase
Ichikawa K, Ito M, Okubo S, Konishi T, Nakano T, Mino T, Nakamura F, Naka M, Tanaka T.
Biochem Biophys Res Commun. 1993 Jun 30;193(3):827-33.
Abstract
Smooth muscle myosin bound phosphatase (MBP) purified from chicken gizzard, which is a holoenzyme of type 1 delta protein phosphatase and dephosphorylated intact myosin, catalyzed the dephosphorylation of calponin phosphorylated by protein kinase C (PK-C). The Km of MBP for calponin was 0.6 microM and the Vmax was 350 nmol/min/mg. All of the multiple sites of phosphorylation by PK-C of calponin were completely dephosphorylated by MBP. Functionally, calponin dephosphorylated by MBP recovered its inhibitory effect on the actin-activated Mg(2+)-ATPase activity of myosin. Therefore, these results suggest that a type 1 delta protein phosphatase causes relaxation of smooth muscle by the dephosphorylation not only of myosin but also of calponin.