FEBS Letters | |
Interaction of smooth muscle caldesmon with S‐100 protein | |
Gusev, Nikolai B.1  Skripnikova, Elena V.1  | |
[1] Department of Biochemistry, School of Biology, Moscow State University, Moscow 119899, USSR | |
关键词: Caldesmon; Calmodulin; Protein; S-100; Protein kinase C phosphorylation; HMM; heavy meromyosin; | |
DOI : 10.1016/0014-5793(89)81577-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The interaction of caldesmon with certain Ca-binding proteins was investigated by means of electrophoresis under non-denaturating conditions. In the presence of Ca2+ calmodulin, troponin C and S-100 protein form a complex with caldesmon. No complex formation takes place in the absence of Ca2+. Lactalbumin and pike parvalbumin (pI4.2) do not interact with caldesmon independently of Ca-concentration. Both S-100 protein and calmodulin effectively inhibit phosphorylation of caldesmon by Ca-phospholipid-dependent protein kinase. At low ionic strength S-100 protein reverses the inhibitory action of caldesmon on the skeletal muscle acto-heavy meromyosin ATPase more effectively than calmodulin. It is supposed that in certain tissues and cell compartments the proteins belonging to the S-100 family are able to substitute for calmodulin in the caldesmondependent regulation of actin and myosin interaction.
【 授权许可】
Unknown
【 预 览 】
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