Interaction of smooth muscle caldesmon with S‐100 protein

FEBS Letters

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