Tyrosine kinase participates in vasoconstriction through a Ca2+‐ and myosin light chain phosphorylation‐independent pathway

FEBS Letters

Zhang, Yong-He³  Kwon, Seong-Chun¹  Ahn, Hee-Yul²  Fang, Lian-Hua² 

[1]Department of Physiology, College of Medicine, Yonsei University, Seoul 120-752, South Korea

[2]Department of Pharmacology, College of Medicine, Chungbuk National University, Cheongju 361-763, South Korea

[3]Department of Pharmacology, School of Basic Medical Science, Peking University, Beijing, P.R. China

关键词: Genistein;    Tyrphostin 25;    Norepinephrine;    Ca2+;    Myosin light chain;    Tyrosine kinase;    NE;    norepinephrine;    MLC;    myosin light chain;   

DOI  :  10.1016/S0014-5793(02)02235-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This study was undertaken to determine the role of tyrosine kinase on intracellular Ca²⁺ ([Ca²⁺]_i), myosin light chain (MLC) phosphorylation, and contraction caused by norepinephrine (NE) in rat aorta. NE induced a sustained contraction with an increase of [Ca²⁺]_i. On the other hand, NE increased the phosphorylation of the 20 kDa MLC transiently. Pretreatment with genistein and tyrphostin 25, tyrosine kinase inhibitors, significantly inhibited NE-induced contraction, but did not affect the increase of [Ca²⁺]_i and MLC phosphorylation. These results suggest that tyrosine kinase may regulate the NE-mediated contraction without altering [Ca²⁺]_i and MLC phosphorylation in rat aorta.

【 授权许可】

Unknown