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Tyrosine kinase participates in vasoconstriction through a Ca 2+ ‐ and myosin light chain phosphorylation‐independent pathway
Author(s) -
Fang Lian-Hua,
Kwon Seong-Chun,
Zhang Yong-He,
Ahn Hee-Yul
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02235-4
Subject(s) - myosin light chain kinase , phosphorylation , tyrosine phosphorylation , tyrosine kinase , contraction (grammar) , vasoconstriction , chemistry , genistein , protein kinase c , myosin , microbiology and biotechnology , endocrinology , medicine , biology , biochemistry , signal transduction
This study was undertaken to determine the role of tyrosine kinase on intracellular Ca 2+ ([Ca 2+ ] i ), myosin light chain (MLC) phosphorylation, and contraction caused by norepinephrine (NE) in rat aorta. NE induced a sustained contraction with an increase of [Ca 2+ ] 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 [Ca 2+ ] i and MLC phosphorylation. These results suggest that tyrosine kinase may regulate the NE‐mediated contraction without altering [Ca 2+ ] i and MLC phosphorylation in rat aorta.