DIFFERENTIAL-EFFECTS OF A K-CHAIN PHOSPHORYLATION IN RELAXATION OF ENDOTHELIN-1-CONTRACTED TRACHEAL SMOOTH-MUSCLE( CHANNEL AGONIST AND CA2+ANTAGONISTS ON MYOSIN LIGHT)

Citation
Ss. Katoch et al., DIFFERENTIAL-EFFECTS OF A K-CHAIN PHOSPHORYLATION IN RELAXATION OF ENDOTHELIN-1-CONTRACTED TRACHEAL SMOOTH-MUSCLE( CHANNEL AGONIST AND CA2+ANTAGONISTS ON MYOSIN LIGHT), Pflugers Archiv, 433(4), 1997, pp. 472-477
Citations number
36
Categorie Soggetti
Physiology
Journal title
ISSN journal
00316768
Volume
433
Issue
4
Year of publication
1997
Pages
472 - 477
Database
ISI
SICI code
0031-6768(1997)433:4<472:DOAKPI>2.0.ZU;2-6
Abstract
Smooth muscle contraction and relaxation are generally considered to b e associated with phosphorylation and dephosphorylation of the 20-kDa regulatory myosin light chain (LC(20)). Thus, contractions of lamb tra cheal smooth muscle induced by Bay K 8644 and relaxed by calcium chann el blockers (verapamil, D-600 and nitrendipine) are accompanied by an increase and decrease, respectively, of LC(20) phosphorylation. Simila rly, endothelin-1 (ET-1) induces a sustained contraction, which is cou pled with elevated LC(20) phosphorylation and reversed by LC(20) depho sphorylation after application of a potassium channel agonist (EMD 526 92). In contrast, calcium channel blockers relax ET-1-induced contract ion without any dephosphorylation of myosin light chains (MLC), sugges ting that MLC phosphatase is inhibited in this case. Obviously, MLC de phosphorylation is not a prerequisite for smooth muscle relaxation. Th e variable relationship between MLC phosphorylation and force during r elaxation suggests that there are mechanisms other than MLC phosphoryl ation that are important for regulation of contraction and relaxation in smooth muscle.