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