Inhibition of myosin light chain kinase by amiloride.

Abstract:

:Phosphorylation of regulatory light chain (LC20) by myosin light chain kinase (MLCK) has been thought to play an important role in both smooth muscle contraction and several functions of vertebrate non-muscle cells. Amiloride, a frequently used Na+/H+ exchange inhibitor, potently inhibited phosphorylation of LC20 by MLCK. The inhibition was non-competitive with respect to myosin but competitive with ATP (Ki = 0.95 microM), suggesting that amiloride may act as an ATP analogue. Amiloride also inhibited the tension development of ether-treated gizzard fibers which were lacking in Na+/H+ antiport, even in the presence of ATP regenerating system. Thus, it must be reminded that amiloride cannot be used as a specific inhibitor of Na+/H+ exchange, and that the inhibition of myosin phosphorylation by amiloride should be taken into consideration in studying the role of Na+/H+ antiport in the cellular function.

authors

Higashihara M

doi

10.1016/0006-291x(89)90808-5

subject

Has Abstract

pub_date

1989-08-15 00:00:00

pages

1253-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)90808-5

journal_volume

162

pub_type

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