Involvement of calponin and caldesmon in sustained contraction of arterial smooth muscle.

Abstract:

:The molecular mechanism of smooth muscle contraction was approached by a novel method, covalent 14C-labeling. Intra- and intermolecular protein interactions during contractile activity are reflected by changed reactivity of protein side chains; these can be detected by reagents which readily permeate through the muscle membrane without affecting the contractility and form covalent bonds with proteins in the muscle. The incorporation of 14CH2ICONH2 into proteins of 1-hour histamine contracted versus resting porcine carotid arterial muscles was determined. Out of fourteen 14C-labeled proteins analyzed, only two showed a change in reactivity during sustained contraction. The incorporation of 14CH2ICONH2 into calponin and caldesmon in contracted muscles was about 66% of that into these same proteins in resting muscles. A transformation of calponin and caldesmon molecules from an extended to a more compact conformation explains the decreased reactivity.

authors

Bárány K,Polyák E,Bárány M

doi

10.1016/0006-291x(92)91274-t

subject

Has Abstract

pub_date

1992-09-16 00:00:00

pages

847-52

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91274-T

journal_volume

187

pub_type

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