NDLI: Exogenous caldesmon promotes relaxation of guinea-pig skinned taenia coli smooth muscles: inhibition of cooperative reattachment of latch bridges?

Content Provider	Springer Nature Link
Author	Albrecht, Kerstin Schneider, Alexandra Liebetrau, Claudia Rüegg, J. C. Pfitzer, Gabriele
Copyright Year	1997
Abstract	In smooth muscle, the state of prolonged contraction (latch state) is associated with very slow energy turnover and cycling of crossbridges that are dephosphorylated. A similar state may be reproduced in skinned fibres when the calcium-induced contraction is terminated by calcium removal with ethylenebis(oxonitrilo)tetraacetate (EGTA) and, during the slow relaxation that follows, force is maintained by dephosphorylated crossbridges that cycle slowly or not at all and may cooperatively reattach after detachment (Khromov et al. 1995, Biophys J 69:2611–2622). In guinea-pig skinned taenia coli that has been pretreated by prolonged incubation with caldesmon (5 μM), the rate of relaxation is approximately 1.6 times greater than in untreated controls, with half-times of relaxation being 1.3 and 2.1 min, respectively. In contrast, preloading the fibres with calponin does not accelerate relaxation. Preloading the fibres with caldesmon also accelerates the relaxation of skinned fibres from the state of rigor contraction when the latter is terminated by immersion into an ATP-containing relaxing solution or, in the presence of inorganic phosphate (Pi), also by flash-photolytic release of ATP from caged-ATP. Even in the latter case, relaxation is comparatively slow, possibly because of cooperative reattachment of dephosphorylated crossbridges which delays net crossbridge detachment and hence relaxation. We propose that by inhibition of cooperative reattachment caldesmon accelerates relaxation, even in the presence of Pi, and that the latch-like state of skinned fibres is supported by dephosphorylated cooperatively attaching crossbridges and may be regulated by the activity of caldesmon in the smooth muscle cell.
Starting Page	534
Ending Page	542
Page Count	9
File Format	PDF
ISSN	00316768
Journal	Pflügers Archiv
Volume Number	434
Issue Number	5
e-ISSN	14322013
Language	English
Publisher	Springer-Verlag
Publisher Date	1997-08-11
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Clinical Biochemistry

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