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Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres

Jaworowski, Åsa; Anderson, Kurt I; Arner, Anders LU ; Engström, Martin LU ; Gimona, Mario; Strasser, Peter and Small, J Victor (1995) In FEBS Letters 365(2-3). p.167-171
Abstract
Calponin (4.1-5.9 microM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20-25% with only minor influence on force in skinned smooth muscle from guinea-pig taenia coli activated at different Ca2+ levels and with thiophosphorylation. Similar results were obtained with a fragment of the N-terminal 1-228 amino acids engineered using a mouse cDNA construct (5.4 microM). Both the native calponin and the fragment inhibited actin filament sliding in a graded manner in an in vitro motility assay. We conclude that calponin influences the kinetics of the actin-myosin interaction in the organised smooth muscle contractile system and that engineered fragments of calponin can be used to probe its action in muscle fibres. The effects can... (More)
Calponin (4.1-5.9 microM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20-25% with only minor influence on force in skinned smooth muscle from guinea-pig taenia coli activated at different Ca2+ levels and with thiophosphorylation. Similar results were obtained with a fragment of the N-terminal 1-228 amino acids engineered using a mouse cDNA construct (5.4 microM). Both the native calponin and the fragment inhibited actin filament sliding in a graded manner in an in vitro motility assay. We conclude that calponin influences the kinetics of the actin-myosin interaction in the organised smooth muscle contractile system and that engineered fragments of calponin can be used to probe its action in muscle fibres. The effects can be due to an introduction of an internal load during filament sliding, possibly by decreasing the detachment rates and increasing the cross-bridge time spent in the attached state. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Calponin, Motility assay, in vitro, Shortening velocity, Smooth muscle
in
FEBS Letters
volume
365
issue
2-3
pages
167 - 171
publisher
Wiley-Blackwell
external identifiers
  • pmid:7781773
  • scopus:0029008415
ISSN
1873-3468
DOI
10.1016/0014-5793(95)00451-E
language
English
LU publication?
yes
id
167c4390-dfd7-4870-ba28-a3182c54c325 (old id 1109127)
date added to LUP
2008-07-25 14:06:11
date last changed
2017-08-20 04:29:54
@article{167c4390-dfd7-4870-ba28-a3182c54c325,
  abstract     = {Calponin (4.1-5.9 microM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20-25% with only minor influence on force in skinned smooth muscle from guinea-pig taenia coli activated at different Ca2+ levels and with thiophosphorylation. Similar results were obtained with a fragment of the N-terminal 1-228 amino acids engineered using a mouse cDNA construct (5.4 microM). Both the native calponin and the fragment inhibited actin filament sliding in a graded manner in an in vitro motility assay. We conclude that calponin influences the kinetics of the actin-myosin interaction in the organised smooth muscle contractile system and that engineered fragments of calponin can be used to probe its action in muscle fibres. The effects can be due to an introduction of an internal load during filament sliding, possibly by decreasing the detachment rates and increasing the cross-bridge time spent in the attached state.},
  author       = {Jaworowski, Åsa and Anderson, Kurt I and Arner, Anders and Engström, Martin and Gimona, Mario and Strasser, Peter and Small, J Victor},
  issn         = {1873-3468},
  keyword      = {Calponin,Motility assay,in vitro,Shortening velocity,Smooth muscle},
  language     = {eng},
  number       = {2-3},
  pages        = {167--171},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres},
  url          = {http://dx.doi.org/10.1016/0014-5793(95)00451-E},
  volume       = {365},
  year         = {1995},
}