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Calponin reduces sh...
Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres
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Jaworowski, Åsa (author)
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Anderson, Kurt I (author)
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- Arner, Anders (author)
- Lund University,Lunds universitet,Kärlfysiologi,Forskargrupper vid Lunds universitet,Vascular Physiology,Lund University Research Groups
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- Engström, Martin (author)
- Lund University,Lunds universitet,Anestesiologi och intensivvård,Sektion II,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Anesthesiology and Intensive Care,Section II,Department of Clinical Sciences, Lund,Faculty of Medicine
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Gimona, Mario (author)
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Strasser, Peter (author)
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Small, J Victor (author)
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(creator_code:org_t)
- 1995
- 1995
- English.
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In: FEBS Letters. - 1873-3468. ; 365:2-3, s. 167-171
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http://dx.doi.org/10...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Calponin
- Motility assay
- in vitro
- Shortening velocity
- Smooth muscle
Publication and Content Type
- art (subject category)
- ref (subject category)
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