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Research Database PMU-SQQUID

Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres.
Jaworowski, A; Anderson, KI; Arner, A; Engström, M; Gimona, M; Strasser, P; Small, JV;
FEBS Lett. 1995; 365(2-3): 167-171.
Originalarbeiten (Zeitschrift)

PMU-Authors

Gimona Mario
Strasser Peter

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.


Useful keywords (using NLM MeSH Indexing)

Actins/metabolism

Animals

Calcium/metabolism

Calcium-Binding Proteins/pharmacology*

Colon/drug effects

Colon/physiology*

Dose-Response Relationship, Drug

Isometric Contraction/drug effects*

Microfilament Proteins

Muscle Fibers, Skeletal/drug effects

Muscle Fibers, Skeletal/physiology*

Muscle Proteins/pharmacology

Muscle, Skeletal/physiology

Muscle, Smooth/drug effects

Muscle, Smooth/physiology*

Myosins/metabolism

Peptide Fragments/pharmacology

Stomach

Swine

Time Factors


Find related publications in this database (Keywords)

CALPONIN
MOTILITY ASSAY, IN VITRO
SHORTENING VELOCITY
SMOOTH MUSCLE