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Complex stiffness of smooth muscle cytoplasm in the presence of Ca-activated brevin

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Gailly, Philippe [UCL] Gillis, Jean-Marie [UCL] Capony, J. P.

Brevin, an F-actin severing protein, regulates actin gel-sol transformation in a Ca(2+)-dependent way. Here, we tested its effect on the stiffness of the cytoplasm of skinned smooth muscle, in the absence of actin-myosin interaction (inhibited myosin ATPase). Complex stiffness was measured by imposing sinusoidal stretches and releases at different frequencies (1-50 Hz). In the presence of Ca-activated brevin, the stiffness decreased by about 30%, at all frequencies, from its initial values in Ca-free, relaxing solution. This decrease reflected a fall in both elasticity and viscosity of the cytoplasm. We propose that brevin specifically operates on an actin network in parallel with the contractile apparatus, e.g. on the actin-filamin gel.

Document type Article de périodique (Journal article) – Article de recherche
Publication date 1991
Journal information "Journal of Muscle Research and Cell Motility" - Vol. 12, no. 4, p. 333-339 (1991)
Peer reviewed yes
Publisher Springer Netherlands (Dordrecht)
issn 0142-4319
e-issn 1573-2657
Publication status Publié
Affiliation UCL - MD/FSIO - Département de physiologie et pharmacologie
MESH Subject Actins - metabolism ; Animals ; Calcium - pharmacology ; Colon ; Cytoplasm ; Electric Stimulation ; Gelsolin ; Guinea Pigs ; Mersalyl - pharmacology ; Microfilament Proteins - pharmacology ; Muscle Contraction - drug effects - physiology ; Muscle, Smooth - drug effects - ultrastructure ; Myosins - antagonists & inhibitors ; Potassium Iodide - pharmacology ; Vanadates - pharmacology
Links
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Bibliographic reference Gailly, Philippe ; Gillis, Jean-Marie ; Capony, J. P.. Complex stiffness of smooth muscle cytoplasm in the presence of Ca-activated brevin. In: Journal of Muscle Research and Cell Motility, Vol. 12, no. 4, p. 333-339 (1991)
Permanent URL http://hdl.handle.net/2078.1/11326