Open AccessPossible Involvement of Calmodulin and the Cytoskeleton in Electrofusion of Plant Protoplasts
Author(s) -
Shunnosuke Abe,
Jun Takeda
Publication year - 1986
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.81.4.1151
Subject(s) - calmodulin , electrofusion , trifluoperazine , verapamil , cytochalasin b , channel blocker , egta , hordeum vulgare , cytochalasin , biology , staurosporine , biophysics , microfilament , biochemistry , calcium , chemistry , cytoskeleton , protein kinase c , botany , kinase , cell , materials science , poaceae , organic chemistry , metallurgy , enzyme
Calmodulin antagonists, trifluoperazine, chlorpromazine, calmidazolium, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), strongly inhibited the electrofusion of barley (Hordeum vulgare L. cv Moor) protoplasts with a marked increase of broken fusion products, after 60 minutes of incubation. W-5, a dechlorinated analog of W-7, was found less effective for the inhibition than W-7. Ethyleneglycol-bis(beta- aminoethylether)-N,N'-tetraacetic acid a Ca(2+) chelator, La(3+), a surface Ca(2+) antagonist, and verapamil, a Ca(2+) channel blocker, also inhibited electrofusion. Dielectrophoresis was inhibited by La(3+). A microtubule inhibitor, vinblastine, inhibited electrofusion strongly while colchicine, slightly. A microfilament inhibitor, cytochalasin B, promoted fused cells to become spherical while phalloidin did not affect electrofusion.