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Biokhimiia ; 55(9): 1578-83, 1990 Sep.
Article in Russian | MEDLINE | ID: mdl-1706630

ABSTRACT

The dependence of Ca2+ transport in synaptosomes along the channels formed by alpha-latrotoxin on [Ca2+]in and the feasibility of transport along these channels of other bivalent cations were studied. It was found that the concentration dependence of Ca2+ influx is nonlinear and is described by the Michaelis-Menten kinetics (Km = 1.07 +/- 0.19 mM). Mg2+, Ba2+, Sr2+, Mn2+ and Co2+ competitively inhibited the Ca2+ influx via latrotoxin channels. Studies with the use of the fluorescent Ca2+ probes, Quin-2 and Fura-2, revealed that these cations can also penetrate inside synaptosomes via latrotoxin channels. The bivalent cation influx via latrotoxin channels caused a decrease of the membrane potential of synaptosomes. The similarity of properties of latrotoxin and endogenous Ca2+ channels is discussed.


Subject(s)
Calcium/metabolism , Ion Channels/metabolism , Spider Venoms/metabolism , Aminoquinolines , Biological Transport , Cations, Divalent/metabolism , Fluorescent Dyes , Fura-2 , Kinetics , Permeability , Synaptosomes/metabolism
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