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Binding of [ 3 H]Nitrendipine to Proteins in the Plasma Membrane of Sea Urchin Sperm
Author(s) -
MikamiTakei Kaori,
Yasumasu Ikuo
Publication year - 1989
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.1989.00581.x
Subject(s) - nitrendipine , hemicentrotus , nifedipine , chemistry , diltiazem , membrane , sea urchin , biophysics , biochemistry , calcium , biology , microbiology and biotechnology , organic chemistry
The plasma membrane fractions of the sperm of four species of sea urchin, obtained by the method by Podell et al. (24), gave similar electrophoretic profiles of proteins. Several proteins in the membrane fraction from Hemicentrotus pulcherrimus bound [ 3 H]nitrendipine, a specific antagonist of voltage‐dependent Ca 2+ channels, added at concentration of about 10 4 times those reported to be effective in muscle and nerve cells. Nifedipine, a close analogue of nitrendipine, decreased the bindings of [ 3 H]nitrendipine to 210, 140, 130 and 110 kDa and increased its bindings to several other proteins. Diltiazem, another type of Ca 2+ channel blocker, enhanced the bindings of [ 3 H]nitrendipine to proteins of 210, 140, 130 and 110 kDa, and decreased its bindings to the other proteins. This effect of diltiazem on the binding of [ 3 H]nitrendipine to proteins in the membrane fraction was similar to its effect on the mammalian excitable membrane fraction. The proteins whose binding to [ 3 H]nitrendipine was blocked by nifedipine and enhanced by diltiazem are Ca 2+ channels.