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Published on: January 24, 2017
Inhibition of the mitochondrial calcium uniporter by antibodies against a 40-kDa glycoproteinT
N E Saris1, T V Sirota, I Virtanen
1Department of Medical Chemistry, University of Helsinki, Finland.
Polyclonal rabbit antibodies against a Ca(2+)-binding mitochondrial glycoprotein were found to inhibit the uniporter-mediated transport of Ca2+ in mitoplasts prepared from rat liver mitochondria. Spermine, a modulator of the uniporter, decreased the inhibition. This glycoprotein of M(r) 40,000, isolated from beef heart mitochondria and earlier shown to form Ca(2+)-conducting channels in black-lipid membranes, thus is a good candidate for being a component of the uniporter. Antibody-IgG was found to specifically bind to mitochondria in human fibroblasts.
Polyclonal rabbit antibodies against a Ca(2+)-binding mitochondrial glycoprotein were found to inhibit the uniporter-mediated transport of Ca2+ in mitoplasts prepared from rat liver mitochondria. Spermine, a modulator of the uniporter, decreased the inhibition. This glycoprotein of M(r) 40,000, isolated from beef heart mitochondria and earlier shown to form Ca(2+)-conducting channels in black-lipid membranes, thus is a good candidate for being a component of the uniporter. Antibody-IgG was found to specifically bind to mitochondria in human fibroblasts.
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