Inhibition of the mitochondrial calcium uniporter by antibodies against a 40-kDa glycoproteinT.

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.