Key result
ATP-dependent potassium channels localize to mitochondrial, ER, and SR membranes in rat heart and liver.
Why the study?
The cellular localization of the protein forming ATP-dependent potassium-selective channels in bilayer lipid membranes was not well characterized.
Answers are grounded in this paper and cite their sources.
Mitochondrial and SR localization in rat heart may inform bioenergetic research; leaves open any clinical relevance pending functional validation.
The localization in the cell of the protein forming the ATP-dependent potassium-selective channels in the bilayer lipid membrane has been studied. The electron microscope investigation of rat liver and heart tissue sections after their incubation with Abs against this protein and the visualization of the protein with secondary Abs conjugated with colloid gold were carried out. Colloid gold particles were observed both in mitochondrial membranes and in membranes of endoplasmic and sarcoplasmic reticulum. In heart mitochondria, these particles were significantly greater than in liver mitochondria. The localization of the channel protein both in mitochondria and reticulum, as well as the structural similarity between the mitochondrial channel and the precursor of calreticulin suggest that the channel protein belongs to the family of calreticulins. The possible function of the protein as a channel subunit of the mitochondrial ATP-dependent potassium channel is discussed.
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Pavlik et al. (2010) studied this question. Antibodies against ATP-dependent potassium-selective channel protein was evaluated on Localization of the channel protein. The ATP-dependent potassium-selective channel protein was localized in mitochondrial, endoplasmic, and sarcoplasmic reticulum membranes of rat liver and heart tissues.
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