ArticleJournal of bioenergetics and biomembranes2000
Calcium-binding properties of the mitochondrial channel-forming hydrophobic component.
Article in Journal of bioenergetics and biomembranes, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Review
- Inorganic polyphosphate (polyP) as an activator and structural component of the mitochondrial permeability transition pore.Biochemical Society transactions · 2016Review
- Formation of palmitic acid/Ca2+ complexes in the mitochondrial membrane: a possible role in the cyclosporin-insensitive permeability transition.Journal of bioenergetics and biomembranes · 2004Article
- Palmitic and stearic acids bind Ca2+ with high affinity and form nonspecific channels in black-lipid membranes. Possible relation to Ca2+-activated mitochondrial pores.Journal of bioenergetics and biomembranes · 2001Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A hydrophobic, low-molecular weight component extracted from mitochondria forms a Ca2+-activated ion channel in black-lipid membranes (Mironova et al., 1997). At pH 8.3-8.5, the component has a high-affinity binding site for Ca2+ with a Kd of 8 x 10(-6) M, while at pH 7.5 this Kd was decreased to 9 x 10(-5) M. Bmax for the Ca2+-binding site did not change significantly with pH. In the range studied, 0.2 +/- 0.06 mmol Ca2+/g component were bound or one calcium ion to eight molecules of the component. The Ca2+ binding was strongly decreased by 50-100 mM Na+, but not by K+. Treatment of mitochondria with CaCl2 prior to ethanolic extraction resulted in a high level of Ca2+-binding capacity of the partially purified component. Cyclosporin A, a specific inhibitor of the mitochondrial permeability transition, when added to the mitochondrial suspension, decreased the Ca2+-binding activity of the purified extract severalfold. The calcium-binding capability of the partially purified component correlates with its calcium-channel activity. This indicates that the channel-forming component might be involved in the permeability transition that stimulates its formation.
Indexed as
Identifiers
11768755What OpenQuestion holds
Registered trials
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