DOI . ORG {
}
Title[redir]:
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
Description:
A mitochondrial hydrophobic component that forms Ca2+-induced nonspecific ion channels in black-lipid membranes (Mironova et al., 1997) has been purified and its nature elucidated. It consists of long-chain saturated fatty acids—mainly palmitic and stearic. These fatty acids, similar to the mitochondrial hydrophobic component, bind Ca2+ with high affinity in comparison with unsaturated fatty acids, saturated fatty acids with shorter aliphatic chains, phospholipids, and other lipids. Ca2+-binding is inhibited by Mg2+ but not by K+. For palmitic acid, the K d for Ca2+ was 5 μM at pH 8.5 and 15 μM at pH 7.5, with the B max of 0.48 ± 0.08 mmol/g. This corresponds to one Ca2+ ion for eight palmitic acid molecules. The data of IR spectroscopy confirm that Ca2+ does not form ionic bonds with palmitic and stearic acids under hydrophobic conditions. It has been found that in the presence of Ca2+, palmitic and stearic acids, but not unsaturated FFA induce a nonspecific permeability in black-lipid membranes. Addition of Ca2+ in order to induce the permeability transition, increases the extractable amount of palmitic and stearic acids, the effect being prevented by a phospholipase A2 inhibitor. The possible involvement of palmitic and stearic acids in the mitochondrial nonspecific permeability is discussed.
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Keywords {🔍}
google, scholar, article, palmitic, acids, biol, biophys, mitochondrial, stearic, chem, saris, biochem, privacy, cookies, content, data, journal, nonspecific, blacklipid, mironova, gateauroesch, levrat, louisot, fatty, acid, permeability, publish, search, channels, membranes, ion, nature, access, biochemistry, biochim, acta, arch, log, research, bind, high, affinity, form, pavlov, lazareva, hydrophobic, lipids, phospholipase, mitochondria, discover,
Topics {✒️}
phospholipase a2 inhibitor ca2+-activated mitochondrial pores black-lipid membranes month download article/chapter saturated fatty acids ca2+ ion interactions form nonspecific channels mitochondrial nonspecific permeability unsaturated fatty acids privacy choices/manage cookies ω-hydroxypalmitic acid palmitic acid molecules full article pdf mitochondrial hydrophobic component ca2+-binding related subjects ca2+ ion fatty acids european economic area shorter aliphatic chains ir spectroscopy confirm form ionic bonds infrared absorption spectroscopy nankodo company limited ca2+-dependent permeabilization check access instant access liver mitochondria odile gateau-roesch conditions privacy policy palmitic acid accepting optional cookies unsaturated ffa induce /www/radiolig/radiolig1 journal finder publish main content log nonspecific permeability permeability transition article journal mitochondria bind ca2+ stearic acids article log nature elucidated privacy policy personal data article mironova books a article cite gateau-roesch
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headline:Palmitic and Stearic Acids Bind Ca2+ with High Affinity and Form Nonspecific Channels in Black-Lipid Membranes. Possible Relation to Ca2+-Activated Mitochondrial Pores
description:A mitochondrial hydrophobic component that forms Ca2+-induced nonspecific ion channels in black-lipid membranes (Mironova et al., 1997) has been purified and its nature elucidated. It consists of long-chain saturated fatty acids—mainly palmitic and stearic. These fatty acids, similar to the mitochondrial hydrophobic component, bind Ca2+ with high affinity in comparison with unsaturated fatty acids, saturated fatty acids with shorter aliphatic chains, phospholipids, and other lipids. Ca2+-binding is inhibited by Mg2+ but not by K+. For palmitic acid, the K
d for Ca2+ was 5 μM at pH 8.5 and 15 μM at pH 7.5, with the B
max of 0.48 ± 0.08 mmol/g. This corresponds to one Ca2+ ion for eight palmitic acid molecules. The data of IR spectroscopy confirm that Ca2+ does not form ionic bonds with palmitic and stearic acids under hydrophobic conditions. It has been found that in the presence of Ca2+, palmitic and stearic acids, but not unsaturated FFA induce a nonspecific permeability in black-lipid membranes. Addition of Ca2+ in order to induce the permeability transition, increases the extractable amount of palmitic and stearic acids, the effect being prevented by a phospholipase A2 inhibitor. The possible involvement of palmitic and stearic acids in the mitochondrial nonspecific permeability is discussed.
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Palmitic acid
calcium binding
mitochondria
CsA-insensitive pore
ion channel
black-lipid membrane
phospholipase A2
Bioorganic Chemistry
Biochemistry
general
Animal Anatomy / Morphology / Histology
Animal Biochemistry
Organic Chemistry
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description:A mitochondrial hydrophobic component that forms Ca2+-induced nonspecific ion channels in black-lipid membranes (Mironova et al., 1997) has been purified and its nature elucidated. It consists of long-chain saturated fatty acids—mainly palmitic and stearic. These fatty acids, similar to the mitochondrial hydrophobic component, bind Ca2+ with high affinity in comparison with unsaturated fatty acids, saturated fatty acids with shorter aliphatic chains, phospholipids, and other lipids. Ca2+-binding is inhibited by Mg2+ but not by K+. For palmitic acid, the K
d for Ca2+ was 5 μM at pH 8.5 and 15 μM at pH 7.5, with the B
max of 0.48 ± 0.08 mmol/g. This corresponds to one Ca2+ ion for eight palmitic acid molecules. The data of IR spectroscopy confirm that Ca2+ does not form ionic bonds with palmitic and stearic acids under hydrophobic conditions. It has been found that in the presence of Ca2+, palmitic and stearic acids, but not unsaturated FFA induce a nonspecific permeability in black-lipid membranes. Addition of Ca2+ in order to induce the permeability transition, increases the extractable amount of palmitic and stearic acids, the effect being prevented by a phospholipase A2 inhibitor. The possible involvement of palmitic and stearic acids in the mitochondrial nonspecific permeability is discussed.
datePublished:
dateModified:
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pageEnd:331
sameAs:https://doi.org/10.1023/A:1010659323937
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Palmitic acid
calcium binding
mitochondria
CsA-insensitive pore
ion channel
black-lipid membrane
phospholipase A2
Bioorganic Chemistry
Biochemistry
general
Animal Anatomy / Morphology / Histology
Animal Biochemistry
Organic Chemistry
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