Binding of 25-hydroxycholesterol and cholesterol to different cytoplasmic proteins

Kandutsch, Andrew A.; Chen, Harry W.; Shown, Elaine P.

doi:10.1073/pnas.74.6.2500

Cited by 64 publications

(19 citation statements)

References 27 publications

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“…OSBP, the canonical mammalian ORP, was originally identified as a cytosolic protein that binds oxysterols (10,11), which are oxygenated derivatives of cholesterol and are important regulators of cholesterol metabolism (12). OSBP is representative of the larger ORP superfamily that is conserved from yeast to man (13)(14)(15)(16), and as discussed below, these proteins bind a variety of sterols.…”

Section: Osh Proteins: Non-vesicular Stps?mentioning

confidence: 99%

A Detour for Yeast Oxysterol Binding Proteins

Beh

McMaster

Kozminski

et al. 2012

Journal of Biological Chemistry

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Oxysterol binding protein-related proteins, including the yeast proteins encoded by the OSH gene family (OSH1-OSH7), are implicated in the non-vesicular transfer of sterols between intracellular membranes and the plasma membrane. In light of recent studies, we revisited the proposal that Osh proteins are sterol transfer proteins and present new models consistent with known Osh protein functions. These models focus on the role of Osh proteins as sterol-dependent regulators of phosphoinositide and sphingolipid pathways. In contrast to their posited role as non-vesicular sterol transfer proteins, we propose that Osh proteins coordinate lipid signaling and membrane reorganization with the assembly of tethering complexes to promote molecular exchanges at membrane contact sites.

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Section: Osh Proteins: Non-vesicular Stps?mentioning

confidence: 99%

A Detour for Yeast Oxysterol Binding Proteins

Beh

McMaster

Kozminski

et al. 2012

Journal of Biological Chemistry

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“…Recently, it has been demonstrated that 25-hydroxycholesterol inhibits the biosynthesis of HMG-CoA reductase . Although the mechanism by which 25-hydroxycholesterol produces its effects on HMG-CoA reductase biosynthesis is unknown, several binding studies (Kandutsch et al, 1977;Kandutsch and Thompson, 1980;Sinensky and Mueller, 1981) suggest that the initial site of action of this compound is a cytosolic protein.…”

mentioning

confidence: 99%

Complementary recessive 25‐hydroxycholesterol‐resistant somatic cell mutants – assay of 25‐hydroxycholesterol binding activity

Sinensky

Logel

Torget

1982

Journal Cellular Physiology

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Complementation analysis of recessive 25-hydroxycholesterol-resistant mutants of the CHO-Kl cell shows the existence of at least two complementation groups, one of which is missing a binding activity for 25-hydroxycholesterol. Both complementation groups are shown to be refractory to inhibition of cellular HMG-CoA reductase activity and in the inhibition of biosynthesis of this enzyme by 25-hydroxycholesterol.

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“…Different transport mechanisms for cholesterol and hydro¬ xylated sterols are likely. This is supported by the description of two cytosolic binding proteins in L-cells and foetal mouse liver cells (Kandutsch et al 1977 Binding of cholesterol to the cytochrome P-450 was reported to be rate-limiting in steroidogenesis (Mahaffee et al 1974;Williams-Smith et al 1976). …”

Section: Discussionmentioning

confidence: 80%

Conversion of 22S-hydroxy-cholesterol and its effect on the metabolism of other sterols in rat adrenal cells and bovine adrenal mitochondria

Huijmans

Degenhart

Kortleve

1982

Acta Endocrinologica

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This study provides evidence that 22S-OH\x=req-\ cholesterol inhibits the conversion of 25-OH-cholesterol but has no effect on the conversion of 22R-OH-cholesterol. The latter sterol is an intermediate in the cholesterol side-chain cleavage, whereas for the conversion of 25\ x=r eq-\ OH-cholesterol into pregnenolone the complete si de\x=req-\ chain cleaving enzyme system is necessary. This complements a previous study in which it was shown, that 22S-OH-cholesterol has an inhibitory effect on the ACTH-induced conversion of cholesterol into corticosterone in isolated rat adrenal cells.The available evidence thus suggests an inhibition by 22S-OH-cholesterol of the first step in the cholesterol side-chain cleavage. The results, obtained from the experiments with rat adrenal cells and with bovine adrenal mitochondria, allow the hypothesis, that a causal relationship exists between conversion of 22S-OH-cholesterol and production of corticosterone, respectively pregnenolone. We conclude, that 22S-OH-cholesterol is a substrate for steroid production in the adrenal cell. This sterol inhibits the ACTH-stimulated corticosterone production. The site of this inhibition is located at one of the first steps in the cholesterol side-chain cleavage, probably the binding of cholesterol to the cytochrome P450-complex.

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Binding of 25-hydroxycholesterol and cholesterol to different cytoplasmic proteins

Abstract: Studies were carried out to determine whether or not oxygenated derivatives of cholesterol (e.g., 25-hydroxycholesterol) that specifically suppress the activity of 3-hy-

Cited by 64 publications

References 27 publications

A Detour for Yeast Oxysterol Binding Proteins

A Detour for Yeast Oxysterol Binding Proteins

Complementary recessive 25‐hydroxycholesterol‐resistant somatic cell mutants – assay of 25‐hydroxycholesterol binding activity

Conversion of 22S-hydroxy-cholesterol and its effect on the metabolism of other sterols in rat adrenal cells and bovine adrenal mitochondria

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