Trihydroxycoprostane

Trihydroxycoprostane is a lipid of Sterol Lipids (ST) class. The involved functions are known as Uptake, Enterohepatic Circulation, Metabolic Inhibition and Ionization. Trihydroxycoprostane often locates in Hepatic, Entire gastrointestinal tract and Abdominal Cavity. The related lipids are 3,7,12-trihydroxycoprostane, (3beta,5beta,7alpha,12alpha)-isomer, Cholestanes and scymnol.

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Introduction

To understand associated biological information of Trihydroxycoprostane, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Trihydroxycoprostane?

There are no associated biomedical information in the current reference collection.

No disease MeSH terms mapped to the current reference collection.

PubChem Associated disorders and diseases

What pathways are associated with Trihydroxycoprostane

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Trihydroxycoprostane?

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What functions are associated with Trihydroxycoprostane?


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What lipids are associated with Trihydroxycoprostane?

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What genes are associated with Trihydroxycoprostane?

There are no associated biomedical information in the current reference collection.

What common seen animal models are associated with Trihydroxycoprostane?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Trihydroxycoprostane

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Authors Title Published Journal PubMed Link
pmid:24853400
pmid:
Fricker G et al. Enterohepatic circulation of scymnol sulfate in an elasmobranch, the little skate (Raja erinacea). 1997 Am. J. Physiol. pmid:9374698
Pikuleva IA et al. Expression, purification, and enzymatic properties of recombinant human cytochrome P450c27 (CYP27). 1997 Arch. Biochem. Biophys. pmid:9210654
Dahlbäck H and Holmberg I Oxidation of 5 beta-cholestane-3 alpha,7 alpha, 12 alpha-triol into 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoic acid by cytochrome P-450(26) from rabbit liver mitochondria. 1990 Biochem. Biophys. Res. Commun. pmid:2322231
Noshiro M et al. The involvement of cytochrome b5 in 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol 25-hydroxylation and taurodeoxycholate 7 alpha-hydroxylation of rat liver. 1982 Biochem. Biophys. Res. Commun. pmid:7115387
Saarem K and Pedersen JI Sex differences in the hydroxylation of cholecalciferol and of 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol in rat liver. 1987 Biochem. J. pmid:2825658
Lidström-Olsson B and Wikvall K The role of sterol carrier protein2 and other hepatic lipid-binding proteins in bile-acid biosynthesis. 1986 Biochem. J. pmid:3800967
Saarem K and Pedersen JI Effect of age, gonadectomy and hypophysectomy on mitochondrial hydroxylation of vitamin D3 (cholecalciferol) and of 5 beta-cholestane-3 alpha,7 alpha,12 alpha-triol in female and male rat liver. 1988 Biochem. J. pmid:2840896
Mast N et al. Distinct binding of cholesterol and 5beta-cholestane-3alpha,7alpha,12alpha-triol to cytochrome P450 27A1: evidence from modeling and site-directed mutagenesis studies. 2006 Biochemistry pmid:16584175