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Amir Babiker

Researcher at Karolinska Institutet

Publications -  11
Citations -  965

Amir Babiker is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Cholesterol & Sterol. The author has an hindex of 11, co-authored 11 publications receiving 924 citations.

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Journal ArticleDOI

Elimination of Cholesterol in Macrophages and Endothelial Cells by the Sterol 27-Hydroxylase Mechanism COMPARISON WITH HIGH DENSITY LIPOPROTEIN-MEDIATED REVERSE CHOLESTEROL TRANSPORT

TL;DR: The results support the contention that the sterol 27-hydroxylase-mediated elimination of cholesterol is more important in macrophages than in endothelial cells.
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Importance of a Novel Oxidative Mechanism for Elimination of Intracellular Cholesterol in Humans

TL;DR: The 27-hydroxylase pathway is of significance for elimination of extrahepatic cholesterol and the net uptake by the human liver of circulating 27-oxygenated products was found to be about 20 mg/24 h.
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Transport of side-chain oxidized oxysterols in the human circulation

TL;DR: The present results are consistent with the previous finding that the less polar cholesterol metabolite 27-hydroxycholesterol competes with cholesterol for transport out of cells using HDL as an acceptor molecule, whereas the transport of the more polar compound 3beta-Hydroxy-5-cholestenoic acid is facilitated by albumin.
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Elimination of cholesterol as cholestenoic acid in human lung by sterol 27-hydroxylase: evidence that most of this steroid in the circulation is of pulmonary origin.

TL;DR: The present results suggest that the sterol 27-hydroxylase in the lung is responsible for at least half of the total flux of 27-oxygenated cholesterol metabolites to the liver and that this enzyme system may be of importance for cholesterol homeostasis in the lungs.
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Activities of Recombinant Human Cytochrome P450c27 (CYP27) Which Produce Intermediates of Alternative Bile Acid Biosynthetic Pathways

TL;DR: Kinetic data indicate that in a reconstituted system, after 27-hydroxycholesterol is formed from cholesterol, it is released from the P450 and then competes with cholesterol for reentry the enzyme active site for further oxidation, indicating that the first hydroxylation step in the overall conversion of cholesterol into 3β-Hydroxy-5-cholestenoic acid is rate-limiting.