Sterol 27-hydroxylase: high levels of activity in vascular endothelium.
Sterol 27-hydroxylase activity in bovine aortic endothelial (BAE) cells in culture has been compared with that in HepG2 cells and in Chinese hamster ovary (CHO) cells using identical culture conditions. The total enzyme activity of BAE cells (3.0 nmol/72 h per mg cell protein) was comparable with th...
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1994-06-01
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Series: | Journal of Lipid Research |
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doaj-939edbcd53e9473fa9a6140cb42019302021-04-26T05:51:09ZengElsevierJournal of Lipid Research0022-22751994-06-0135610261030Sterol 27-hydroxylase: high levels of activity in vascular endothelium.A B Reiss0K O Martin1N B Javitt2D W Martin3E A Grossi4A C Galloway5Department of Medicine, New York University Medical Center, NY 10016.Department of Medicine, New York University Medical Center, NY 10016.Department of Medicine, New York University Medical Center, NY 10016.Department of Medicine, New York University Medical Center, NY 10016.Department of Medicine, New York University Medical Center, NY 10016.Department of Medicine, New York University Medical Center, NY 10016.Sterol 27-hydroxylase activity in bovine aortic endothelial (BAE) cells in culture has been compared with that in HepG2 cells and in Chinese hamster ovary (CHO) cells using identical culture conditions. The total enzyme activity of BAE cells (3.0 nmol/72 h per mg cell protein) was comparable with that of HepG2 cells (4.0 nmol/72 h per mg protein) and both values were significantly greater than that in CHO cells (0.002 nmol/72 h per mg protein). The enzyme was identified in the mitochondria extracted from BAE cells by Western blotting using an antibody of proven specificity, and its metabolites 27-hydroxycholesterol and 3 beta-hydroxy-5-cholestenoic acid were identified by mass spectrum analysis. The presence of the enzyme in endothelium provides a mechanism for preventing accumulation of intracellular cholesterol by initiating a pathway of bile acid synthesis different from that initiated by 7 alpha-hydroxylation of cholesterol in the liver.http://www.sciencedirect.com/science/article/pii/S0022227520400999 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
A B Reiss K O Martin N B Javitt D W Martin E A Grossi A C Galloway |
spellingShingle |
A B Reiss K O Martin N B Javitt D W Martin E A Grossi A C Galloway Sterol 27-hydroxylase: high levels of activity in vascular endothelium. Journal of Lipid Research |
author_facet |
A B Reiss K O Martin N B Javitt D W Martin E A Grossi A C Galloway |
author_sort |
A B Reiss |
title |
Sterol 27-hydroxylase: high levels of activity in vascular endothelium. |
title_short |
Sterol 27-hydroxylase: high levels of activity in vascular endothelium. |
title_full |
Sterol 27-hydroxylase: high levels of activity in vascular endothelium. |
title_fullStr |
Sterol 27-hydroxylase: high levels of activity in vascular endothelium. |
title_full_unstemmed |
Sterol 27-hydroxylase: high levels of activity in vascular endothelium. |
title_sort |
sterol 27-hydroxylase: high levels of activity in vascular endothelium. |
publisher |
Elsevier |
series |
Journal of Lipid Research |
issn |
0022-2275 |
publishDate |
1994-06-01 |
description |
Sterol 27-hydroxylase activity in bovine aortic endothelial (BAE) cells in culture has been compared with that in HepG2 cells and in Chinese hamster ovary (CHO) cells using identical culture conditions. The total enzyme activity of BAE cells (3.0 nmol/72 h per mg cell protein) was comparable with that of HepG2 cells (4.0 nmol/72 h per mg protein) and both values were significantly greater than that in CHO cells (0.002 nmol/72 h per mg protein). The enzyme was identified in the mitochondria extracted from BAE cells by Western blotting using an antibody of proven specificity, and its metabolites 27-hydroxycholesterol and 3 beta-hydroxy-5-cholestenoic acid were identified by mass spectrum analysis. The presence of the enzyme in endothelium provides a mechanism for preventing accumulation of intracellular cholesterol by initiating a pathway of bile acid synthesis different from that initiated by 7 alpha-hydroxylation of cholesterol in the liver. |
url |
http://www.sciencedirect.com/science/article/pii/S0022227520400999 |
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