Pub. Date : 1997 Aug 15
PMID : 9337870
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 2 | Oxysterol-binding protein (OSBP) is a high-affinity receptor for a variety of oxysterols, such as 25-hydroxycholesterol, that down-regulate cholesterol synthesis and stimulate cholesterol esterification. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 3 | Oxysterol-binding protein (OSBP) is a high-affinity receptor for a variety of oxysterols, such as 25-hydroxycholesterol, that down-regulate cholesterol synthesis and stimulate cholesterol esterification. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 4 | Oxysterol-binding protein (OSBP) is a high-affinity receptor for a variety of oxysterols, such as 25-hydroxycholesterol, that down-regulate cholesterol synthesis and stimulate cholesterol esterification. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 5 | Oxysterol-binding protein (OSBP) is a high-affinity receptor for a variety of oxysterols, such as 25-hydroxycholesterol, that down-regulate cholesterol synthesis and stimulate cholesterol esterification. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 6 | To examine a potential role for OSBP in regulating cholesterol metabolism, we stably overexpressed this protein in Chinese-hamster ovary (CHO)-K1 cells. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 7 | CHO-OSBP cells showed a 40-60% decrease in acyl-CoA:cholesterol acyltransferase activity and mRNA, a 50% elevation in mRNA for three sterol-regulated genes [LDL receptor, 3-hydroxy-3-methylgluraryl (HMG)-CoA reductase and HMG-CoA synthase], and an 80% increase in [14C]acetate incorporation into cholesterol. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 8 | CHO-K1 cells overexpressing two OSBP mutants with a complete or N-terminal deletion of the pleckstrin homology (PH) domain had cholesterol esterification and synthesis rates that were similar to those shown by mock-transfected controls. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |
| 9 | CHO-K1 cells overexpressing OSBP have pronounced alterations in cholesterol esterification and synthesis, indicating a potential role for this receptor in cholesterol homoeostasis. | Cholesterol | LOW QUALITY PROTEIN: oxysterol-binding protein 1 | Cricetulus griseus |