Abstract：
:A discriminating system capable of recognizing the oxygenated sterols was investigated in human lymphocytes. After labelling entire cells with 25-hydroxy [3H] cholesterol (10 nM) the cytosol was ultracentrifuged on a linear sucrose density gradient. Bound 25-hydroxy [3H] cholesterol was located in a single peak with a sedimentation coefficient of 8.3 S. Pronase treatment abolished the radioactive peak. This 8.3 S protein had a low binding capacity for 25-hydroxy [3H] cholesterol and probably a high affinity. This last parameter was not determined on account of some difficulties encountered in a cell-free system relating to the physico-chemical properties of 25-hydroxycholesterol. Only the hydroxylated sterols closely related to 25-hydroxycholesterol were capable of specifically binding to the 8.3 S protein, in contrast with cholesterol. This protein differed from the binding proteins of oxygenated derivatives of vitamin D3 and glucocorticoids. With the human lymphocyte as a model and under our experimental conditions, this hydroxylated sterol-binding protein seems to be involved rather in the cell division control than in the regulation of HMG-CoA reductase activity: indeed, the hydroxysterols able to inhibit thymidine [3H] incorporation into DNA are recognized by this protein whereas the hydroxysterols active on HMG-CoA reductase activity without affecting thymidine [3H] incorporation into DNA are not.
journal_name
Biochimiejournal_title
Biochimieauthors
Defay RE,Astruc ME,Roussillon S,Descomps B,Crastes De Paulet Adoi
10.1016/s0300-9084(82)80437-9subject
Has Abstractpub_date
1982-05-01 00:00:00pages
331-9issue
5eissn
0300-9084issn
1638-6183pii
S0300-9084(82)80437-9journal_volume
64pub_type
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