Abstract:
:Side chain-hydroxylated derivatives of cholesterol (OH sterol) inhibiting lymphoblastic transformation bind with high affinity and specificity to a hydroxysterol binding protein (OHSBP) in the cytosol of human lymphocytes. These binding properties of OHSBP suggested some analogies with that of steroid hormone receptors. The observation of a nuclear binding of 25-OH[3H]cholesterol prompted us to apply to the cytosolic OH sterol-OHSBP complex the physico-chemical treatments known to 'activate' the steroid hormone receptors. A change of sedimentation coefficient from 8.3 to 4.3 S was observed in hypertonic buffer (0.4 M KCl) but the resulting 4.3 S complex dissociates easily whereas the 'native' 8.3 S form does not. Moreover, molybdate did not prevent the 8.3----4.3 S transformation induced by KCl and neither ammonium sulfate precipitation nor increasing temperature had any effect on the sedimentation coefficient of the 8.3 S complex. Thus, several physico-chemical features differentiate the OH sterol-OHSBP complex from steroid hormone receptors.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Defay R,Astruc M,Beseme F,Descomps B,Crastes de Paulet Adoi
10.1016/0014-5793(84)80798-xsubject
Has Abstractpub_date
1984-08-06 00:00:00pages
319-26issue
2eissn
0014-5793issn
1873-3468journal_volume
173pub_type
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