F Le Gaillard

  • Citations Per Year
Learn More
HMG-CoA reductase is the key enzyme for the biosynthesis of isoprenoid compounds essential for cell growth and differentiation. Its tyrosine kinase-dependent modulation has recently been suggested and described in the ErbB-2 overexpressing cell line SKBR-3 [Asslan et al. (1998) Biochem. J. 330, 241-246]. Epidermal growth factor (EGF) increased the HMG-CoA(More)
3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) reductase is the major rate-limiting enzyme in sterol and non-sterol isoprenoid synthesis. Isoprenoids are involved in the mechanisms of cell proliferation and transformation leading notably to crucial post-translational maturation of small G-proteins of the Ras superfamily. HMG-CoA reductase is among the most highly(More)
The isolation of transcortin in a pure form made possible the preparation of a monospecific anti-human transcortin rabbit serum. Serum transcortin levels were measured by electroimmunodiffusion. Experimental results expressed as errors by the calculating of interserial reproducibility were 4.74 per 100. The mean value was significantly different for men (36(More)
The transcortin we have used in this work is extremely pure. This was shown by the polymerisation observed at pH 4. This polymerisation is never observed with an impure form of transcortin [4]. Moreover, since it is known that the presence of cortisol in the binding site is an essential condition to the activity of purified transcortin [5], it appears that(More)
The molecular weight of human transcortin, calculated from the sedimentation coefficient, was found to be 49,500, thus slightly lower than previously reported values. After purification, human transcortin trended to polymerize rapidly, with participation of both non covalent bonds and one disulfide bridge per dimer. The physicochemical parameters, the(More)
Previous studies from our laboratory demonstrated that high-density lipoproteins (subclass 3; HDL3) bind to sites specific for apolipoprotein AI on the human adenocarcinoma cell line A549 and that HDL3 binding promotes a mitogenic effect [Favre, Tazi, Le Gaillard, Bennis, Hachem and Soula (1993) J. Lipid Res. 34, 1093-1106]. In the present study, we have(More)
The binding activity of human corticosteroid-binding globulin (CBG) is pH dependent and governed in alkaline pH ranges by the pK of arginine. No essential arginine residues is located in the binding site. The loss of biological activity is rapid and complete as soon as one arginine residue is modified by phenylglyoxal. There is also a transconformation of(More)