J. Kolena et al., LIGAND-INDUCED RAPID DESENSITIZATION CAUSES STRUCTURAL ALTERATION OF RAT OVARIAN LH HCG RECEPTOR/, EXPERIMENTAL AND CLINICAL ENDOCRINOLOGY & DIABETES, 104(6), 1996, pp. 459-463
The role of the physical state of ovarian membranes was studied in the
process of the early desensitization of the LH/hCG receptor. Thirty m
in after injection of a desensitizing dose of hCG to rats, the hCG-res
ponsive adenylylcyclase activity was reduced, whereas hCG binding to o
varian membranes was still normal. Early desensitization decreased rig
idity of membrane lipids, determined by fluorescence polarization of D
PH. Possible structure-functional properties of the LH/hCG receptor we
re analyzed by thermal perturbation technique. Desensitization decreas
ed thermal stability of the LH/hCG receptor in membranes and in proteo
liposomes. Desensitization modified the quenching of protein fluoresce
nce and intrinsic fluorescence spectral properties of membranes. The S
tern-Volmer constants for control and desensitized membranes were foun
d to be 4.3 and 5.5, respectively, indicating that desensitization ele
vated the accessibility of fluorophores for acrylamide. The changes of
the physical properties of membranes resulting from desensitization w
as exhibited solely in the treatment with hCG in vivo, but not in vitr
o. The results suggest that the hCG-induced alteration of the physical
state of luteal membranes may be a requirement for the induction of c
hanges that lead to desensitization.