Endocrinology, Vol 125, 2167-2174, Copyright © 1989 by Endocrine Society

ARTICLES

The human liver growth hormone receptor

JF Hocquette, MC Postel-Vinay, C Kayser, B de Hemptinne and A Amar-Costesec
Unite de Biologie et Pathologie de la Croissance et du Developpement, INSERM U.30, Hopital des Enfants Malades, Paris, France.

Human livers, obtained from donors at the time of transplant, were homogenized in 0.25 M sucrose and fractionated by differential centrifugation. The specific binding of [125I] human (h) GH to total particulate fractions from 18 livers varied from 0.4-5.1% of the total radioactivity/100 micrograms protein. Binding affinity was 2.0 +/- 0.3 X 10(9) M-1, and binding capacity ranged from 14-53 fmol/mg protein. A different proportion of receptors occupied by endogenous hGH did not explain the large variation in binding. Binding sites were specific for hGH. Dissociation of the hormone-receptor complex was extremely slow. No specific binding of [125I]hPRL was observed. Specific binding of insulin was found in fractions from all livers and varied less than hGH binding. Cross-linking of [125I]hGH to plasma membrane and microsome receptors yielded two major autoradiographic bands corresponding to an estimated mol wt of 103,000 for the receptor, with a possible subunit of 54,000. Human liver primary fractions were characterized. The binding of hGH and insulin displayed a nucleo-microsomal distribution pattern in the primary fractions; 54.2% and 27.9% of the hGH-binding activity were found in the microsomes and the nuclear fraction, respectively, whereas insulin binds equally to nuclear and microsomal elements. Our findings suggest that hGH-binding sites are present in the plasma membrane and also in one or more intracellular compartments, whereas a high proportion of insulin receptors is associated with the plasma membrane.

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