Evidence for differential binding of growth hormones to membrane and cytosolic GH binding proteins of rabbit liver.

The existence of three GH binding proteins in rabbit liver membranes has been adduced from binding studies with a panel of monoclonal antibodies. Immunologically cross-reactive analogues of 'type 2' binding proteins were shown to exist in rabbit liver cytosol and in affinity purified receptor from liver microsomes. We now report differences in the binding of human and ovine GH with respect to two antigenic determinants on the 'type 1' GH binding protein. The discovery of these differences has enabled the detection of cross-reactive analogues of both binding protein types '1' and '2' in liver cytosol and in affinity purified preparations from liver membranes. These findings show a close structural relationship between the pool of cytosolic GH binding proteins and those present in the membranes; and differential ligand binding to, as well as absolute ligand selection by GH binding proteins, which could reflect the ability of GH to trigger a range of biological responses either through different receptors or differential interaction with particular receptor subtypes.