Growth Hormone Binding Protein (GHBP) consists of 238 amino acids and includes four sides for glycosylation and three disulfid bounds. In humans GHBP is formed by receptor shedding of the growth hormone receptor by a metalloprotease (ADAM17).
Regulation of biological availability of GH is possibly the physiologic role of of GHBP. Thus, the half-life of GH is prolonged up to 100 minutes by binding to GHBP.
GHBP correlates positively with the intraabdominal fat mass and is increased in type II diabetics with hyperinsulinaemia but not in type I diabetics. This correlation might indicate that GHBP is a suitable biomarker for the amount of visceral adipose tissue.
The growth hormone binding protein ELISA allows the quantiative measurement of GHBP in serum and plasma. Recombinant human GHBP, produced in eukaryotic cell lines, is used for assay standardization.