The Growth Hormone Binding Protein (GHBP) consists of 238 amino acids and contains three disulfide bridges and four possible glycolylation positions. Human GHBP is formed by proteolytic cleavage (metalloproteases) of the mature growth hormone receptor located in the cell membrane.
The function of GHBP could be in the regulation of the biological availability of GH, the half-life of GH extends to 100 minutes.
Correlation studies showed a strong positive correlation of GHBP concentration with the amount of intra-abdominal adipose tissue and type II diabetes. This correlation suggests that GHBP may be a biomarker for visceral adipose tissue.
The growth hormone binding protein ELISA allows the quantification of GHBP in serum and plasma. Recombinant human GHBP produced in eukaryotic cells is used as standard material.