Growth hormone-binding protein enhances growth hormone activity in vivo.

TURYN D; DOMINICI FP; SOTELO AI; BARTKE A

AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM

AMER PHYSIOLOGICAL SOC

Año: 1997 vol. 273 p. 549 - 556

0193-1849

The decay curve of labeled growth hormone (GH) in the plasma followed a three-compartment model and could be described by the equation: concentration = Ae-alpha t + Be-beta t + Ce-gamma t, where A, B, and C are y-intercepts and alpha, beta, and gamma are compartments. When 125I-labeled ovine prolactin (oPRL) was injected, the decay curve could be described by the equation: concentration = Ae-alpha t + Ce-gamma t. Formation of 125I-labeled bovine-GH-binding protein (GHBP) complexes with somatogenic characteristics was demonstrated in the serum of both normal and GH transgenic mice. In contrast, 125I-oPRL was unable to form complexes of this type in any of the mice studied. Receptor-mediated liver uptake was found to be faster for PRL than for GH (5-6 min vs. 15-20 min). Liver uptake of radioactivity was significantly lower for PRL than for GH [liver to blood ratio (L/B) of 1.7 +/- 0.3 at 6 min vs. L/B of 3.7 +/- 0.6 at 20 min, respectively]. The presence of binding proteins for GH substantially reduces the clearance of this hormone and consequently increases the liver uptake of GH (mediated by GH receptors). This suggests that GHBPs act to increase the biological activity of GH in vivo.