Serum growth hormone-binding protein is decreased in prepubertal children with idiopathic short stature

1996 ◽  
Vol 19 (6) ◽  
pp. 348-352 ◽  
Author(s):  
N. Dávila ◽  
M. Moreira-Andrés ◽  
J. Alcañiz ◽  
B. Barceló
Keyword(s):  
Growth Hormone ◽  
Short Stature ◽  
Binding Protein ◽  
Idiopathic Short Stature ◽  
Hormone Binding ◽  
Serum Growth Hormone ◽  
Prepubertal Children ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

Effect of growth hormone on the low level of growth hormone binding protein in idiopathic short stature

1992 ◽  
Vol 37 (3) ◽  
pp. 249-253 ◽  
Author(s):  
Manuel Fontoura ◽  
Elizabeth Mugnier ◽  
Raja Brauner ◽  
Raphael Rappaport ◽  
Marie-Catherine Postel-Vlnay
Keyword(s):  
Growth Hormone ◽  
Short Stature ◽  
Binding Protein ◽  
Idiopathic Short Stature ◽  
Hormone Binding ◽  
Low Level ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

Growth hormone-binding protein levels: Studies of children with short stature

Metabolism ◽  
1994 ◽  
Vol 43 (3) ◽  
pp. 357-359 ◽  
Author(s):  
Nelly Mauras ◽  
Lena M.S. Carlsson ◽  
Suzanne Murphy ◽  
Thomas J. Merimee
Keyword(s):  
Growth Hormone ◽  
Short Stature ◽  
Binding Protein ◽  
Hormone Binding ◽  
Protein Levels ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

Comparison between the human serum growth hormone-binding protein and the water-soluble growth hormone-binding site released from IM-9 lymphocytes

1993 ◽  
Vol 129 (6) ◽  
pp. 559-564 ◽  
Author(s):  
Guy Massa ◽  
Mapoko Ilondo ◽  
Magda Vanderschueren-Lodeweyckx
Keyword(s):  
Growth Hormone ◽  
Human Serum ◽  
Binding Site ◽  
Binding Protein ◽  
Water Soluble ◽  
Hormone Binding ◽  
Serum Growth Hormone ◽  
Gh Receptor ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

The characteristics of the human serum growth hormone-binding protein (GHBP) were compared with those of a water-soluble GH-binding site prepared by incubating cultured IM-9 lymphocytes in assay buffer with 25 mmol/l iodoacetamide. High-performance liquid chromatography gel filtration of the water-soluble GH-binding site incubated with 125I-labeled human GH ([125I]hGH) revealed a large peak of bound [125I]hGH eluting at the same position as the peak of [125I]hGH bound to the GHBP in serum. The estimated Mr of the peak was 120 000, presumably representing one [125I]hGH bound to two binding sites. The binding specificities of the serum GHBP, the water-soluble GH-binding site and the GH receptor on IM-9 lymphocytes were identical. The binding affinities for 22 000 hGH and for 20 000 hGH of the serum GHBP were similar to the binding affinity of the water-soluble GH-binding site but lower than those of the cellular GH receptor. These findings show that the characteristics of the serum GHBP are comparable to those of the water-soluble GH-binding site released from IM-9 cells and support the hypothesis that in man the serum GHBP is produced by proteolytic cleavage of the cellular GH receptor.

Sign in / Sign up

Export Citation Format

Share Document