Regulation of growth hormone binding protein in man: comparison of gel chromatography and immunoprecipitation methods

1993 ◽  
Vol 76 (2) ◽  
pp. 302-308 ◽  
Author(s):  
K. K. Ho
Keyword(s):  
Growth Hormone ◽  
Binding Protein ◽  
Gel Chromatography ◽  
Hormone Binding ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein ◽  
Regulation Of Growth

Growth hormone binding protein in patients with renal failure

1992 ◽  
Vol 127 (6) ◽  
pp. 485-488 ◽  
Author(s):  
Hiralal G Maheshwari ◽  
Ian Rifkin ◽  
Joan Butler ◽  
Michael Norman
Keyword(s):  
Growth Hormone ◽  
Renal Failure ◽  
Renal Disease ◽  
Binding Protein ◽  
Scatchard Analysis ◽  
Gel Chromatography ◽  
Hormone Binding ◽  
Binding Studies ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

To investigate changes in the growth hormone binding protein (GH-BP) in renal disease, gel chromatography was used to separate free and bound hormone after incubation with 125I-GH, the results being expressed as a percentage of radioactive GH eluting in a high molecular weight (70–80 kD) peak. In 26 normal individuals, binding was 39.3±8.0%, while in 11 patients with renal disease who were off dialysis binding was reduced to 16.8±5.6%. Similarly, in 9 patients undergoing hemodialysis binding was reduced to 24.6±6.8%, in 8 patients undergoing chronic ambulatory peritoneal dialysis binding was reduced to 25.7±7.6%, and in 9 patients within three months of a renal transplant binding was reduced to 25.1±8.6%. Scatchard analysis showed that these changes were not a result of decreased affinity of GH-BP for GH, and receptor binding studies showed that uremic serum was not inhibiting binding. The decreased concentration of GH-BP may indicate decreased expression of the GH receptor in target tissues, and hence diminished responsiveness to GH in renal failure.

Androgen regulation of growth hormone binding protein

Metabolism ◽  
1996 ◽  
Vol 45 (12) ◽  
pp. 1521-1526 ◽  
Author(s):  
Bruce S. Keenan ◽  
Gail E. Richards ◽  
Moises Mercado ◽  
John S. Dallas ◽  
Gary D. Eakman ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Binding Protein ◽  
Hormone Binding ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein ◽  
Androgen Regulation ◽  
Regulation Of Growth

Regulation of Growth Hormone-Binding Protein: Clinical Implications

1993 ◽  
Vol 6 (3-4) ◽  
Author(s):  
M.C. Postel-Vinay ◽  
J. Leger ◽  
A. Sotiropoulos ◽  
M.C. Delehaye-Zervas ◽  
J. Finidori ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Binding Protein ◽  
Clinical Implications ◽  
Hormone Binding ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein ◽  
Regulation Of Growth

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.

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