Growth hormone-binding protein determination in plasma: a comparison of immunofunctional and growth hormone-binding assays

1993 ◽  
Vol 76 (5) ◽  
pp. 1291-1294 ◽  
Author(s):  
M. Mercado
Keyword(s):  
Growth Hormone ◽  
Binding Protein ◽  
Hormone Binding ◽  
Binding Assays ◽  
Protein Determination ◽  
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.

Growth hormone-binding protein related immunoreactivity is regulated by the degree of insulinopenia in diabetes mellitus

1996 ◽  
Vol 44 (6) ◽  
pp. 673-678 ◽  
Author(s):  
J. Kratzsch ◽  
K. Kellner ◽  
T. Zilkens ◽  
H. Schmidt-Gayk ◽  
T. Selisko ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Growth Hormone ◽  
Binding Protein ◽  
Hormone Binding ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

Growth hormone binding protein and growth hormone availability in acromegalic patients treated with long-acting octreotide (Sandostatin-LAR)

1997 ◽  
Vol 136 (1) ◽  
pp. 61-66 ◽  
Author(s):  
Sanne Fisker ◽  
Andreas Kaal ◽  
Marcella Montini ◽  
Alberto Pedroncelli ◽  
Giorgio Pagani ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Binding Protein ◽  
Hormone Binding ◽  
Age And Gender ◽  
Growth Hormone Binding Protein ◽  
Igf I ◽  
Octreotide Treatment ◽  
Hormone Binding Protein ◽  
And Gender ◽  
Long Acting

Abstract Objective: In the medical treatment of acromegaly different factors are influencial; among these the impact on growth hormone binding protein (GHBP) has not been clarified. Design: Twenty acromegalic patients and nineteen age- and gender-matched normal subjects participated in this study. The patients were treated for 21 months with depot long-acting microsphere-enclosed octreotide (Sandostatin-LAR). Previously, all the patients were treated s.c. with octreotide t.i.d. After a 2-week wash-out period (baseline) the patients received the first i.m. injection of the long-acting octreotide. The first two injections were administered at 60-day intervals; thereafter the injections were at 28-day intervals. Methods: The levels of GHBP, complexed GHBP, growth hormone (GH) and insulin-like growth factor-I (IGF-I) were determined in fasting serum samples. Results: In the 2-week wash-out period GHBP levels decreased from 1·13 ± 0·17 to 0·92 ± 0·15 nmol/l (P < 0·05). During the 21-months treatment, GHBP increased again to 1·10 ± 0·16 nmol/l. In the age- and gender-matched control group GHBP levels were significantly higher at all times (1·95 ± 0·21 nmol/l, P(all) < 0·02). Mean levels of 8-h GH decreased from 12·6 ± 2·58 μg/l at baseline to 1·97 ± 0·20 μg/l after 21 months of treatment (P < 0·05). Mean 8-h GH levels were unchanged during long-acting octreotide treatment compared with levels during s.c. treatment (1·97 ± 0·20 μg/l and 1·90 ± 0·20 μg/l respectively). In fasting blood samples GH-complexed GHBP ranged from 13·8 ± 2·4% (9 months) to 25·4 ± 4·5% (baseline) of total GHBP. Serum IGF-I increased from 367 ± 45 to 764 ± 80 μg/l (P < 0·05) during the 2-week wash-out period and decreased to 290 ± 35 μg/l (P < 0·05) after 21 months of treatment with long-acting octreotide. IGF-I levels after 21 months were significantly lower than during s.c. octreotide treatment (P < 0·05). Conclusion: Serum GHBP levels are similar during treatment with long-acting octreotide as compared with regular octreotide. Furthermore, significant changes in GHBP can occur within 2 weeks. Finally, in addition to the lowering effect on GH levels, the induced increase in GHBP levels may imply a further advantage in octreotide treatment of acromegaly, circulating GH bound to GHBP may less readily reach the tissues. European Journal of Endocrinology 136 61–66

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