Growth hormone-binding protein (GH-BP) levels in follicular fluid from human preovulatory follicles: correlation with serum GH-BP levels

1993 ◽  
Vol 77 (1) ◽  
pp. 33-39 ◽  
Author(s):  
T. Amit
Keyword(s):  
Growth Hormone ◽  
Follicular Fluid ◽  
Binding Protein ◽  
Hormone Binding ◽  
Growth Hormone Binding Protein ◽  
Preovulatory Follicles ◽  
Hormone Binding Protein ◽  
Serum Gh

Ontogeny and nutritional regulation of the serum growth hormone-binding protein in the rat

1991 ◽  
Vol 125 (4) ◽  
pp. 409-415 ◽  
Author(s):  
Nkuadi Mulumba ◽  
Guy Massa ◽  
Jean-Marie Ketelslegers ◽  
Marc Maes
Keyword(s):  
Growth Hormone ◽  
Binding Protein ◽  
Female Rats ◽  
Male Rats ◽  
Nutritional Regulation ◽  
Hormone Binding ◽  
Serum Growth Hormone ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein ◽  
Serum Gh

Abstract. The ontogeny and the nutritional regulation of the serum growth hormone-binding protein in Wistar rats was studied in vitro using Ultrogel AcA34 filtration of serum incubated with 125I-bovine growth hormone. The level of the specific binding of GH to serum GH-binding protein was low in 1-week-old rats (female rats 2.3±0.9%; N=6, and male rats 2.1±8%; N=6 ) and increased with puberty, to reach 10-fold higher levels in 12-week-old adult female (26.1±2.3%; N=6) and 5-fold higher levels in adult male rats (11.2±0.9%; N=6). From 6 weeks of age and onwards, the level of serum GH-binding protein was significantly higher in female than in male rats, reflecting sexual dimorphism. The nutritional dependence of GH-binding protein was supported by the 46% decline of serum GH-binding protein levels in 6-week-old female rats fasted for 3 days (11.6±0.9 and 6.3±1.1% in control and fasted rats, respectively; N=8/group; p<0.001). After 4 days of refeeding, no difference was found between control and experimental animals. During development and after nutritional manipulation, Scatchard analysis revealed that the changes in GH-binding protein were due to changes in binding capacity and not affinity. The levels of serum GH-binding protein were positively correlated with the levels of hepatic GH binding sites, suggesting that the regulation of both proteins is closely related during development and in states of nutritional sufficiency and deprivation.

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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