The Effect of Circulating Growth Hormone-Binding Protein on Metabolic Clearance, Distribution, and Degradation of Human Growth Hormone*

Baumann, Gerhard; Amburn, Klaus; Buchanan, Thomas A.

doi:10.1210/jcem-64-4-657

Cited by 231 publications

(78 citation statements)

References 19 publications

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“…Most studies, although not all (31), point to an effect of GHBP on GH kinetics (12,13,29,30). GHBP is the extracellular domain of the GHR, but it has not been clarified whether circulating GHBP mirrors tissue GHR status (40).…”

Section: Discussionmentioning

confidence: 99%

Kinetics and secretion of placental growth hormone around parturition

Fuglsang¹,

Sandager²,

Møller³

et al. 2006

eur j endocrinol

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Objective: During pregnancy, placental growth hormone (PGH) is secreted into the maternal circulation, replacing pituitary GH. It is controversial whether PGH levels decline during vaginal birth. After placental expulsion, PGH is eliminated from the maternal blood. GH binding protein (GHBP) and body mass index (BMI) influence GH kinetics, but their impact on PGH kinetics is unknown. The present study was undertaken to define the kinetics of PGH during vaginal delivery and Caesarian section and to relate these kinetics to GHBP and BMI. Design: A short term, prospective cohort study. Methods: Twelve women had repeated blood samples drawn during vaginal delivery. From 26 women undergoing planned Caesarian delivery (CS) repeated blood samples were withdrawn before, during and after the CS, allowing PGH half-life determination. Results: During vaginal delivery, median PGH values did not change before expulsion of the placenta, although individual fluctuations were seen. Clearance of PGH from the maternal circulation was best described by a two-compartment model. The initial half-life of serum PGH was (mean^S.D.) 5.8^2.4 min, and the late half-life was (median) 87.0 min (range: 25.1 -679.6 min). The late halflife was correlated to the pre-gestational BMI (r ¼ 0.39, P ¼ 0.047), but not to the serum GHBP concentration. Conclusions: Serum PGH did not decrease significantly during vaginal delivery. Elimination of PGH fitted a two-compartment model, with an estimated initial half-life of 5.8 min. The late phase serum half-life of PGH was related to BMI, suggesting a role for maternal fat mass in PGH metabolism.European Journal of Endocrinology 154 449-457

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Section: Discussionmentioning

confidence: 99%

Kinetics and secretion of placental growth hormone around parturition

Fuglsang¹,

Sandager²,

Møller³

et al. 2006

eur j endocrinol

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“…This figure corresponds with the observation that virtually no high molecular weight forms of hGH are present in cord serum (33). Peak 11-BP has been shown to decrease the metabolic clearance of GH (34). It is therefore possible that the exceptionally fast disappearance rate of hGH in the human infant (13) is in part due to the low levels of GH-BP.…”

Section: Discussionmentioning

confidence: 99%

Serum Growth Hormone-Binding Proteins in the Human Fetus and Infant

Massa

Zegher

Vanderschueren-Lodeweyckx

1992

Pediatr Res

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ABSTRACT. Growth hormone-binding protein (GH-BP) levels were studied in cord serum of 69 human infants born after 24 to 41 wk of gestation and in serum of 14 infants aged 1 to 3 mo. GH-BP levels were measured by HPLCgel filtration of serum incubated overnight with '251-hGH. The radioactive elution profile revealed two small I2'IhGH peaks of high molecular weight and a large peak, corresponding to monomeric Iz5I-hGH. The first peak of high molecular weight was variable, showed some of the characteristics (high molecular weight, displaceability by a large excess of unlabeled hGH) of the described low affinity, high capacity GH-BP, and did not correlate with gestational age or birth weight (peak I-BP). The second peak was identified as '251-hGH bound to the high affinity, low capacity GH-BP (peak 11-BP). Mean 2 SD specific binding of Iz5I-hGH to this peak was significantly (p < 0.0001) different between preterm infants (3.1 2 1.1%; n = 51), term infants at birth (4.2 f 1.1%; n = 18), and 1-to 3-mo-old infants (8.5 + 1.6%; n = 14). To evaluate the effect of intrauterine nutritional state, the ponderal index (weight/length3) was calculated. Peak 11-BP levels were lower (p < 0.05) in infants with the ponderal index < 2.35 (2.8 k 1.0%; n = 20) than in those with the ponderal index between 2.35 and 2.65 (3.4 k 1.2%; n = 29) or > 2.65 (3.8 2 1.2%; n = 20). We conclude that GH-BP are present in human cord serum throughout the 3rd trimester of gestation. The levels of peak 11-BP are influenced by fetal age and intrauterine growth and increase quickly after birth. (Pediatr Res 32: 69-72,1992)

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“…The high affinity GHBP is identical to the extracellular domain of the membrane-bound GHR (Leung et al 1987) and is formed by either alternative splicing of the GHR gene (Baumbach et al 1989, Smith et al 1989, Martini et al 1997 or proteolytic cleavage of the extracellular domain of the GHR (Leung et al 1987, Sotiropoulos et al 1993. GHBPs have been shown to modify the cellular actions of GH by altering its in vivo kinetics and metabolism (Baumann et al 1987, Veldhuis 1993 and by competing with receptors for ligand (Lim et al 1990, Mannor et al 1991. In addition, circulating levels of GHBP in the rabbit, pig and rat have been shown to reflect GHR concentrations in target tissues (Mulumba et al 1991, Ambler et al 1992, Ymer & Herington 1992.…”

Section: Introductionmentioning

confidence: 99%

Plasma growth hormone and growth hormone-binding protein during development in the marsupial brushtail possum (Trichosurus vulpecula)

Saunders

Gemmell²,

Waters³

et al. 2002

Journal of Endocrinology

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Plasma concentrations of growth hormone (GH) were measured in the brushtail possum (Trichosurus vulpecula) pouch young from 25 through to 198 days post-partum (n=71). GH concentrations were highest early in pouch life (around 100 ng/ml), and thereafter declined in an exponential fashion to reach adult concentrations (10·8 1·8 ng/ml; n=21) by approximately 121-145 days post-partum, one to two months before the young is weaned. Growth hormone-binding protein (GHBP), which has been shown to modify the cellular actions of GH in eutherian mammals, was identified for the first time in a marsupial. Based on size exclusion gel filtration, possum GHBP had an estimated molecular mass of ]65 kDa, similar to that identified in other mammalian species, and binding of 125 I-labelled human GH (hGH) was displaced by excess hGH (20 µg). An immunoprecipitation method, in which plasma GHBP was rendered polyethylene glycol precipitable with a monoclonal antibody to the rabbit GHBP/GH receptor (MAb 43) and labelled with 125 I-hGH, was used to quantitate plasma GHBP by Scatchard analysis in the developing (pooled plasma samples) and adult (individual animals) possums. Binding affinity (K a ) values in pouch young aged between 45 and 54 and 144 and 153 days post-partum varied between 1·0 and 2·4 10 9 /M, which was slightly higher than that in adult plasma (0·96 0·2 10 9 /M, n=6). Binding capacity (B max ) values increased from nondetectable levels in animals aged 25-38 days post-partum to reach concentrations around half that seen in the adult (1·4 0·2 10 -9 M) by about 117 days post-partum and remained at this level until 153 days post-partum. Therefore, in early pouch life when plasma GH concentrations are highest, the very low concentrations of GHBP are unlikely to be important in terms of competing with GH-receptor for ligand or altering the half-life of circulating GH.

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The Effect of Circulating Growth Hormone-Binding Protein on Metabolic Clearance, Distribution, and Degradation of Human Growth Hormone*

Cited by 231 publications

References 19 publications

Kinetics and secretion of placental growth hormone around parturition

Kinetics and secretion of placental growth hormone around parturition

Serum Growth Hormone-Binding Proteins in the Human Fetus and Infant

Plasma growth hormone and growth hormone-binding protein during development in the marsupial brushtail possum (Trichosurus vulpecula)

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