Physiology and pathophysiology of growth hormone-binding protein: Methodological and clinical aspects

Fisker, Sanne

doi:10.1016/j.ghir.2005.11.001

Cited by 54 publications

(51 citation statements)

References 344 publications

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“…In man, there is evidence that GHBP is derived from proteolytical cleavage of the extracellular domain of the GH receptor and may reflect GH receptor status (55). Several studies have reported that GHBP levels are increased in obesity (27,41,71) and a direct relationship between abdominal adiposity and GHBP concentration has been observed (71). The physiological significance of increased GHBP in obesity is presently unknown.…”

Section: The Gh-insulin-like-growth-factor-i (Igf-i) Axis In Obesitymentioning

confidence: 99%

Obesity, growth hormone and weight loss

Rasmussen

2010

Molecular and Cellular Endocrinology

104

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Growth hormone (GH) is the most important hormonal regulator of postnatal longitudinal growth in man. In adults GH is no longer needed for longitudinal growth. Adults with growth hormone deficiency (GHD) are characterised by perturbations in body composition, lipid metabolism, cardiovascular risk profile and bone mineral density. It is well established that adult GHD usually is accompanied by an increase in fat accumulation and GH replacement in adult patients with GHD results in reduction of fat mass and abdominal fat mass in particular. It is also recognized that obesity and abdominal obesity in particular results in a secondary reduction in GH secretion and subnormal insulin-like growth factor-I (IGF-I) levels. The recovery of the GH IGF-I axis after weight loss suggest an acquired defect, however, the pathophysiologic role of GH in obesity is yet to be fully understood. In clinical studies examining the efficacy of GH in obese subjects very little or no effect are observed with respect to weight loss, whereas GH seems to reduce total and abdominal fat mass in obese subjects. The observed reductions in abdominal fat mass are modest and similar to what can be achieved by diet or exercise interventions.

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Section: The Gh-insulin-like-growth-factor-i (Igf-i) Axis In Obesitymentioning

confidence: 99%

Obesity, growth hormone and weight loss

Rasmussen

2010

Molecular and Cellular Endocrinology

104

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“…In mammals, previous studies reported that exogenous GH increased expression of both GHRs and levels of growth hormone binding protein (GHBP) (7,12). The mammalian GHBP is made by either proteolytic cleavage of the GHR extracellular domain (human and rabbit) or as a splice variant of the GHR gene (mouse and rat) (18). Neither the transcript identity nor the mechanisms of GHBP formation have been reported in the rainbow trout.…”

Section: Rainbow Trout Gh Microarray Analysismentioning

confidence: 99%

Effects of short-term growth hormone treatment on liver and muscle transcriptomes in rainbow trout (Oncorhynchus mykiss)

Gahr

Vallejo

Weber

et al. 2008

Physiological Genomics

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“…The mature protein is comprised of three domains: an extracellular domain (246-amino-acid residues encoded by exons 2–7), a short transmembrane domain (24 residues, encoded by exon 8), and the intracellular portion of the GHR (350 residues, encoded by exons 9–10). Unlike the case in rodents, where the circulating GHBP is generated by alternative GHR mRNA splicing [14], in humans, circulating GHBP is the proteolytically cleaved, extracellular domain of the cell surface GHR [15, 16]. …”

Section: Introductionmentioning

confidence: 99%

Extreme Elevation of Serum Growth Hormone-Binding Protein Concentrations Resulting from a Novel Heterozygous Splice Site Mutation of the Growth Hormone Receptor Gene

et al. 2009

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Background/Aims: Circulating growth hormone-binding protein (GHBP), in humans, is the proteolytic product of the growth hormone receptor (GHR). We investigated a prepubertal male subject who was of short stature, but who had a markedly elevated serum level of GHBP. Methods: Serum and DNA from the patient and his mother were analyzed. Results: Both the patient and mother had serum GHBP concentrations over 100-fold higher than normal, by assays, and Western and ligand blot analysis. Sequencing of the GHR gene revealed a novel heterozygous C>A transversion at position 785-3 in the acceptor splice site of intron 7. Conclusion: In silico analysis of the altered sequence suggested that 785-3(C>A) is a splicing mutation, with either retention of intron 7 or the skipping of exon 8. The consequence is a truncated GHR lacking the transmembrane domain (encoded by exon 8) and the cytoplasmic domain. We hypothesize that this GHR variant cannot anchor to the cell membrane, and the continual secretion into the circulation explains the elevated levels of serum GHBP detected in the patient and his mother. Despite this mutation, the presence of the wild-type GHR allele, presumably, permits some normality in GH-induced action.

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Physiology and pathophysiology of growth hormone-binding protein: Methodological and clinical aspects

Cited by 54 publications

References 344 publications

Obesity, growth hormone and weight loss

Obesity, growth hormone and weight loss

Effects of short-term growth hormone treatment on liver and muscle transcriptomes in rainbow trout (Oncorhynchus mykiss)

Extreme Elevation of Serum Growth Hormone-Binding Protein Concentrations Resulting from a Novel Heterozygous Splice Site Mutation of the Growth Hormone Receptor Gene

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