Growth hormone deficiency.
Department of Chemical Pathology, St James's University Hospital, Leeds, UK.Annals of Clinical Biochemistry (Impact Factor: 2.08). 10/1987; 24 ( Pt 5):429-34.
Article: Use of growth hormone in children.[Show abstract] [Hide abstract]
ABSTRACT: The introduction of recombinant DNA-derived human growth hormone (rhGH) in the mid-1980s allowed studies to be undertaken in a number of growth disorders other than the classic indication--growth-hormone deficiency (GHD). In patients with GHD, optimizing the dose and frequency of rhGH administration, and early instigation of therapy, has led to near-normalization of final height. The use of rhGH in the treatment of Turner syndrome, Prader-Willi syndrome, intrauterine growth restriction, and chronic renal failure demonstrated the efficacy of therapy, although the increase in final height (5-7 cm) is less than that achieved in GHD. Cost-benefit implications need to be considered in the next phases of evaluating the role of rhGH therapy in these indications. To date, rhGH has only received approval for the management of idiopathic short stature in the US; as with the other wider growth indications, the lack of formal randomized, controlled trials hampers the full evaluation of efficacy, and a cautious approach should, therefore, be adopted for this particular indication. rhGH has a good safety record, although there are current concerns about the possible long-term increased risk of colonic and lymphatic malignancy, which will require monitoring through national cancer registries.Nature Clinical Practice Endocrinology & Metabolism 06/2006; 2(5):260-8. · 7.55 Impact Factor
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ABSTRACT: Advances in molecular biology have led to the identification of mutations within several novel genes associated with the phenotype of isolated growth hormone deficiency, combined pituitary hormone deficiency, and syndromes such as septo-optic dysplasia. Progress has also been made in terms of the optimum diagnosis of disorders of stature and their treatment. The use of growth hormone for the treatment of adults with growth hormone deficiency and conditions such as Turner's syndrome, Prader-Willi syndrome, intrauterine growth restriction, and chronic renal failure has changed the practice of endocrinology, although cost-benefit implications remain to be established.The Lancet 07/2004; 363(9425):1977-87. · 39.21 Impact Factor
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ABSTRACT: Growth hormone (GH) is an important regulator of growth and body composition. It has been shown that GH release can be promoted by administration of various amino acids (AAs), such as arginine and lysine, that are present in soy protein. We previously showed that oral ingestion of soy protein stimulates the GH release, it is not known however to which extent other proteins stimulate the GH secretion. Ingestion of soy protein (soy), gelatin protein (gelatin), alpha-lactalbumin protein (alpha-lactalbumin) and milk protein (milk) were compared on their GH-stimulating capacity. After oral ingestion of protein (0.6 g protein per kg bodyweight), blood was sampled every 20 min for 5 h to analyze GH, AA, insulin and glucose concentrations. The study was performed in eight healthy women (aged 19-26 years; body mass index 19-26 kg/m(2)) in a randomized, single blind, placebo-controlled crossover design. GH responses were more increased after ingestion of gelatine (8.2+/-1.1 microg/l) compared with ingestion of soy, alpha-lactalbumin and milk (5.0+/-0.8, 4.5+/-0.6 and 6.4+/-1.0 microg/l, respectively) (P<0.05). After ingestion of each protein, GH responses were higher compared with placebo ingestion (P<0.05). Simultaneously ingestion of gelatin resulted in the highest serum-arginine concentrations (ARG) compared with after ingestion of the other proteins (P<0.05). Insulin as well as glucose concentrations were not different after ingestion of the various proteins (P<0.05). The GH-promoting activity of protein depends on the protein source, in that, gelatin protein is the most potent GH stimulator. Arginine may be the responsible AA in the GH-promoting effect of gelatin, although each protein may have its own specific AA-spectrum involved in the stimulation of the somatotropic axis.European journal of clinical nutrition 03/2010; 64(5):441-6. · 3.07 Impact Factor
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