Heterogeneity of Growth Hormone

Baumann, Gerhard

doi:10.1007/978-1-4684-5505-2_2

Cited by 9 publications

(2 citation statements)

References 108 publications

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“…Charge heterogeneity has been described pre¬ viously for several adenohypophysial hormones, with GH and prolactin having been studied to some extent (reviewed by Lewis, 1984). This charge heterogeneity may be related to post-translational modifications, among which the most relevant would be proteolytic processing, N-acylation, deamidation, glycosylation or phosphorylation (Baumann, 1988;Lewis, Singh, Lewis & Abadi, 1988). It is likely that this molecular heterogeneity is a feature of GH and prolactin in all vertebrates, however, studies have been largely restricted to mammals.…”

Section: Discussionmentioning

confidence: 96%

“…The bases of this molecular diversity include gene multiplicity; differential mRNA splicing; posttranslational modification (deamidation, phos¬ phorylation, glycosylation, etc. ); agreggation; degradative processes and protein-protein interac¬ tion (Baumann, 1988). The majority of the studies regarding GH and prolactin variants have been performed in mammals and there is little infor¬ mation from other classes of vertebrate.…”

Section: Introductionmentioning

confidence: 99%

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Phosphorylation of prolactin and growth hormone

Arámburo¹,

Montiel²,

Proudman³

et al. 1992

Journal of Molecular Endocrinology

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To determine whether GH and prolactin could be phosphorylated, turkey GH, chicken GH, chicken prolactin and turkey prolactin were incubated in vitro with the catalytic subunit of protein kinase A and [gamma-32P]ATP. Phosphorylation was assessed after sodium dodecyl sulphate-polyacrylamide gel electrophoresis, Western blotting and autoradiography. Polyacrylamide electrophoresis showed that both purified native chicken GH and turkey GH were phosphorylated under the conditions employed. However, the glycosylated variant of chicken GH did not appear to be labelled. Chicken prolactin, turkey prolactin and the glycosylated variant of turkey prolactin were all intensely phosphorylated by protein kinase A. Ovine and rat prolactins could also be phosphorylated by protein kinase A. The phosphate content of different native prolactin (turkey, ovine and rat) and GH (ovine and chicken) preparations was also determined and found to be significant. Chicken pituitary cells in primary culture incorporated 32P in GH- and prolactin-like bands isolated by non-denaturing polyacrylamide gel electrophoresis, and this was stimulated by phorbol myristate acetate. Phosphorylation of GH and prolactin may thus explain some of the charge heterogeneity of these hormones.

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Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Phosphorylation of prolactin and growth hormone

Arámburo¹,

Montiel²,

Proudman³

et al. 1992

Journal of Molecular Endocrinology

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Growth Disorders

Lee¹,

Muzumdar²,

Saenger³

2012

Textbook of Clinical Pediatrics

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Contribution of hGH20K variant to blood hGH response in sauna and exercise

Doré

Brisson

Fournier

et al. 1991

Europ. J. Appl. Physiol.

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Exercise-induced increases in blood somatotropin (hGH) have always been considered in terms of quantity of the circulating molecules. Knowing that the hypophysis can release several GH species, we investigated the differential release in blood of total hGH (hGHT) and the main hGH variant (hGH20K) molecules in six trained male swimmers exposed to three different conditions known to favor GH release in blood: 45 min--70% maximum oxygen uptake (VO2max) bicycling and swimming, and 20 min of sauna bathing. Based on the binding specificity of hGH antibodies, hGH20K was isolated then assayed using the Nichols immunoradiometric assay system. All three experimental conditions produced significant (P less than 0.001) elevations in blood hGHT and hGH20K. In all three cases, mean blood hGH20K contribution to blood hGHT was relatively constant (11.9, SE 0.7%). Rises in rectal temperature were not statistically related to the changes in blood hGHT. This demonstration of a relatively constant elevation in hGH20K during bicycling, swimming, and sauna bathing can hardly explain the large differences in blood hGHT responses reported in literature under similar conditions.

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Heterogeneity of Growth Hormone

Cited by 9 publications

References 108 publications

Phosphorylation of prolactin and growth hormone

Phosphorylation of prolactin and growth hormone

Growth Disorders

Contribution of hGH20K variant to blood hGH response in sauna and exercise

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