Naturally-occurring pituitary growth hormone is phosphorylated

Liberti, J.P.; Antoni, Beth Ann; Chlebowski, J F

doi:10.1016/0006-291x(85)90105-6

Cited by 36 publications

(12 citation statements)

References 13 publications

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“…In other mammals (rat and sheep) and chicken, the presence of phosphorylated GH has been demonstrated by various laboratories. Liberti et al showed that after addition of 32 P-labeled ATP to pituitary extracts, labeling of GH occurred [31,32]. It was later found that addition of protein kinase A (PKA) and 32 P-labeled ATP to chicken pituitary protein extracts would generate a radiolabeled GH, therefore suggesting that PKA is the protein kinase responsible for phosphorylation of chicken GH [33].…”

Section: Somatotropinmentioning

confidence: 99%

Phosphoproteomic analysis of the human pituitary

et al. 2006

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The pituitary is the central endocrine gland that regulates the functions of various target organs in the human body. Because of the pivotal regulatory role of the pituitary, it is essential to define on a global scale the components of the pituitary protein machinery, including a comprehensive characterization of the post-translational modifications of the pituitary proteins. Of particular interest is the examination of the phosphorylation status of the pituitary in health and disease. Towards the goal of global profiling of pituitary protein phosphorylation, we report here the application of the in-gel IEF-LC-MS/MS approach to the study of the pituitary phosphoproteome. The analytical strategy combined isoelectric focusing in immobilized pH gradient strips with immobilized metal ion affinity chromatography and mass spectrometry. With this method, a total of 50 phosphorylation sites were characterized in 26 proteins. Because the investigation involved primary tissue, the findings provide a direct glimpse into the phosphoprotein machinery operating within the human pituitary tissue microenvironment.

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Section: Somatotropinmentioning

confidence: 99%

Phosphoproteomic analysis of the human pituitary

et al. 2006

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“…Phosphorylation. A small number of biologically active peptides and precursors, notably ACTH Eipper & Mains, 1982), growth hormone (Liberti, Antoni & Chlebowski, 1985;Liberti & Joshi, 1986), prolactin (Oetting, Tuazon, Traugh & Walker, 1986), progastrin ) and proenkephalin-derived peptide B (D' Souza & Lindberg, 1988) have been found to occur naturally in phosphorylated forms. Physiological casein kinase phosphorylation of serine or threonine may occur when glutamic or aspartic acid is situated two residues Cterminally (Mercier, Grosclaude & Ribadeau Dumas, 1972;Pinna, Meggio & Donella-Deana, 1980).…”

Section: Prosthetic Modificationsmentioning

confidence: 99%

Post‐translational Modification of Peptide Messengers in the Gut

Dimaline

1988

Exp Physiol

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Classical methods such as precursor isolation, cell-free translation and pulse-chase experiments have been of limited use in studying biosynthesis of gastrointestinal peptides, because cell populations are generally sparse and intermingled with other cell types, rates of peptide turnover are low, and levels of mRNA are generally low. However, with the advent of recombinant DNA technology, and its application in predicting precursor sequences, the opportunity has arisen for an alternative approach to the study of propeptides. The success of this approach has to some extent resulted in the eclipse of studies of post-translational processing, although they are still of considerable physiological importance. Study of gastrointestinal peptides is proving a fruitful source of information about the mechanisms involved, as is now clear from recent work on the precursors for gastrin, cholecystokinin (CCK) and vasoactive intestinal peptide (VIP).This review will focus upon these three precursors to illustrate the important features and the physiological significance of post-translational processing, and to outline the strategies currently used to identify the structural modifications which take place in the synthesis of the peptides. Examples will also be drawn where appropriate from other precursors.

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“…The data presented here provide evidence that phosphorylation of GH and prolactin is a feature not restricted to the few mammals investigated (Liberti et al 1985;Liberti & Joshi, 1986;Oetting et al 1986). Phosphorylation of these avian hormones suggests that this is a feature present in all ver¬ tebrates.…”

Section: Discussionmentioning

confidence: 49%

“…However, turkey prolactin showed a ratio of 0.68 nmol PO^nmol protein, suggesting that almost two-thirds of the turkey prolactin molecules present in the preparation employed may contain esterified phosphate. Some mammalian GH is phosphorylated (Liberti et al 1985;Liberti & Joshi, 1986). Recently it has also been shown that the charge heterogeneity of salmon GH seems to be related to its phosphate content, since treatment of the purified salmon GH with alkaline phosphatase appears to eliminate most of the charge variants of the hormone when analysed by two-dimensional electrophoresis (Skibeli et al 1990).…”

Section: Discussionmentioning

confidence: 99%

“…A phosphorylated form of GH has been described in both sheep and rats (Liberti, Antoni & Chlebowski, 1985;Liberti & Joshi, 1986). Recently, it has been shown that purified Atlantic salmon GH can be phosphorylated in vitro by a calmodulin-dependent protein kinase and that the charge heterogeneity of salmon GH may be related to phosphorylation, since the charge heterogeneity observed in two-dimen¬ sional electrophoresis disappears after treatment of salmon GH with alkaline phosphatase (Skibeli, Andersen & Gautvik, 1990).…”

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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Naturally-occurring pituitary growth hormone is phosphorylated

Cited by 36 publications

References 13 publications

Phosphoproteomic analysis of the human pituitary

Phosphoproteomic analysis of the human pituitary

Post‐translational Modification of Peptide Messengers in the Gut

Phosphorylation of prolactin and growth hormone

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