Isoforms of turkey prolactin: Evidence for differences in glycosylation and in tryptic peptide mapping

Corcoran, David; Proudman, J. A.

doi:10.1016/0305-0491(91)90338-e

Cited by 24 publications

(12 citation statements)

References 25 publications

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“…The isoforms of PRL detected by Western blotting correspond to those previously detected in pituitary gland from adult turkey hens [29]. These isoforms are consistent with the G-and NG-PRL isoforms described by Corcoran and Proudman [28] with the 27-kDa and 24-kDa forms corresponding to the G-and NG-PRL forms, respectively. In our experiment, the proportion of G-versus NG-PRL appeared to fluctuate during embryonic development.…”

Section: Discussionsupporting

confidence: 83%

“…Glycosylation represents a major mechanism for modification of PRL; glycosylated (G)-PRLs have different binding and biological characteristics [25], and the relative proportion of PRL isoforms can vary with the status of the animal [26,27]. In turkey hens, PRL is present in the pituitary gland in 3 different isoforms, 1 nonglycosylated (NG)-PRL and 2 G-PRLs, which comigrate on SDS-PAGE [28]. The ratio of G-PRL to NG-PRL has been shown to fluctuate with the reproductive status of the animal [29].…”

Section: Introductionmentioning

confidence: 98%

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Quantification of Prolactin Messenger Ribonucleic Acid, Pituitary Content and Plasma Levels of Prolactin, and Detection of Immunoreactive Isoforms of Prolactin in Pituitaries from Turkey Embryos During Ontogeny1

Bédécarrats¹,

Guemene²,

Morvan³

et al. 1999

Biology of Reproduction

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The content of prolactin mRNA as well as total prolactin content and type of isoforms of prolactin were measured in single pituitary glands from turkey embryos and poults. Levels of mRNA and pituitary content of prolactin remained low until 5 days before hatching, while plasma concentrations remained low until 2 days before hatching. Levels of prolactin mRNA then increased until the day of hatch, stayed stable during the 3 first days of age, and significantly increased until 2 wk of age. Similar changes were observed in pituitary content and plasma levels of prolactin. Two immunoreactive bands of apparent molecular masses of 24 and 27 kDa, corresponding to the nonglycosylated and glycosylated form of prolactin, respectively, were visualized on Western blots. In pituitary glands from embryos at 22 days of incubation, 31.5% of the protein was glycosylated, whereas in embryos at 27 days of incubation and poults at 1 and 7 days of age, 48.6%, 48.0%, and 56. 0% of prolactin was glycosylated, respectively. The results indicate that the increases in the synthesis and the release of prolactin occur mainly around and after the time of hatching in the turkey embryo. Higher percentages of glycosylated isoforms were associated with increasing levels of total prolactin in the pituitary gland. Thus, the synthesis of prolactin and its post-translational modifications may be important factors involved in the physiologic changes occurring around the time of hatching.

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Section: Discussionsupporting

confidence: 83%

Section: Introductionmentioning

confidence: 98%

Quantification of Prolactin Messenger Ribonucleic Acid, Pituitary Content and Plasma Levels of Prolactin, and Detection of Immunoreactive Isoforms of Prolactin in Pituitaries from Turkey Embryos During Ontogeny1

Bédécarrats¹,

Guemene²,

Morvan³

et al. 1999

Biology of Reproduction

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“…3). The slightly larger putative variant of turkey pro¬ lactin has been shown to bind Concanavalin A, suggesting that it is a glycoprotein (Corcoran & Proudman, 1991). These data support a size hetero¬ geneity for turkey prolactin and the existence of a glycosylated turkey prolactin.…”

Section: Discussionsupporting

confidence: 50%

“…The following hormones were employed in these studies: chicken GH (Arámburo et al 19896); turkey GH, obtained by chromatofocusing (Proudman & Opel, 1990); glycosylated chicken GH (prepared by the method of Berghman et al 1987), chicken prolactin (AFP-4444B, kindly donated by Dr. A. F. Parlow, Pituitary Hormones and Antisera Center, Torrance, CA, U.S.A.); ovine GH (NIDDKoGH-13), ovine prolactin (NIDDK-oPRL-17); rat prolactin (NIDDK-rPRL-B6; all obtained from the National Hormone and Pituitary Program, NIDDK, Baltimore, MD, U.S.A.) and turkey prolactin, which contained both the holoprotein and the glycosylated variant of the hormone (Corcoran & Proudman, 1991). The ability of each of these hormones to be phosphorylated in vitro by protein kinase A was examined, following the method of Oetting et al (1986) with some modifications.…”

Section: Phosphorylation Of Hormones In Vitromentioning

confidence: 99%

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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“…[18], NaK-ATPase subunit levels were determined using the SDS-polyacrylamide gel electrophoresis, Western blot and slot blot analysis [30]. The cell samples were denatured in a solution containing 8 M urea, 50 mg/ml dithiothreitol, and 0.01 M H3PO4, pH 6.8 overnight at room temperature [2]. 4 pg protein from each of the cell samples was applied to a 7.0% SDS-polyacrylamide gel and run at a current of 40 mA for approximately 2 h. Protein samples in the polyacrylamide gel were then transferred to a polyvinylidene difluoride (PVDF) membrane (Millipore Inc., Bedford, Mass., USA) using a semidry blotting system (Pharmacia, Piscataway, N.J., USA) at a current of 0.8 mA/cm2 for 2 h. NaK-ATPase subunits were quan tified by means of a immunochemiluminescent procedure (Tropix, Inc.).…”

Section: Introductionmentioning

confidence: 99%

Regulation of NaK-ATPase by Platelet-Derived Growth Factors in Cultured Rat Thoracic Aortic Smooth Muscle Cells

Lo¹

1996

J Biomed Sci

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Regulation of (Na^+ + K^+)-adenosine triphosphatase (NaK-ATPase) by platelet- derived growth factor (PDGF) in cultured rat thoracic aortic smooth muscle cells (SMC) was examined. PDGF-BB enhances SMC proliferation and NaK-ATPase activity. Ouabain, an inhibitor of NaK-ATPase activity, prevents PDGF-BB-induced SMC proliferation. As shown by Western blot and immunochemiluminescence analysis, PDGF-BB also enhances α(1), truncated α(1), and β(1) NaK-ATPase subunit levels. PDGF-AA and PDGF-AB show no effect on α(1) and truncated ai levels in slot blot analysis. Induction of NaKATPase subunit levels by PDGF-BB could be one of the initial events in vascular SMC proliferation.

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Isoforms of turkey prolactin: Evidence for differences in glycosylation and in tryptic peptide mapping

Cited by 24 publications

References 25 publications

Quantification of Prolactin Messenger Ribonucleic Acid, Pituitary Content and Plasma Levels of Prolactin, and Detection of Immunoreactive Isoforms of Prolactin in Pituitaries from Turkey Embryos During Ontogeny1

Quantification of Prolactin Messenger Ribonucleic Acid, Pituitary Content and Plasma Levels of Prolactin, and Detection of Immunoreactive Isoforms of Prolactin in Pituitaries from Turkey Embryos During Ontogeny1

Phosphorylation of prolactin and growth hormone

Regulation of NaK-ATPase by Platelet-Derived Growth Factors in Cultured Rat Thoracic Aortic Smooth Muscle Cells

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