Changes in Parathyroid Hormone-Related Peptide Receptor Binding in the Shell Gland of Laying Hens (Gallus domesticus) during the Oviposition Cycle

Ieda, Teruko; Takahashi, Tetsuya; Sakai, Noboru; Yasuoka, Tadashi; Kawashima, Mitsuo; Shimada, Kiyoshi

doi:10.1006/gcen.1999.7395

Cited by 12 publications

(4 citation statements)

References 7 publications

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“…Binding assays were performed as previously reported for avian cell membranes (Ieda et al 2000;Yasuoka et al 1996). All assays were carried out in triplicate at 4°C for 2 h in microcentrifuge tubes pre-treated with TE supplemented with 2% bovine serum albumin (Sigma-Aldrich) and with 30 μg protein/tube of membrane fractions in TE buffer to give a final incubation volume of 300 μl.…”

Section: Binding Assaymentioning

confidence: 99%

Ligand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytes

et al. 2005

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Whole animal studies have indicated that Ca(2+) uptake by the gastrointestinal tract is regulated by the action of parathyroid hormone-related peptide (PTHrP) in teleost fish. We have characterised PTH receptors (PTHR) in piscine enterocytes and established, by using amino-terminal PTHrP peptides, the amino acid residues important for receptor activation and for stabilising the ligand/receptor complex. Ligand binding of (125)I-(1-35(tyr)) PTHrP to the membrane fraction of isolated sea bream enterocytes revealed the existence of a single saturable high-affinity receptor (K (D)=2.59 nM; B (max)=71 fmol/mg protein). Reverse transcription/polymerase chain reaction with specific primers for sea bream PTH1R and PTH3R confirmed the mRNA expression of only the later receptor. Fugu (1-34)PTHrP increased cAMP levels in enterocytes but had no effect on total inositol phosphate accumulation. The amino-terminal peptides (2-34)PTHrP, (3-34)PTHrP and (7-34)PTHrP bound efficiently to the receptor but were severely defective in stimulating cAMP in enterocyte cells indicating that the first six residues of piscine (1-34)PTHrP, although not important for receptor binding, are essential for activation of the adenylate cyclase/phosphokinase A (AC-PKA)-receptor-coupled intracellular signalling pathway. Therefore, PTHrP in teleosts acts on the gastrointestinal tract through PTH3R and the AC-PKA intracellular signalling pathway and might regulate Ca(2+) uptake at this site. Ligand-receptor binding and activity throughout the vertebrates appears to be allocated to the same amino acid residues of the amino-terminal domain of the PTHrP molecule.

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Section: Binding Assaymentioning

confidence: 99%

Ligand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytes

et al. 2005

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“…The B max value, calculated by Scatchard analysis, was in the order of 10 −14 mol/mg of protein, which suggests that the specific cPTHrP binding component found in the anterior pituitary had a limited capacity. Orders of magnitude of the K d (10 −10 M) and B max (10 −14 M) values were close to those of the K d and B max values of cPTHrP receptor found in the calvarial bone, kidney (Yasuoka et al, 1996), shell glands (Ieda et al, 2000), and adrenocortical cells (Kawashima et al, 2005) of the chicken, and in the shell glands of the guinea fowl (Ogawa et al, 2000). Therefore, the binding component for cPTHrP in plasma membrane fractions of the anterior pituitary is likely to be a receptor for cPTHrP.…”

Section: Discussionmentioning

confidence: 60%

“…The primary role of these hormones is to maintain calcium homeostasis (Yates et al, 1988) with calcitonin (Kenny, 1986) and vitamin D (Savaram et al, 2008;Bar, 2009). Parathyroid hormone-related peptide receptor has been found in the calvarial bone and kidney of the chicken (Yasuoka et al, 1996), shell glands of the chicken (Ieda et al, 2000) and the guinea fowl (Ogawa et al, 2000), and adrenocortical cells of the chicken (Kawashima et al, 2005). Parathyroid hormone-related peptide stimulates bone resorption and increases renal tubular reabsorption of calcium (Yates et al, 1988).…”

Section: Introductionmentioning

confidence: 97%

Parathyroid hormone-related peptide directly increases adrenocorticotropic hormone secretion from the anterior pituitary in hens

Nakayama¹,

Takahashi

Oomatsu³

et al. 2011

Poultry Science

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The presence of the receptor for parathyroid hormone-related peptide (PTHrP) and the effect of PTHrP on adrenocorticotropic hormone (ACTH) secretion in the hen anterior pituitary were examined. The plasma membrane fraction of the anterior pituitary was found to contain a specific chicken PTHrP (cPTHrP) binding component. The binding component had properties of a receptor, such as binding specificity to cPTHrP, reversibility, saturable binding, high affinity, and limited capacity; therefore, it was elucidated that the PTHrP receptor exists in the plasma membrane of the hen anterior pituitary. A third ventricular injection of cPTHrP in nonlaying hens caused a decrease in the chicken ACTH level of the anterior pituitary and an increase in the chicken ACTH level of blood plasma, with an increase in the binding affinity and a decrease in the binding capacity of PTHrP receptor in the anterior pituitary. The present study suggests that PTHrP may act directly on the anterior pituitary via its receptor binding and may enhance ACTH secretion from this tissue in hens.

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“…In amphibians, PTH/PTHrP receptors have been characterized and an immunoreactive PTHrP-like peptide with widespread tissue distribution has been detected [24,25]. In chicken, PTH and PTHrP homologues have also been isolated and are involved in chondroblast and osteoblast differentiation, although their role in calcium transport mechanisms is poorly understood [26-31]. Amphibians and birds occupy unique phylogenetic positions, the former at the transition of aquatic to terrestrial life, the latter at the transition to homeothermy, and both organisms have a complex system in calcium regulation.…”

Section: Introductionmentioning

confidence: 99%

Gene structure, transcripts and calciotropic effects of the PTH family of peptides in Xenopus and chicken

et al. 2010

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BackgroundParathyroid hormone (PTH) and PTH-related peptide (PTHrP) belong to a family of endocrine factors that share a highly conserved N-terminal region (amino acids 1-34) and play key roles in calcium homeostasis, bone formation and skeletal development. Recently, PTH-like peptide (PTH-L) was identified in teleost fish raising questions about the evolution of these proteins. Although PTH and PTHrP have been intensively studied in mammals their function in other vertebrates is poorly documented. Amphibians and birds occupy unique phylogenetic positions, the former at the transition of aquatic to terrestrial life and the latter at the transition to homeothermy. Moreover, both organisms have characteristics indicative of a complex system in calcium regulation. This study investigated PTH family evolution in vertebrates with special emphasis on Xenopus and chicken.ResultsThe PTH-L gene is present throughout the vertebrates with the exception of placental mammals. Gene structure of PTH and PTH-L seems to be conserved in vertebrates while PTHrP gene structure is divergent and has acquired new exons and alternative promoters. Splice variants of PTHrP and PTH-L are common in Xenopus and chicken and transcripts of the former have a widespread tissue distribution, although PTH-L is more restricted. PTH is widely expressed in fish tissue but from Xenopus to mammals becomes largely restricted to the parathyroid gland. The N-terminal (1-34) region of PTH, PTHrP and PTH-L in Xenopus and chicken share high sequence conservation and the capacity to modify calcium fluxes across epithelia suggesting a conserved role in calcium metabolism possibly via similar receptors.ConclusionsThe parathyroid hormone family contains 3 principal members, PTH, PTHrP and the recently identified PTH-L. In teleosts there are 5 genes which encode PTHrP (2), PTH (2) and PTH-L and in tetrapods there are 3 genes (PTHrP, PTH and PTH-L), the exception is placental mammals which have 2 genes and lack PTH-L. It is hypothesized that genes of the PTH family appeared at approximately the same time during the vertebrate radiation and evolved via gene duplication/deletion events. PTH-L was lost from the genome of eutherian mammals and PTH, which has a paracrine distribution in lower vertebrates, became the product of a specific endocrine tissue in Amphibia, the parathyroid gland. The PTHrP gene organisation diverged and became more complex in vertebrates and retained its widespread tissue distribution which is congruent with its paracrine nature.

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Changes in Parathyroid Hormone-Related Peptide Receptor Binding in the Shell Gland of Laying Hens (Gallus domesticus) during the Oviposition Cycle

Cited by 12 publications

References 7 publications

Ligand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytes

Ligand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytes

Parathyroid hormone-related peptide directly increases adrenocorticotropic hormone secretion from the anterior pituitary in hens

Gene structure, transcripts and calciotropic effects of the PTH family of peptides in Xenopus and chicken

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