Expression of P2Y receptors in the rat anterior pituitary

Yu, Qiang; Guo, Wei; Song, Xianmin; Liu, Xiaofeng; Xiang, Zhenghua; He, Cheng; Burnstock, Geoffrey

doi:10.1007/s11302-011-9236-9

Cited by 10 publications

(11 citation statements)

References 29 publications

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“…Earlier studies with dispersed pituitary cells revealed the presence of this type of receptors in lactotrophs and other non-identified cell type [36]. Immunoreactive P2Y1 receptors were identified in rat thyrotrophs [37] and our experiments shows that mouse TαT1 cells also express functional P2Y1 receptors. In contrast to TRH-responsive lactotrophs, which express P2X4 receptor channels as well [38], the present data suggest that P2X receptor channels capable of generating global calcium signaling are not expressed in TαT1 cells.…”

Section: Discussionsupporting

confidence: 68%

Calcium signaling properties of a thyrotroph cell line, mouse TαT1 cells

Tomić

Bargi‐Souza²,

Leiva-Salcedo

et al. 2015

Cell Calcium

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TαT1 cells are mouse thyrotroph cell line frequently used for studies on thyroid-stimulating hormone beta subunit gene expression and other cellular functions. Here we have characterized calcium-signaling pathways in TαT1 cells, an issue not previously addressed in these cells and incompletely described in native thyrotrophs. TαT1 cells are excitable and fire action potentials spontaneously and in response to application of thyrotropin-releasing hormone (TRH), the native hypothalamic agonist for thyrotrophs. Spontaneous electrical activity is coupled to small amplitude fluctuations in intracellular calcium, whereas TRH stimulates both calcium mobilization from intracellular pools and calcium influx. Non-receptor-mediated depletion of intracellular pool also leads to a prominent facilitation of calcium influx. Both receptor and non-receptor stimulated calcium influx is substantially attenuated but not completely abolished by inhibition of voltage-gated calcium channels, suggesting that depletion of intracellular calcium pool in these cells provides a signal for both voltage-independent and –dependent calcium influx, the latter by facilitating the pacemaking activity. These cells also express purinergic P2Y1 receptors and their activation by extracellular ATP mimics TRH action on calcium mobilization and influx. The thyroid hormone triiodothyronine prolongs duration of TRH-induced calcium spikes during 30-min exposure. These data indicate that TαT1 cells are capable of responding to natively feed-forward TRH signaling and intrapituitary ATP signaling with acute calcium mobilization and sustained calcium influx. Amplification of TRH-induced calcium signaling by triiodothyronine further suggests the existence of a pathway for positive feedback effects of thyroid hormones probably in a non-genomic manner.

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Section: Discussionsupporting

confidence: 68%

Calcium signaling properties of a thyrotroph cell line, mouse TαT1 cells

Tomić

Bargi‐Souza²,

Leiva-Salcedo

et al. 2015

Cell Calcium

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“…In human thyrotrophs, ATP stimulates the calcium-phosphatidylinositol cascade, indicating the presence of P2YRs (Raspe et al, 1991). Consistent with these findings, an immunohistochemical study has shown that the majority of rat pituitary thyrotrophs express P2Y1 and P2Y4R (Yu et al, 2011). In addition, pharmacological evidence points to the presence of A 1 R and A 2a R in thyrotrophs.…”

Section: Purinergic Regulation Of the Hypothalamic-pituitary-thyrosupporting

confidence: 54%

“…Immunohistochemical analysis suggested that P2Y 1 R and P2Y 4 R are expressed in gonadotrophs (Yu et al, 2011) and single cell calcium analysis proposed the expression of P2Y 2 R in these cells (Chen et al, 1995; Chen et al, 1996a; Chen et al, 1996b; Chen et al, 1994). However, electrophysiological analysis in gonadotrophs from embryonic, neonatal, and adult rats revealed that ATP application generates a depolarizing and non-oscillatory current, in contrast to calcium-mobilizing GnRH that triggered an oscillatory hyperpolarizing current driven by small calcium-controlled potassium channels (Stojilkovic et al, 2010b).…”

Section: Purinergic Regulation Of the Hypothalamic-pituitary-gonadmentioning

confidence: 99%

Purinergic signaling pathways in endocrine system

Bjelobaba

Janjic

Stojilković

2015

Autonomic Neuroscience

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Adenosine-5′-triphosphate is released by neuroendocrine, endocrine, and other cell types and acts as an extracellular agonist for ligand-gated P2X cationic channels and G protein-coupled P2Y receptors in numerous organs and tissues, including the endocrine system. The breakdown of ATP by ectonucleotidases not only terminates its extracellular messenger functions, but also provides a pathway for the generation of two additional agonists: adenosine 5′-diphosphate, acting via some P2Y receptors, and adenosine, a native agonist for G protein-coupled adenosine receptors, also expressed in the endocrine system. This article provides a review of purinergic signaling pathways in the hypothalamic magnocellular neurosecretory cells and neurohypophysis, hypothalamic parvocellular neuroendocrine system, adenohypophysis, and effector glands organized in five axes: hypothalamic-pituitary-gonadal, hypothalamic-pituitary-thyroid, hypothalamic-pituitary-adrenal, hypothalamic-pituitary-growth hormone, and hypothalamic-pituitary-prolactin. We attempted to summarize current knowledge of purinergic receptor subtypes expressed in the endocrine system, including their roles in intracellular signaling, hormone secretion, and other cell functions. We also briefly review the release mechanism for adenosine-5′-triphosphate by neuroendocrine, endocrine and surrounding cells, the enzymes involved in adenosine-5′-triphosphate hydrolysis to adenosine-5′-diphosphate and adenosine, and the relevance of this pathway for sequential activation of receptors and termination of signaling.

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“…Of the remaining two tested antibodies, the Santa Cruz reagent was used with seemingly good results in mouse skeletal muscle (Chen et al, 2011) and in rat anterior pituitary (Yu et al, 2011a) and for the MBL antibody we could not find specific references of its use, but Jiang et al demonstrated apparently specific staining with an antibody made to the same epitope (Jiang et al, 2009). …”

Section: Discussionmentioning

confidence: 99%

Lack of specificity shown by P2Y6 receptor antibodies

Hill

2013

Naunyn-Schmiedeberg's Arch Pharmacol

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P2Y6 receptor in bladder smooth muscle responds to UDP by increasing muscle tone and augmenting bladder contractions. The exact cellular location of the receptor is however unknown. Three commercially available antibodies to P2Y6 receptor gave clean bands on Western blot which were eliminated by specific peptide competition. Two of the three also immunostained bladder smooth muscle cells while leaving adjacent interstitial cells of Cajal unstained. However, attempts to validate the specificity of these antibodies by performing the same assays on bladders from P2Y6 knockout mice were unsuccessful. In Western blots, all three antibodies bound similar proteins in both wild type and P2Y6 knockout tissue. Immunostaining of knockout tissue sections also showed no difference in staining patterns or intensity. We conclude that rigorous controls are required when using commercial reagents to this G-protein coupled receptor and perhaps to other members of the P2Y receptor family.

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Expression of P2Y receptors in the rat anterior pituitary

Cited by 10 publications

References 29 publications

Calcium signaling properties of a thyrotroph cell line, mouse TαT1 cells

Calcium signaling properties of a thyrotroph cell line, mouse TαT1 cells

Purinergic signaling pathways in endocrine system

Lack of specificity shown by P2Y6 receptor antibodies

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