Processing of chromogranin A in the parathyroid: generation of parastatin-related peptides

Fasciotto, Brigitte H.; Denny, Joshua C.; Greeley, George H.; Cohn, David V.

doi:10.1016/s0196-9781(00)00283-7

Cited by 20 publications

(20 citation statements)

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“…Several distinct biological activities have been assigned to the catestatin domain, i.e., inhibiting catecholamine secretion from bovine chromaffin cells [36], PTH secretion from porcine parathyroid cells [33,117] and bacterial and fungal growth [55], while activating histamine release in a mastoparan-like manner from rat mast cells [93]. Unlike the helical structure of mastoparan [118], the primary sequence of human catestatin, ssmklsfrar aygfrgpgpql, forms a loosely coiled structure with an electropositive Arg-rich loop that stabilizes the hydrophobic form assumed to be essential for its catechol- amine release-inhibitory action [115].…”

Section: Catestatinmentioning

confidence: 99%

“…While the release of PTH is stimulated by low plasma Ca 2+ levels or IL-8 via the CXC2 type of G protein coupled receptor at normal, 1 mM Ca 2+ [139], it is inhibited via two different pathways, (1) by high plasma Ca 2+ activating the calcium sensor [140], and (2) by three of the CgAderived peptides at low plasma Ca 2+ , namely VS-I and CgA 1-40 [38,102,103], PST [141,142] and parastatin [33,117]. The inhibitory mechanism for high plasma Ca 2+ in human parathyroid cells involves an increase in intracellular Ca 2+ sufficient for enhanced efflux of K + via a tetraethylammonium (TEA)-sensitive, calcium-regulated K + channel [140].…”

Section: Catestatinmentioning

confidence: 99%

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The endocrine role for chromogranin A: A prohormone for peptides with regulatory properties

Helle

Corti²,

Metz‐Boutigue

et al. 2007

Cell. Mol. Life Sci.

183

194

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Chromogranin A (CgA) belongs to the granin family of uniquely acidic secretory proteins co-stored and co-secreted with other hormones and peptides in elements of the diffuse neuroendocrine system. The granins arise from different genes and are characterized by numerous sites for post-translational cleavage into shorter peptides with postulated regulatory properties. This review is directed towards endocrine aspects of CgA and its biologically active peptides. There is ample evidence from in vitro studies of distinct effects and targets for three CgA-derived peptides, vasostatin-I, pancreastatin and catestatin. Endocrine regulations are indicated from in vivo studies, consistent with the postulated prohormone function of CgA for peptides with regulatory properties. Most of the effects fit into patterns of direct or indirect, inhibitory modulations of major functions, implicating CgA peptides in regulation of calcium and glucose metabolism, cardiovascular functions, gastrointestinal motility and nociception, tissue repair, inflammatory responses and as host defense peptides in the first phase of microbial invasions.

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Section: Catestatinmentioning

confidence: 99%

Section: Catestatinmentioning

confidence: 99%

The endocrine role for chromogranin A: A prohormone for peptides with regulatory properties

Helle

Corti²,

Metz‐Boutigue

et al. 2007

Cell. Mol. Life Sci.

183

194

View full text Add to dashboard Cite

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“…In corroborating experiments, Moallem et al (1998) found that hypocalcemia (and hyperphosphatemia) increased PTH mRNA stability by changing the ability of cytosolic proteins to bind the PTH mRNA 3 -untranslated region in rats. Factors not evaluated in this study that may affect PTH mRNA expression, synthesis, and secretion, include endothelin 1, PTH fragments, chromogranin A and its bioactive peptides, phosphate, vitamin D, and other calcium-sensing proteins such as megalin/gp330/LRP-2 (Fujii et al 1991, Fujimi et al 1991, Lundgren et al 1994, Kilav et al 1995, Slatopolsky & Delmez 1996, Fasciotto et al 2000.…”

Section: Discussionmentioning

confidence: 99%

Parathyroid hormone (PTH) secretion, PTH mRNA and calcium-sensing receptor mRNA expression in equine parathyroid cells, and effects of interleukin (IL)-1, IL-6, and tumor necrosis factor-alpha on equine parathyroid cell function

Toribio¹,

Kohn²,

Capen³

et al. 2003

Journal of Molecular Endocrinology

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Parathyroid hormone (PTH) is secreted by the chief cells of the parathyroid gland in response to changes in ionized calcium (Ca 2+ ) concentrations. In this study, we measured PTH secretion, and PTH mRNA and calcium-sensing receptor (CaR) mRNA expression by equine parathyroid chief cells in vitro. We also evaluated the effects of interleukin (IL)-1 , IL-6, and tumor necrosis factor (TNF)-on PTH secretion, and PTH and CaR mRNA expression. The relationship between PTH and Ca 2+ was inversely related. PTH secretion decreased from 100% (day 0) to 13% (day 30). PTH mRNA expression declined from 100% (day 0) to 25% (day 30). CaR mRNA decreased from 100% (day 0) to 16% (day 30). Chief cells exposed to high (2·0 mM) Ca 2+ concentrations had a lower PTH mRNA expression compared with low Ca 2+ concentrations. Ca 2+ concentrations had no effect on CaR mRNA expression. The inhibitory effect of high Ca 2+ concentrations on PTH secretion also declined over time. After day 10, there was no significant difference in PTH secretion between low and high Ca 2+ concentrations. IL-1 decreased both PTH secretion (75%) and PTH mRNA expression (73%), and resulted in a significant overexpression of CaR mRNA (up to 142%). The effects of IL-1 were blocked by an IL-1 receptor antagonist. IL-1 decreased the Ca 2+ set-point from 1·4 mM to 1·2 mM. IL-6 decreased PTH secretion (74%), but had no effect on PTH and CaR mRNA expression. TNF-had no effect on PTH secretion, and PTH and CaR mRNA expression. In summary, the decreased responsiveness of parathyroid cells to Ca 2+ from 0 to 30 days can be explained, in part, by the reduced CaR expression. IL-1 and IL-6 but not TNF-affected parathyroid function in vitro and may be important in influencing PTH secretion in the septic horse.

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“…Processing of CgA to CAT occurs by intraand extracellular processing (Parmer et al 2000;Biswas et al 2008). Biological activity has been assigned to CAT in a number of tissues such as bovine chromaffin cells (Mahata et al 1997), the human baroreceptor centre of the nucleus tractus solitarius (Mahapatra 2008), porcine parathyroid cells (Fasciotto et al 2000), rat mast cells (Krüger et al 2003) in frog (Mazza et al 2008) and rat heart , and in Gram-positive and negative bacteria (Briolat et al 2005;Radek et al 2008). …”

Section: Cgamentioning

confidence: 99%

Chromogranins A and B and Secretogranin II as Prohormones for Regulatory Peptides from the Diffuse Neuroendocrine System

Helle

2010

Results and Problems in Cell Differentiation

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Chromogranin A (CgA), chromogranin B (CgB), and secretogranin II (SgII) belong to a family of uniquely acidic secretory proteins in elements of the diffuse neuroendocrine system. These "granins" are characterized by numerous pairs of basic amino acids as potential sites for intra- and extragranular processing. In response to adequate stimuli, the granins are coreleased with neurotransmitters and hormones and appear in the circulation as potential modulators of homeostatic processes. This review is directed towards functional aspects of the secreted CgA, CgB, and SgII and their biologically active sequences. Widely different effects and targets have been reported for granin-derived peptides. So far, the CgA peptides vasostatin-I, pancreastatin, and catestatin, the CgB peptides CgB(1-41) and secretolytin, and the SgII peptide secretoneurin are the most likely candidates for granin-derived regulatory peptides. Most of their effects fit into patterns of direct or indirect modulations of major functions, in particular associated with inflammatory conditions.

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Processing of chromogranin A in the parathyroid: generation of parastatin-related peptides

Cited by 20 publications

References 50 publications

The endocrine role for chromogranin A: A prohormone for peptides with regulatory properties

The endocrine role for chromogranin A: A prohormone for peptides with regulatory properties

Parathyroid hormone (PTH) secretion, PTH mRNA and calcium-sensing receptor mRNA expression in equine parathyroid cells, and effects of interleukin (IL)-1, IL-6, and tumor necrosis factor-alpha on equine parathyroid cell function

Chromogranins A and B and Secretogranin II as Prohormones for Regulatory Peptides from the Diffuse Neuroendocrine System

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