Secretoneurin and chemoattractant receptor interactions

Chen, Kong; Gill, Bruce M.; Rahimpour, R.; Xu, Luoling; Feldman, Ross D.; Xiao, Qing; McDonald, Thomas J.; Taupenot, Laurent; Mahata, Sushil K.; Singh, Bhagirath; O’Connor, Daniel T.; Kelvin, David J.

doi:10.1016/s0165-5728(98)00094-0

Cited by 41 publications

(27 citation statements)

References 31 publications

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“…Previous studies demonstrated that SN elevates intracellular calcium concentrations in human monocytes and that the chemotactic activity of SN can be blocked by treatment of cells with PTx (Schratzberger et al 1997;Kong et al 1998). In addition, SN was shown to interact with specific cell surface binding sites on human monocytes (Kong et al 1998). In the present study, SN-evoked neurite outgrowth could be abolished by PTx, indicating the existence of a specific SN receptor on cerebellar granule cells coupled to G i/o -protein.…”

Section: Discussionmentioning

confidence: 99%

“…The SgII mRNA is widely but distinctly distributed in brain ) (Mahata et al 1992) including the cerebellum (Cozzi et al 1989). A number of biological effects of SN have been reported, such as transmitter release (Saria et al 1993;Agneter et al 1995), chemotaxis (Reinisch et al 1993;Kähler et al 1996;Dunzendorfer et al 1998;Kong et al 1998), proliferation (Kähler et al 1997a,b), gonadotropin release from the pituitary (Blazquez et al 1998) and survival of cerebellar granule cells (Fujita et al 1999). Secretoneurinlike immunoreactivity showed a widespread distribution (Marksteiner et al 1993a,b) in endocrine Schmid et al 1995) and nervous tissues (Kirchmair et al 1994;Dun et al 1997) of various species.…”

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confidence: 99%

“…A specific SN receptor has not yet been identified. However, specific high affinity binding sites for SN have been characterized on human monocytes as well as two monocytic cell lines (Kong et al 1998;Schneitler et al 1998). Treatment of monocytes with SN increased intracellular calcium levels and SN-induced chemotaxis was inhibited by pertussis toxin (PTx) as well as by a protein kinase C (PKC) inhibitor , suggesting that SN might act via a classical G-protein-coupled neuropeptide receptor, as with other neuropeptides fully characterized to date.…”

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confidence: 99%

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Secretoneurin promotes pertussis toxin‐sensitive neurite outgrowth in cerebellar granule cells

Gasser¹,

Berti²,

Hauser

et al. 2003

Journal of Neurochemistry

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The neuropeptide secretoneurin (SN) is an endoproteolytic product of the chromogranin secretogranin II. We investigated the effects of SN on the differentiation of immature cerebellar granule cells derived from the external granular layer (EGL). Secretoneurin caused concentration-dependent increases in neurite outgrowth, reflecting differentiation. The maximum effect was reached at a concentration of 100 nM SN. Secretoneurin immunoneutralization using specific antiserum significantly decreased neurite outgrowth; however, neurite morphology was altered. An affinity chromatography-purified antibody significantly inhibited the outgrowth response to SN ( p < 0.001) without altering the morphology. Binding studies suggest the existence of specific G-protein-coupled receptors on the surface of monocytes that recognize SN. Assuming that SN promotes neurite outgrowth in EGL cells by acting through a similar G-protein-coupled mechanism, we treated SN-stimulated EGL cultures with pertussis toxin. Exposure to pertussis toxin (0.1 lg/mL) showed a significant inhibition of the SN-induced outgrowth. To establish a second messenger pathway we used the protein kinase C inhibitor staurosporine. We found that EGL cell viability was not enhanced following chronic SN treatment for 24 h. These data indicate that SN is a novel trophic substance that can affect cerebellar maturation, primarily by accelerating granule cell differentiation through a signalling mechanism that is coupled to pertussis toxin-sensitive G-proteins.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Secretoneurin promotes pertussis toxin‐sensitive neurite outgrowth in cerebellar granule cells

Gasser¹,

Berti²,

Hauser

et al. 2003

Journal of Neurochemistry

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“…1 Extracellularly, they are postulated to serve as prohormones to generate biologically active peptides, which may influence hormonal release 5 and have vascular 6 and chemoattractant functions. 7 Recently, Strub and colleagues 8 demonstrated that several peptides displaying antimicrobial properties (at micromolar range) were naturally generated from CGB and CGA in bovine chromaffin granules. Among these active peptides, secretolytin and vasostatin-1 corresponding to CGB 614-626 and CGA 1-76, respectively, were identified.…”

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confidence: 99%

Presence of chromogranin-derived antimicrobial peptides in plasma during coronary artery bypass surgery and evidence of an immune origin of these peptides

Tasiemski

Hammad

Vandenbulcke

et al. 2002

Blood

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Chromogranin A (CGA) and chromogranin B (CGB) are acidic proteins stored in secretory organelles of endocrine cells and neurons. In addition to their roles as helper proteins in the packaging of pep-tides, they may serve as prohormones to generate biologically active peptides such as vasostatin-1 and secretolytin. These molecules derived from CGA and CGB, respectively, possess antimicrobial properties. The present study demonstrates that plasmatic levels of both vasostatin-1 and secretolytin increase during surgery in patients undergoing cardiopulmonary bypass (CPB). Vasostatin-1 and secretoly-tin, initially present in plasma at low levels , are released just after skin incision. Consequently, they can be added to enk-elytin, an antibacterial peptide derived from proenkephalin A, for the panoply of components acting as a first protective barrier against hypothetical invasion of pathogens, which may occur during surgery. CGA and CGB, more commonly viewed as markers for endocrine and neuronal cells, were also found to have an immune origin. RNA messengers coding for CGB were amplified by reverse transcription-polymerase chain reaction in human monocytes, and immunocyto-chemical analysis by confocal micros-copy revealed the presence of CGA or CGB or both in monocytes and neutro-phils. A combination of techniques including confocal microscopic analysis, mass spectrometry measurement, and antibac-terial tests allowed for the identification of the positive role of interleukin 6 (IL-6) in the secretolytin release from mono-cytes in vitro. Because IL-6 release is known to be strongly enhanced during CPB, we suggest a possible relationship between IL-6 and the increased level of secretolytin in patients undergoing CPB. (Blood. 2002;100:553-559)

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“…However, the relationship between SN and the secretion of airway mucin remains unclear. Furthermore, the specific cell-surface receptor for SN is also unclear, although there is sufficient evidence to support the hypothesis that a G-protein-coupled receptor is involved [10,11,12]. Research has indicated that SN stimulates increases in intercellular calcium and activates both cAMP production and ERK-dependent pathways in LβT2 cells [13,14].…”

Section: Introductionmentioning

confidence: 99%

Secretoneurin Induces Airway Mucus Hypersecretion by Enhancing the Binding of EGF to NRP1

Zhou

et al. 2014

Cell Physiol Biochem

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Aims: Secretoneurin(SN), a neuropeptide, has been considered a reliable marker of allergenic stimulation. However, the relationship between SN and the secretion of airway mucin remains unclear. In this study, we aimed to examine the in vitro relationship between SN and airway mucin over synthesis, as well as the signaling pathways involved. Methods and Results: Exogenous SN was added to two human airway epithelial cell lines (16HBE and NCI-H292). Measured by real-time quantitative polymerase chain reaction (qPCR) and enzyme-linked immuno sorbent assay (ELISA) respectively, the intracellular mucin(MUC)5AC mRNA and MUC5AC protein of culture supernates exhibited a time- and dose-dependent increase after stimulation of SN. Based on the evidence of an increased phosphorylation of ERK1/2 induced by exogenous SN, we performed the radioactive binding assay. We failed to find direct binding of SN to either epidermal growth factor receptor (EGFR) or Neuropilin-1(NRP1), the co-receptor of EGFR. But we detected an enhanced binding of EGF to NRP1 in the two airway epithelial cell lines induced by exogenous SN. Either EGF neutralizing antibody or MEK specific inhibitor (PD-98059) could attenuate the over synthesis of MUC5AC induced by exogenous SN, indicating an endogenous EGF dependent mechanism in MUC5AC over synthesis induced by SN. Conclusions: We conclude that SN induces MUC5AC hypersecretion in a dose- and time-dependent manner; moreover, the MUC5AC over synthesis induced by SN is strongly associated with the enhanced binding of EGF to NRP1 and the activation of EGFR and ERK1/2 subsequently.

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Secretoneurin and chemoattractant receptor interactions

Cited by 41 publications

References 31 publications

Secretoneurin promotes pertussis toxin‐sensitive neurite outgrowth in cerebellar granule cells

Secretoneurin promotes pertussis toxin‐sensitive neurite outgrowth in cerebellar granule cells

Presence of chromogranin-derived antimicrobial peptides in plasma during coronary artery bypass surgery and evidence of an immune origin of these peptides

Secretoneurin Induces Airway Mucus Hypersecretion by Enhancing the Binding of EGF to NRP1

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