Aqueous extracts of Anemarrhena asphodeloides stimulate glucagon-like pepetide-1 secretion in enteroendocrine NCI-H716 cells
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Abstract
Anemarrhena asphodeloides (AA), a bitter taste herbal medicine, has been prescribed in traditional oriental medicine to treat diabetes mellitus. Here, AA was extracted and fractionated to investigate its effects on the stimulation of glucagon-like peptide-1 (GLP-1) secretion in enteroendocrine cells. GLP-1 is secreted from the human enteroendocrine L cells to the blood in response to ingested nutrients. Because GLP-1 increases glucose dependent insulin release, it is known as a therapeutic method for the treatment of type II diabetes mellitus. The human enteroendocrine L cell line NCI-H716 expresses various chemoreceptors including the G protein coupled receptor (GPCR). Previous studies suggested that, through the GPCR signaling pathway, the secretion of GLP-1 can be induced in NCI-H716. Accordingly, we studied the GLP-1 stimulation effect of the AA extract and its mode-of-action using the GLP-1 ELISA and microarray. Functional categorization of the microarray data confirmed up or down-regulated gene expressions associated with the GPCR signaling pathway. This study demonstrates that AA extracts have a scientific possibility as a GLP-1 stimulant and thus may have the potential to be a therapeutic herbal medicine for type II diabetes mellitus.
Keywords
Anemarrhena asphodeloides (AA) Glucagonlike peptide-1 (GLP-1) Enteroendocrine cell NCI-H716 Type II diabetes mellitus Herbal medicinePreview
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References
- 1.Hui, H., Tang, G. & Go, V.L. Hypoglycemic herbs and their action mechanisms. Chin. Med. 4, 11 (2009).CrossRefGoogle Scholar
- 2.Bolen, S. et al. Systematic review: comparative effectiveness and safety of oral medications for type 2 diabetes mellitus. Ann. Intern. Med. 147, 386–399 (2007).CrossRefGoogle Scholar
- 3.Jang, H.J. et al. Gut-expressed gustducin and taste receptors regulate secretion of glucagon-like peptide-1. Proc. Natl. Acad. Sci. USA 104, 15069–15074 (2007).CrossRefGoogle Scholar
- 4.Le Neve, B. & Daniel, H. Selected tetrapeptides lead to a GLP-1 release from the human enteroendocrine cell line NCI-H716. Regul. Pept. 167, 14–20 (2011).CrossRefGoogle Scholar
- 5.Kreymann, B., Williams, G., Ghatei, M.A. & Bloom, S.R. Glucagon-like peptide-1 7–36: a physiological incretin in man. Lancet 2, 1300–1304 (1987).CrossRefGoogle Scholar
- 6.Wettergren, A. et al. Truncated GLP-1 (proglucagon 78–107-amide) inhibits gastric and pancreatic functions in man. Dig. Dis. Sci. 38, 665–673 (1993).CrossRefGoogle Scholar
- 7.D’Alessio, D.A., Kahn, S.E., Leusner, C.R. & Ensinck, J.W. Glucagon-like peptide 1 enhances glucose tolerance both by stimulation of insulin release and by increasing insulin-independent glucose disposal. J. Clin. Invest. 93, 2263–2266 (1994).CrossRefGoogle Scholar
- 8.Todd, J.F. et al. Glucagon-like peptide-1 (GLP-1): a trial of treatment in non-insulin-dependent diabetes mellitus. Eur. J. Clin. Invest. 27, 533–536 (1997).CrossRefGoogle Scholar
- 9.Venkatakrishnan, A.J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185–194 (2013).CrossRefGoogle Scholar
- 10.Kinnamon, S.C. Taste receptor signalling-from tongues to lungs. Acta Physiol. (Oxf ) 204, 158–168 (2012).CrossRefGoogle Scholar
- 11.Kim, S.J. et al. Pancreatic beta-cell prosurvival effects of the incretin hormones involve post-translational modification of Kv2.1 delayed rectifier channels. Cell Death Differ. 19, 333–344 (2012).CrossRefGoogle Scholar
- 12.Hoa, N.K., Phan, D.V., Thuan, N.D. & Ostenson, C.G. Insulin secretion is stimulated by ethanol extract of Anemarrhena asphodeloides in isolated islet of healthy Wistar and diabetic Goto-Kakizaki Rats. Exp. Clin. Endocrinol. Diabetes. 112, 520–525 (2004).CrossRefGoogle Scholar
- 13.Choi, E.K. et al. Hexane fraction of Citrus aurantium L. stimulates glucagon-like peptide-1 (GLP-1) secretion via membrane depolarization in NCI-H716 cells. BioChip J. 6, 41–47 (2012).CrossRefGoogle Scholar
- 14.Shin, M.H. et al. Gentiana scabra extracts stimulate glucagon-like peptide-1 secretion via G protein-coupled receptor pathway. BioChip J. 6, 114–119 (2012).CrossRefGoogle Scholar
- 15.Shi, C.S. et al. Regulator of G-protein signaling 3 (RGS3) inhibits Gbeta1gamma 2-induced inositol phosphate production, mitogen-activated protein kinase activation, and Akt activation. J. Biol. Chem. 276, 24293–24300 (2001).CrossRefGoogle Scholar
- 16.von Buchholtz, L. et al. RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells. Eur. J. Neurosci. 19, 1535–1544 (2004).CrossRefGoogle Scholar
- 17.Bennett, V. & Baines, A.J. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 81, 1353–1392 (2001).Google Scholar
- 18.Stabach, P.R., Devarajan, P., Stankewich, M.C., Bannykh, S. & Morrow, J.S. Ankyrin facilitates intracellular trafficking of alpha1-Na+-K+-ATPase in polarized cells. Am. J. Physiol. Cell. Physiol. 295, C1202–1214 (2008).CrossRefGoogle Scholar
- 19.Singleton, P.A. & Bourguignon, L.Y. CD44 interaction with ankyrin and IP3 receptor in lipid rafts promotes hyaluronan-mediated Ca2+ signaling leading to nitric oxide production and endothelial cell adhesion and proliferation. Exp. Cell Res. 295, 102–118 (2004).CrossRefGoogle Scholar
- 20.Tolhurst, G. et al. Glutamine triggers and potentiates glucagon-like peptide-1 secretion by raising cytosolic Ca2+ and cAMP. Endocrinology 152, 405–413 (2011).CrossRefGoogle Scholar
- 21.Chung, H.J., Jan, Y.N. & Jan, L.Y. Polarized axonal surface expression of neuronal KCNQ channels is mediated by multiple signals in the KCNQ2 and KCNQ3 C-terminal domains. Proc. Natl. Acad. Sci. USA 103, 8870–8875 (2006).CrossRefGoogle Scholar
- 22.Choi, E.-K. et al. Genome-wide gene expression analysis of Patrinia scabiosaefolia reveals an antibiotic effect. BioChip J. 5, 246–254 (2011).CrossRefGoogle Scholar
- 23.Kim, K.-S. et al. Global transcriptome analysis of the Escherichia coli O157 response to Houttuynia Cordata Thunb. BioChip J. 4, 237–246 (2010).CrossRefGoogle Scholar
- 24.Kim, K.-S. et al. The multi-target antibiotic efficacy of Angelica dahurica Bentham et Hooker extract exposed to the Escherichia coli O157:H7. BioChip J. 5, 333–342 (2011).CrossRefGoogle Scholar
- 25.Yang, H.J. et al. Global transcriptome analysis of the E. coli O157 response to Agrimonia pilosa extract. Mol. Cell. Toxicol. 7, 299–310 (2011).CrossRefGoogle Scholar