Abstract
Using alginic acid to adsorb polypeptides at pH 2.7, we isolated a peptide pea albumin 1b (PA1b) from pea seeds. The PA1b is a single chain peptide consisting of 37 amino acid residues with 6 cysteines which constitutes the cystine-knot structure. Using microfluorometry and patch clamp techniques, we found that PA1b significantly elevated the intracellular calcium level ([Ca2+]i) and elicited membrane capacitance increase in the primary rat pancreatic β cells. The PA1b effect on [Ca2+]i elevation was abolished in the absence of extracellular Ca2+ or in the presence of L-type Ca2+ channel blocker, nimodipine. Interestingly, we found that PA1b significantly depolarized membrane potential, which could lead to the opening of voltage-dependent L-type Ca2+ channels and influx of extracellular Ca2+, and then evoke robust secretion. In this study we identified the plant peptide PA1b which is capable of affecting the excitability and function of mammalian pancreatic β cell.
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Supported by the National Natural Science Foundation of China (Grant Nos. 30370674, 30470448, and 30470646), the CAS Project (Grant No. KSCX2-SW-224), and the China “863” Program (Grant No. 2012AA214066). The laboratory of Tao Xu is also supported by the Partner Group Scheme of the Max Planck Institute for Biophysical Chemistry, Göttingen
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Hu, Z., Dun, X., Zhang, M. et al. PA1b, a plant peptide, induces intracellular [Ca2+] increase via Ca2+ influx through the L-type Ca2+ channel and triggers secretion in pancreatic β cells. SCI CHINA SER C 50, 285–291 (2007). https://doi.org/10.1007/s11427-007-0052-y
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DOI: https://doi.org/10.1007/s11427-007-0052-y