TAILIEUCHUNG - Báo cáo khoa học: Activity of the plant peptide aglycin in mammalian systems

A 37 residue peptide, aglycin, has been purified from porcine intestine. The sequence is identical to that of residues 27–63 of plant albumin 1 B precur-sor (PA1B, chain b) from pea seeds. Aglycin resists in vitro proteolysis by pepsin, trypsin and Glu-C protease, compatible with its intestinal occur-rence and an exogenous origin from plant food. | ỊFEBS Journal Activity of the plant peptide aglycin in mammalian systems Xin-Peng Dun1 Jian-He Wang1 Lei Chen1 Jie Lu1 Fa-Fang Li1 Yan-Ying Zhao1 Ella Cederlund2 Galina Bryzgalova3 Suad Efendic3 Hans Jornvall2 Zheng-Wang Chen1 2 and Tomas Bergman2 1 Schoolof Life Science and Technology Huazhong University of Science and Technology Wuhan China 2 Department of MedicalBiochemistry and Biophysics Karolinska Institutet Stockholm Sweden 3 Department of Molecular Medicine and Surgery Karolinska University Hospital Stockholm Sweden Keywords aglycin albumin 1 B precursor blood glucose mice voltage-dependent anionselective channelprotein 1 Correspondence T. Bergman MedicalBiochemistry and Biophysics Karolinska Institutet SE-171 77 Stockholm Sweden Fax 46 8 337 462 Tel 46 8 524 87780 E-mail . Chen Schoolof Life Science and Technology Huazhong University of Science and Technology Wuhan 430074 China Fax Tel 86 27 8779 2027 E-mail zwchen21@ A 37 residue peptide aglycin has been purified from porcine intestine. The sequence is identical to that of residues 27-63 of plant albumin 1 B precursor PA1B chain b from pea seeds. Aglycin resists in vitro proteolysis by pepsin trypsin and Glu-C protease compatible with its intestinal occurrence and an exogenous origin from plant food. When subcutaneously injected into mice at 10 Ig-g 1 body weight aglycin has a hyperglycemic effect resulting in a doubling of the blood glucose level within 60 min. Using surface plasmon resonance biosensor technology an aglycin binding protein with an apparent molecular mass of 34 kDa was detected in membrane protein extracts from porcine and mice pancreas. The polypeptide was purified by affinity chromatography and identified through peptide mass fingerprinting as the voltage-dependent anion-selective channel protein 1. The results indicate that aglycin has the potential to interfere with mammalian physiology. Received 3 October 2006 revised 23 November 2006 accepted 29 .

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