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Characterization and immunomodulatory function comparison of various bursal-derived peptides isolated from the humoral central immune organ

Authors :
Feng, Xiu-Li
Liu, Qing-Tao
Cao, Rui-Bing
Zhou, Bin
Zhang, Yuan-Peng
Liu, Ke
Liu, Xiao-Dong
Wei, Jian-Chao
Li, Xin-Feng
Chen, Pu-Yan
Source :
Peptides. Feb2012, Vol. 33 Issue 2, p258-264. 7p.
Publication Year :
2012

Abstract

Abstract: The bursa of Fabricius (BF) is the acknowledged central immune organ, which is important to the B cell differentiation and antibody production. However, due to difficult purification, the immunomodulatory peptides from BF were little reported. In this study, the extract samples of BF were taken to a chromatographic analysis by RP-HPLC. Five novel low molecular weight peptides were isolated from BF, with amino acid sequences of YEYAY, RMYEE, GPPAT, AGCCNG, and RRL, and named as Bursal pentapeptide (BPP)-III, -IV, -V, and Bursal hexapeptide (BHP), and Bursal tripeptide (BTP), respectively. BSP-I, BSP-II, BPP-I and BPP-II are recently reported to be the bursal-derived bioactive peptides. In this paper, we analyzed the chemical formula and characteristics of these nine bursal-derived peptides. The immunization comparative experiment verified the different immunomodulatory activity of these nine bursal peptides on antibody and cytokine productions. Furthermore, the results showed that at reachable concentrations, BPP-II and BPP-I induced antibody productions, lymphocyte viabilities and cytokine responses in different dose-dependent manner in the immunized mice model, respectively. These results provided important orientations for the comprehensively understanding and study of the humoral central immune system of human, and provided a novel insight on the treatment of serious disease and immune improvement of human. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
01969781
Volume :
33
Issue :
2
Database :
Academic Search Index
Journal :
Peptides
Publication Type :
Academic Journal
Accession number :
72337217
Full Text :
https://doi.org/10.1016/j.peptides.2012.01.012