Molecular characteristics and physiological functions of major royal jelly protein 1 oligomer

Autor: Takanori Moriyama, Yoshihisa Yamaguchi, Masatomo Omi, Reo Nozaki, Seiichi Kobayashi, Shogo Tamura, Kikuji Yamaguchi, Toru Kono
Rok vydání: 2009
Předmět:
Zdroj: PROTEOMICS. 9:5534-5543
ISSN: 1615-9861
1615-9853
Popis: Royal jelly contains numerous components, including proteins. Major royal jelly protein (MRJP) 1 is the most abundant protein among the soluble royal jelly proteins. In its physiological state, MRJP 1 exists as a monomer and/or oligomer. This study focuses the molecular characteristics and functions of MRJP 1 oligomer. MRJP 1 oligomer purified using HPLC techniques was subjected to the following analyses. The molecular weight of MRJP 1 oligomer was found to be 290 kDa using blue native-PAGE. MRJP 1 oligomer was separated into 55 and 5 kDa spots on 2-D blue native/SDS-PAGE. The 55 kDa protein was identified as MRJP 1 monomer by proteome analysis, whereas the 5 kDa protein was identified as Apisimin by N-terminal amino acid sequencing, and this protein may function as a subunit-joining protein within MRJP 1 oligomer. We also found that the oligomeric form included noncovalent bonds and was stable under heat treatment at 56 degrees C. Furthermore, MRJP 1 oligomer dose dependently enhanced and sustained cell proliferation in the human lymphoid cell line Jurkat. In conclusion, MRJP 1 oligomer is a heat-resistant protein comprising MRJP 1 monomer and Apisimin, and has cell proliferation activity. These findings will contribute to further studies analyzing the effects of MRJP 1 in humans.
Databáze: OpenAIRE
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