4.6 Article

Heat Resistant Characteristics of Major Royal Jelly Protein 1 (MRJP1) Oligomer

Journal

PLOS ONE
Volume 10, Issue 5, Pages -

Publisher

PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0119169

Keywords

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Funding

  1. Sapporo Regional Innovation Strategy Promotion Program Grant from the Knowledge Cluster Initiative of the Ministry of Education, Sports, Science and Technology (MEXT)
  2. Japan Royal Jelly Co., Ltd.
  3. Hokkaido University, Sapporo, Japan

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Soluble royal jelly protein is a candidate factor responsible for mammiferous cell proliferation. Major royal jelly protein 1 (MRJP1), which consists of oligomeric and monomeric forms, is an abundant proliferative protein in royal jelly. We previously reported that MRJP1 oligomer has biochemical heat resistance. Therefore, in the present study, we investigated the effects of several heat treatments (56, 65 and 96 degrees C) on the proliferative activity of MRJP1 oligomer. Heat resistance studies showed that the oligomer molecular forms were slightly maintained until 56 degrees C, but the molecular forms were converted to macromolecular heat-aggregated MRJP1 oligomer at 65 degrees C and 96 degrees C. But, the growth activity of MRJP1 oligomer treated with 96 degrees C was slightly attenuated when compared to unheated MRJP1 oligomer. On the other hand, the cell proliferation activity was preserved until 96 degrees C by the cell culture analysis of Jurkat cells. In contrast, those of IEC-6 cells were not preserved even at 56 degrees C. The present observations suggest that the bioactive heat-resistance properties were different by the origin of the cells. The cell proliferation analysis showed that MRJP1 oligomer, but not MRJP2 and MRJP3, significantly increased cell numbers, suggesting that MRJP1 oligomer is the predominant proliferation factor for mammiferous cells.

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