ArticlePloS one2015
Heat Resistant Characteristics of Major Royal Jelly Protein 1 (MRJP1) Oligomer.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- Ectopic expression of structurally similar major royal jelly proteins reveals their distinct functions inJournal of Zhejiang University. Science. B · 2026Article
- Monitoring and Maintaining the Freshness of Royal Jelly: A Review of Analytical Approaches and Preservation Technologies.Foods (Basel, Switzerland) · 2025Review
- Royal jelly a promising therapeutic intervention and functional food supplement: A systematic review.Heliyon · 2024Review
- Current Status of the Bioactive Properties of Royal Jelly: A Comprehensive Review with a Focus on Its Anticancer, Anti-Inflammatory, and Antioxidant Effects.Molecules (Basel, Switzerland) · 2023Review
- Ethanol-soluble proteins from the royal jelly of Xinjiang black bees.Protein science : a publication of the Protein Society · 2021Article
- Royal jelly attenuates metabolic defects in aBiology open · 2020Article
- Royal Jelly and Its Components Promote Healthy Aging and Longevity: From Animal Models to Humans.International journal of molecular sciences · 2019Review
- pH-dependent stability of honey bee (Apis mellifera) major royal jelly proteins.Scientific reports · 2019Article
- Architecture of the native major royal jelly protein 1 oligomer.Nature communications · 2018Article
- Characterizing the Structure and Oligomerization of Major Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and Complementary Biophysical Tools.Biochemistry · 2017Article
- Therapeutic Properties of Bioactive Compounds from Different Honeybee Products.Frontiers in pharmacology · 2017Review
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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°C) on the proliferative activity of MRJP1 oligomer. Heat resistance studies showed that the oligomer molecular forms were slightly maintained until 56℃, but the molecular forms were converted to macromolecular heat-aggregated MRJP1 oligomer at 65℃ and 96℃. But, the growth activity of MRJP1 oligomer treated with 96°C was slightly attenuated when compared to unheated MRJP1 oligomer. On the other hand, the cell proliferation activity was preserved until 96℃ by the cell culture analysis of Jurkat cells. In contrast, those of IEC-6 cells were not preserved even at 56°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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