Gastrointestinal enzyme production of bioactive peptides from royal jelly protein and their antihypertensive ability in SHR

Matsui, Toshiro; Yukiyoshi, Akiko; S, Doi; Sugimoto, Hiroyuki; Yamada, Hideo; Matsumoto, Kiyoshi

doi:10.1016/s0955-2863(01)00198-x

Cited by 162 publications

(118 citation statements)

References 23 publications

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“…MRJP1 stimulates rat hepatocyte DNA synthesis, prolongs the proliferation of hepatocytes, increases albumin production (Kamakura et al, 2001b), and regulates mouse macrophages to release tumor necrosis factor α (TNF-α) (Majtan et al, 2006). Peptides derived from MRJP1 by enzymatic hydrolysis in the gastrointestinal tract possess potent antihypertensive activity in rats (Matsui et al, 2002). Furthermore, the C-terminal of MRJP1 may be a precursor of the antimicrobial peptides known as Jelleines (Fontana et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody

Shen

Wang

Zhai

et al. 2015

J. Zhejiang Univ. Sci. B

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Major royal jelly protein 1 (MRJP1), designated apalbumin 1, has been regarded as a freshness marker of royal jelly (RJ). A MRJP1-specific peptide (IKEALPHVPIFD) identified by bioinformatics analysis of homologous members of the major royal protein family was synthesized and used to raise polyclonal anti-MRJP1 antibody (anti-SP-MRJP1 antibody). Western blot analysis showed that anti-SP-MRJP1 antibody only reacted with MRJP1 in RJ. In contrast, the previously reported antibody against recombinant MRJP1 (anti-R-MRJP1 antibody) reacted with other members of MRJP family in RJ. Enzyme-linked immunosorbent assay (ELISA) using anti-SP-MRJP1 antibody demonstrated that MRJP1 content in RJ stored at 40 °C significantly degraded by 37.3%, 55.9%, 58.0%, 60.6%, 65.7%, 72.7%, and 73.1% at 7, 14, 21, 28, 35, 42, and 49 d, respectively, when compared with MRJP1 content in fresh RJ (0 d). Optical density analysis of MRJP bands from sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profiles demonstrated that the degradation of MRJP1, MRJP2, MRJP3, and MRJP5 in RJ was strongly and positively correlated with the period of storage (P<0.0001). Our results indicated anti-SP-MRJP1 antibody was highly specific for MRJP1, and ELISA using the antibody is a sensitive and easy-to-use method to determine the freshness and authenticity of RJ.

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Section: Introductionmentioning

confidence: 99%

Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody

Shen

Wang

Zhai

et al. 2015

J. Zhejiang Univ. Sci. B

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“…The phenomenon associated with the blood pressure lowering effect must be the dual inhibitory function of the dipeptide YY against renin and ACE. As the peptide was prepared from the protein fraction by protease, the peptide could be generated in the gastrointestine after an oral dose of the RJ, possibly as described by Matsui et al (31).…”

Section: Discussionmentioning

confidence: 99%

A dipeptide YY derived from royal jelly proteins inhibits renin activity

Sultana

Nabi²,

Nasir³

et al. 2008

Int J Mol Med

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Abstract. Renin is the rate limiting enzyme in the reninangiotensin (RA) system that regulates blood pressure and electrolyte balance. In this study, we investigated the renin inhibitory effect of a royal jelly (RJ)-derived peptide. A dipeptide YY was isolated from the digested fraction of RJ proteins by proteases and was found to inhibit human renin activity. The inhibition constant (K i ) of YY was estimated to be 10 μM when the K m was 0.16 μM using sheep angiotensinogen as the substrate. The peptide was observed to lower blood pressure in spontaneously hypertensive rats.

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“…The structure and bioactivity of short-chain peptides are more easily preserved through gastrointestinal passage than those of their long-chain counterparts [272] -whereas sequences containing Pro residue(s) are generally more resistant to degradation by digestive enzymes [273]. Furthermore, peptides absorbed following digestion may accumulate in specific organs, and then exert their action in a systematic and gradual manner [274,275]. However, antihypertensive peptides that cannot be absorbed from the digestive tract may still exert their function directly in the intestinal lumen -e.g.…”

Section: Bioavailabilitymentioning

confidence: 99%