Novel opioid peptides derived from mitochondrial cytochrome b: Cytochrophins

Brantl, Victor; Gramsch, Christian; Lottspeich, Friedrich; Henschen, Agnes; Jaeger, Karl-Heinz; Herz, A.

doi:10.1016/0014-2999(85)90773-3

Cited by 61 publications

(17 citation statements)

References 3 publications

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“…This is consistent with the fact that soymorphins containing the YPF sequence are -selective. Casomorphins (e.g., human -casomorphin-7, YPFVEPI), 2) hemorphin (YPWT) derived from hemoglobin, 7) and endomorphin-1 and 2 (YPWF-NH 2 and YPFF-NH 2 respectively) 5) containing the Tyr-Pro-aromatic amino acid sequence in these molecules, are also -selective opioid peptides, of animal origin. In contrast, opioid peptides of plant origin, such as gluten exorphin 4,8) and rubiscolin, 9,10) with the Tyr-Pro-non-aromatic amino acid sequence, are selective for the receptor.…”

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confidence: 99%

Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Ohinata

Agui

Yoshikawa

2007

Bioscience, Biotechnology, and Biochemistry

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Based on the amino acid sequence YPFV found in the soy -conglycinin -subunit, which is common to an opioid peptide human -casomorphin-4, peptides YPF-VV, YPFVVN, and YPFVVNA were synthesized according to their primary structure. On guinea pig ileum (GPI) assay, they showed opioid activity (IC 50 = 6.0, 9.2 and 13 M respectively) more potent than humancasomorphins, and were named soymorphins-5, -6, and -7, respectively. Their opioid activities on mouse vas deferens (MVD) assay were less potent than on GPI assay, suggesting that they are selective for the opioid receptor. Human -casomorphin-4 and soymorphin-5 were released from the soy 7S fraction (-conglycinin) by the action of gastrointestinal proteases. Soymorphins-5, -6, and -7 had anxiolytic activities after oral administration at doses of 10-30 mg/kg in the elevated plus-maze test in mice.Key words: opioid peptide; opioid receptor; anxiolytic effect; soy protein; -conglycinin -subunitOpioid is a chemical substance that has morphine-like action. An opioid peptide, bovine -casomorphin-7 (YPFPGPI), isolated from casein peptone, was the first example of bioactive peptides released from food proteins.1) We have reported that human -casomorphin-4 (YPFV) and related peptides derived from human -casein also have opioid activities, though they are less potent than their bovine counterparts.2) Of three soyconglycinin subunits (, 0 , and ), 3) the -subunit has the human -casomorphin-4 sequence (YPFV). Longer peptides, YPFVV, YPFVVN, and YPFVVNA, were synthesized according to the primary structure of theconglycinin -subunit by the Fmoc strategy, and their opioid activities were tested by guinea pig ileum (GPI) and mouse vas deferens (MVD) assay, as previously described.4) All experiments were approved by the Kyoto University Ethics Committee for Animal Research Use.The peptides were found to have opioid activities on GPI assay. Figure 1 indicates the typical suppressive effect of YPFVV on electrically stimulated contractions on GPI assay. YPFVVN and YPFVVNA also dosedependently inhibited ileum contractions (data not shown). These results suggest that YPFVV, YPFVVN, and YPFVVNA have opioid activities; they were named soymorphins-5, -6, and -7 respectively. The opioid activities of synthetic peptides derived from the soyconglycinin -subunit are summarized in Table 1. The IC 50 values of soymorphins-5, -6, and -7 on GPI assay were 6.0, 9.2, and 13 mM respectively, and their opioid activities were more potent than those of humancasomorphin-4, -5, and -6 (IC 50 = 20, 14, and 25 mM, respectively). There are three types of opioid receptors: , , and . 5,6) The opioid activities of soymorphins were larger on GPI assay than those on MVD assay, suggesting that these peptides are selective for theopioid receptor. The affinities for the -opioid receptor were 17, 39, and 47 mM respectively, and the rank order of their affinities for the receptor was consistent with that of the opioid activities on GPI assay. Taking all this 1 µM 3 µM 10 µM 1 min Guinea Pig Ileum (GPI) Assay. Ileum-...

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confidence: 99%

Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Ohinata

Agui

Yoshikawa

2007

Bioscience, Biotechnology, and Biochemistry

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“…This analysis yielded almost exclusively neuropeptides. Although a number of degradation products from proteins such as hemoglobin and cytochrome c are bioactive molecules [80,81], it is unlikely that all the identified protein fragments act as signaling molecules. Instead, as the author suggested, these might originate from post-mortem protease activity.…”

Section: Peptidomics In the Post-genome Eramentioning

confidence: 99%

Peptidomics

Baggerman

Verleyen

Clynen

et al. 2004

Journal of Chromatography B

131

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Peptides occur in the whole animal kingdom, from the least evolved phyla with a very simple nervous system (coelenterates) to the highest vertebrates and are involved in most, if not all, physiological processes in animals. Knowing the amino acid sequence of peptide hormones or neurotransmitters is important since this allows for synthesis of large quantities of peptides to perform further functional analysis. Immunocytochemistry, radioimmunoassays (RIA), enzyme-linked immunosorbant assays (ELISA) and mass spectrometry can then provide information on the temporal and spatial distribution and quantification of the (neuro)peptide. Ever since the 1970s, a wealth of peptides has been discovered and investigated and this flow seems to be far from over. This is partially due to the use of new approaches mainly based on chromatographical purifications as well as molecular biological techniques. Surprisingly, peptides have so far been neglected in most proteomic studies. The finalization of the genome projects has opened new opportunities for rapid identification and functional analysis of (neuro)peptides as well. In analogy with the proteomics technology, where all proteins expressed in a cell or tissue are analyzed, the peptidomic approach aims at the simultaneous visualization and identification of the whole peptidome of a cell or tissue, i.e. all expressed peptides with their post-translational modifications (PTMs). This technology provides us with a fast and efficient tool to analyze the peptides from any tissue. This paper reviews the approaches that have been used so far to achieve this.

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“…Studying functions of some of such fragments and of those obtained by experimental proteolysis has shown that they can serve as oligopeptide regulators. Thus, a number of fragments of milk proteins (casein [17][18][19][20][21], α-lactalbumin, β-lactoglobulin, and lactoferrin [22,23]) as well of cytochrome c [24,25] and hemoglobin [26][27][28][29] are able to exhibit opioid activity, i.e. they are neuropeptides.…”

Section: Structurementioning

confidence: 99%

Structural and functional diversity of natural antimicrobial oligopeptides

Zamyatnin

2011

Science and Technology Against Microbial Pathogens

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Antimicrobial peptides have been isolated and characterized from tissues and organisms representing virtually every kingdom and phylum, ranging from prokaryotes to humans. These molecules are small, relatively compact compounds, which are structurally and functionally rather diverse. This consideration is focussed on the structural and functional properties of the natural antimicrobial oligopeptides that are ribisomally synthesised without extensive posttranslational modifications. They are cationic molecules as the molecules are usually rich in lysine, and arginine. They are also amphipathic, containing hydrophobic and hydrophilic region. Natural antimicrobial oligopeptides have a broad spectrum of antimicrobial activity. They serve as an ancient defence mechanism against pathogenic microorganisms that easily come into contact with the host through the environment. These molecules are considered as part of the innate immune system of all species. Lastly, the review discusses the potential applications in health care products.

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Novel opioid peptides derived from mitochondrial cytochrome b: Cytochrophins

Cited by 61 publications

References 3 publications

Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Soymorphins, Novel μ Opioid Peptides Derived from Soy β-Conglycinin β-Subunit, Have Anxiolytic Activities

Peptidomics

Structural and functional diversity of natural antimicrobial oligopeptides

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