Search

The anti-allergic activity of Perilla glycopeptide (Pe-GP) isolated from dried Perilla frutescens BRH-TON leaves was investigated. Pe-GP was found to be effective in inhibiting histamine release from IgE-sensitized rat peritoneal mast cells induced by a specific antigen. The histamine release induced by several substances such as concanavalin A, compound 48/80, mastoparan, and ionophore A23187, was also found to be inhibited by Pe-OP. These results suggest that Pe-GP mainly interrupts a pathway of histamine release after calcium influx. Anti-allergic activity of Pe-GP was investigated by ear-swelling response in mice that had been passively sensitized with IgE via intravenous injection. Pe-GP, injected intraperitoneally before exposure to the antigen, was found to inhibit the allergic response in a dosedependent manner (5-100 mg/kg). Pe-GP shows promise as an anti-allergic substance for medical use as well as in health foods. シソ(Perilla frutescens B_)葉熱水抽出液から分離精製されたシソ糖ペプチド(Pe-GP,6kDa)の抗アレルギー活性を検討した。Pe-GPは,ラット腹腔内より単離してIgEで感作したマスト細胞において,特異抗原で刺激したときに誘発されるヒスタミン遊離反応を抑制した。同様にPe-GPはconcanavalin A,compound48/80,mastoparan,ionophore A23187などの誘発するヒスタミン遊離反応も抑制した。これらの結果からPe-GPはヒスタミン遊離機構のうちカルシウム動員以降の経路を主として抑えると考えられる。Pe-GPの生体内における抗アレルギー活性は,IgEを静注して受動感作したマウスの耳介浮腫反応により検討した。抗原塗布前にあらかじめ腹腔内に投与しておくと,Pe-GPは5-100mg/mlの範囲で濃度依存的に浮腫を抑制し抗アレルギー活性を示した。Pe-GPの抗アレルギー活性を有する医薬品としての開発が,健康食品と同様,期待される。

application/pdf, We have developed two novel 3-phenyl-3-trifluoromethyldiazirinyl bis-glucose derivatives to investigate the properties of the adipocyte glucose transporter GLUT4. These compounds were substituted by electron-with-drawing (iodo and nitro) groups on the aromatic ring of 3-phenyl-3-tritluoromethyldiazirine photophore and were found to be more photosensitive than compounds without such substituents. The compounds were used as inhibitors of insulin-stimulated glucose transport activity in order to assess half-maximal inhibition or relative affinity values for GLUT4. The affinities were found to be 60-130 times higher than the parent compound D-glu-cose. Because of the increased photo-reactivity and high affinity these compounds will be useful in studies directed at further elucidation of GLUT4 function., 日本薬学会Chemical & pharmaceutical bulletin 50(7) p.1004-1006より転載

Oligomerization, conformational changes, and the consequent neurodegeneration of Alzheimer's β-amyloid protein (AβP) play crucial roles in the pathogenesis of Alzheimer's disease (AD). Mounting evidence suggests that oligomeric AβPs cause the disruption of calcium homeostasis, eventually leading to neuronal death. We have demonstrated that oligomeric AβPs directly incorporate into neuronal membranes, form cation-sensitive ion channels (“amyloid channels”), and cause the disruption of calcium homeostasis via the amyloid channels. Other disease-related amyloidogenic proteins, such as prion protein in prion diseases or α-synuclein in dementia with Lewy bodies, exhibit similarities in the incorporation into membranes and the formation of calcium-permeable channels. Here, based on our experimental results and those of numerous other studies, we review the current understanding of the direct binding of AβP into membrane surfaces and the formation of calcium-permeable channels. The implication of composition of membrane lipids and the possible development of new drugs by influencing membrane properties and attenuating amyloid channels for the treatment and prevention of AD is also discussed.