S-（烯基）巯基半胱氨酸：化学合成、生物活性及与氧化还原相关的机制。

S-alk(en)ylmercaptocysteine: chemical synthesis, biological activities, and redox-related mechanism.

机构信息

Department of Food Science, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.

出版信息

J Agric Food Chem. 2013 Feb 27;61(8):1896-903. doi: 10.1021/jf305486q. Epub 2013 Feb 14.

Abstract

S-Alk(en)ylmercaptocysteine (CySSR, R = methyl, ethyl, propyl, 1-propenyl, and allyl), which are the putative metabolites of Allium thiosulfinates, were chemically synthesized. CySSR, but not the corresponding monosulfide species S-alk(en)yl cysteine (CySR), were able to induce quinone reductase (QR, a representative phase II enzyme) in Hepa 1c1c7 cells and inhibit nitric oxide (NO, an inflammatory biomarker) formation in lipopolysaccharide (LPS)-activated RAW 264.7 cells. These results indicate the importance of the disulfide bond for the biological activities of CySSR. Glutathione (GSH) and N-acetylcysteine (NAC), but not other types of cellular antioxidants, suppressed multiple biological activities of CySSR in vitro. The inhibitory effects of GSH and NAC on the biological activities of CySSR were correlated with a glutaredoxin (Grx)-dependent intracellular reduction of CySSR to generate cysteine and RSH, which were secreted into the extracellular medium.

摘要

S-（烯基）巯基半胱氨酸（CySSR，R=甲基、乙基、丙基、1-丙烯基和烯丙基），是大蒜硫代亚磺酸酯的可能代谢物，被化学合成。CySSR，但不是相应的单硫化物 S-（烯基）半胱氨酸（CySR），能够诱导 Hepa 1c1c7 细胞中的醌还原酶（QR，一种代表性的 II 相酶），并抑制脂多糖（LPS）激活的 RAW 264.7 细胞中的一氧化氮（NO，一种炎症生物标志物）的形成。这些结果表明二硫键对于 CySSR 的生物学活性很重要。谷胱甘肽（GSH）和 N-乙酰半胱氨酸（NAC），而不是其他类型的细胞抗氧化剂，在体外抑制了 CySSR 的多种生物学活性。GSH 和 NAC 对 CySSR 生物学活性的抑制作用与依赖于谷氧还蛋白（Grx）的细胞内还原 CySSR 生成半胱氨酸和 RSH 有关，这些物质被分泌到细胞外培养基中。