Tei Meina, Uchida Kazuyuki, Mutsuga Mayu, Chambers James K, Nakayama Hiroyuki
Department of Veterinary Pathology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.
J Vet Med Sci. 2012 Apr;74(4):481-3. doi: 10.1292/jvms.11-0420. Epub 2011 Nov 14.
Curcumin is a constituent phenol compound of turmeric, and has been used as a dietary spice and Indian medicine. Curcumin has been reported to inhibit the formation of amyloid β fibrils and aggregation. In this study, the binding activity of curcumin to various types of canine amyloid was examined. Tissue samples used were lesions of AA, AL, amyloid of canine amyloid-producing odontogenic tumor (Aapot), and senile cardiovascular amyloid (ScA). Curcumin stained all types of amyloid. The binding of curcumin to AA, ScA, and AL was lost by the KMnO(4) treatment, but Aapot maintained the binding. These findings indicate that curcumin binds several types of amyloid, while the binding sites of amyloid molecules might be different from that of Congo red.
姜黄素是姜黄中的一种酚类化合物，一直被用作膳食香料和印度药物。据报道，姜黄素可抑制β-淀粉样蛋白纤维的形成和聚集。在本研究中，检测了姜黄素与各种类型犬类淀粉样蛋白的结合活性。所用的组织样本为AA型、AL型、犬源性淀粉样瘤（Aapot）的淀粉样蛋白以及老年心血管淀粉样蛋白（ScA）的病变组织。姜黄素可对所有类型的淀粉样蛋白进行染色。用高锰酸钾处理后，姜黄素与AA型、ScA和AL型的结合消失，但Aapot仍保持结合。这些发现表明，姜黄素可与多种类型的淀粉样蛋白结合，而淀粉样蛋白分子的结合位点可能与刚果红不同。
