Zhang W, Johnson B R, Suri D E, Martinez J, Bjornsson T D
Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA 19107-5563, USA.
Acta Neuropathol. 1998 Oct;96(4):395-400. doi: 10.1007/s004010050910.
The brain of Alzheimer's disease patients contains deposits of the 39-42-amino acid (approximately 4 kDa) amyloid beta-peptide, which is derived from the beta-amyloid precursor protein. These pathological deposits have been shown to consist in part of insoluble 8- and 16-kDa aggregates of the amyloid beta-peptide. This report confirms that the amyloid beta-peptide is a substrate for tissue transglutaminase (TGase) and demonstrates that human brain preparations from Alzheimer's disease patients and control patients form cross-linked dimers from added iodinated amyloid beta-peptide. Immunohistochemical staining for TGase revealed its presence in tissue sections and isolated amyloid plaque cores obtained from brains of patients diagnosed as having Alzheimer's disease. These results provide evidence that the previously described insoluble amyloid deposits in Alzheimer's disease may involve TGase-mediated cross-linked amyloid beta-peptide polymers, and suggest a potential role for TGase in the pathogenesis of this disease.
阿尔茨海默病患者的大脑中含有由β-淀粉样前体蛋白衍生而来的39 - 42个氨基酸（约4 kDa）的淀粉样β肽沉积物。这些病理性沉积物已被证明部分由淀粉样β肽的不溶性8 kDa和16 kDa聚集体组成。本报告证实淀粉样β肽是组织转谷氨酰胺酶（TGase）的底物，并表明来自阿尔茨海默病患者和对照患者的人脑制剂能使添加的碘化淀粉样β肽形成交联二聚体。对TGase的免疫组织化学染色显示其存在于从被诊断患有阿尔茨海默病患者的大脑获得的组织切片和分离的淀粉样斑块核心中。这些结果提供了证据，表明先前描述的阿尔茨海默病中不溶性淀粉样沉积物可能涉及TGase介导的交联淀粉样β肽聚合物，并提示TGase在该疾病的发病机制中可能发挥作用。
