Bernstein H G, Rinne R, Kirschke H, Järvinen M, Knöfel B, Rinne A
Institute for Neurobiology, Magdeburg, Germany.
Brain Res Bull. 1994;33(5):477-81. doi: 10.1016/0361-9230(94)90071-x.
The cellular localization of cystatin A, an endogenously occurring inhibitor of lysosomal thiol proteases (cathepsins B, H, L and S), was studied immunohistochemically in human postmortem brain using the peroxidase-antiperoxidase method. Both polyclonal and monoclonal antibodies to cystatin A were employed. Western blot analysis revealed one molecular form of the inhibitor in human brain extracts. Its molecular weight was about 13,000. Immunostaining appeared in a sizeable population of neurons and a few cells surrounding cerebral blood vessels (pericytes). In Alzheimer disease subjects cystatin A was found in many neuritic plaques. Possible functional consequences with regard to a role of cystatin A in the inhibition of the Alzheimer amyloid precursor protein (APP)-clipping enzyme, cathepsin B, are discussed.
采用过氧化物酶-抗过氧化物酶法，通过免疫组织化学方法研究了半胱氨酸蛋白酶抑制剂A（一种内源性溶酶体巯基蛋白酶（组织蛋白酶B、H、L和S）抑制剂）在人死后大脑中的细胞定位。使用了针对半胱氨酸蛋白酶抑制剂A的多克隆抗体和单克隆抗体。蛋白质免疫印迹分析显示人脑提取物中该抑制剂存在一种分子形式。其分子量约为13,000。免疫染色出现在相当数量的神经元以及一些围绕脑血管的细胞（周细胞）中。在阿尔茨海默病患者中，在许多神经炎性斑块中发现了半胱氨酸蛋白酶抑制剂A。讨论了半胱氨酸蛋白酶抑制剂A在抑制阿尔茨海默病淀粉样前体蛋白（APP）剪切酶组织蛋白酶B方面可能的功能后果。
