Westermark P, Shirahama T, Skinner M, Brun A, Cameron R, Cohen A S
Lab Invest. 1982 May;46(5):457-60.
Sections of brain tissue from patients with Alzheimer's disease with amyloid deposits in vessels, in plaques, and within nerve cells were studied by means of an immunoperoxidase method using a specific antiamyloid P component (AP) antiserum. Amyloid deposits in vessels were found to be strongly positive for protein AP, whereas the Alzheimer's plaques and the neurofibrillary tangles were negative or only weakly positive. The absence of protein AP in some intracerebral amyloid deposits might be due to an inability of the protein AP in some intracerebral amyloid deposits might be due to an inability of the protein to penetrate the blood-brain barrier. These findings support the theory that protein AP is absorbed to already formed amyloid fibrils, but the possibility that it may participate in the formation of vascular amyloid cannot be dismissed. The findings also indicate that protein AP is not necessary for the formation of amyloid fibrils at least in some forms of cerebral amyloidosis.
采用特异性抗淀粉样蛋白P成分(AP)抗血清的免疫过氧化物酶法,对患有阿尔茨海默病且血管、斑块及神经细胞内有淀粉样沉积物的患者脑组织切片进行了研究。结果发现,血管中的淀粉样沉积物对蛋白AP呈强阳性,而阿尔茨海默斑块和神经原纤维缠结呈阴性或仅弱阳性。一些脑内淀粉样沉积物中缺乏蛋白AP,可能是由于该蛋白无法穿透血脑屏障。这些发现支持了蛋白AP被已形成的淀粉样纤维吸附的理论,但它可能参与血管淀粉样蛋白形成的可能性也不能排除。这些发现还表明,至少在某些形式的脑淀粉样变性中,蛋白AP对于淀粉样纤维的形成并非必需。