Wien Tale N, Sørby Randi, Espenes Arild, Gunnes Gjermund, Nordstoga Knut, Landsverk Thor, Husby Gunnar
Department of Rheumatology/Institute of Immunology, Rikshospitalet, University of Oslo, 0027 Oslo, Norway.
Amyloid. 2003 Dec;10(4):240-9. doi: 10.3109/13506120309041741.
The spleen is the primary target for spontaneous as well as experimental AA amyloidosis in animals such as mice and mink, and is therefore a valuable organ for study of the initial phases of amyloid fibrillogenesis and deposition. We have investigated splenic amyloid AA deposits induced in the mink, and we demonstrate a novel target for AA, namely the splenic ellipsoids. We show presence of amyloid P component (AP), glycosaminoglycans (GAGs) and apolipoprotein E (apoE), all well-known common elements of amyloid, co-localizing with AA. In addition, apolipoprotein AI (apoAI) was seen co-localized to the AA deposits in the ellipsoids. We hypothesize that the ellipsoids may be important splenic structures for initial AA formation. The apoAI in the ellipsoids could displace SAA from acute phase HDL at this site, thereby making SAA available for amyloid formation and deposition.
在小鼠和水貂等动物中,脾脏是自发性以及实验性AA淀粉样变性的主要靶器官,因此是研究淀粉样纤维形成和沉积初始阶段的重要器官。我们研究了水貂脾脏中诱导产生的AA淀粉样沉积物,并证明了AA的一个新靶点,即脾椭球。我们发现淀粉样P成分(AP)、糖胺聚糖(GAGs)和载脂蛋白E(apoE)这些淀粉样物质的所有常见成分都与AA共定位。此外,还观察到载脂蛋白AI(apoAI)与椭球中的AA沉积物共定位。我们推测椭球可能是AA初始形成的重要脾脏结构。椭球中的apoAI可在该部位将急性期高密度脂蛋白(HDL)中的血清淀粉样蛋白A(SAA)置换出来,从而使SAA可用于淀粉样蛋白的形成和沉积。