Athanasou N A, Kokubun S, West L, Sallie B, Puddle B
Nuffield Department of Pathology and Bacteriology, John Radcliffe Hospital, Oxford, UK.
Eur Spine J. 1995;4(5):308-12. doi: 10.1007/BF00301041.
Intervertebral discs are a common site of localized articular and some forms of systemic articular amyloid deposition. Whether there is an intrinsic matrix factor that favours amyloid deposition in intervertebral disc connective tissues is uncertain, but it is known that small localized deposits of amyloid in intervertebral discs are largely age related. As the glycosaminoglycans (GAGs) composition of the intervertebral disc is known to change with age, and as some forms of systemic amyloid deposition have been shown to be associated with particular highly sulphated GAGs, we examined the GAGs profile of amyloid deposits in intervertebral discs using mucin histochemistry (Alcian blue: MgCl2 critical electrolyte concentration) and immunohistochemistry. We found strong staining for very highly sulphated GAGs (0.9 M and 1 M MgCl2) and confirmed the presence of keratan sulphate in both localized and systemic, dialysis-associated beta 2-microglobulin amyloid deposits within disc fibrocartilage. These findings suggest that qualitative and quantitative changes in matrix GAGs, particularly strongly sulphated GAGs such as keratan sulphate, may play a role in the pathogenesis of localized and systemic amyloid deposition in intervertebral discs.
椎间盘是局部关节和某些形式的系统性关节淀粉样蛋白沉积的常见部位。椎间盘结缔组织中是否存在有利于淀粉样蛋白沉积的内在基质因子尚不确定，但已知椎间盘中小的局部淀粉样蛋白沉积在很大程度上与年龄相关。由于已知椎间盘的糖胺聚糖（GAGs）组成会随年龄变化，并且由于某些形式的系统性淀粉样蛋白沉积已被证明与特定的高度硫酸化GAGs有关，我们使用粘蛋白组织化学（阿尔辛蓝：MgCl2临界电解质浓度）和免疫组织化学检查了椎间盘中淀粉样蛋白沉积物的GAGs谱。我们发现了对非常高度硫酸化的GAGs（0.9 M和1 M MgCl2）的强染色，并证实了在椎间盘纤维软骨内的局部和系统性、透析相关的β2-微球蛋白淀粉样蛋白沉积物中均存在硫酸角质素。这些发现表明，基质GAGs的定性和定量变化，特别是像硫酸角质素这样的强硫酸化GAGs，可能在椎间盘局部和系统性淀粉样蛋白沉积的发病机制中起作用。
