Department of Dermatology, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, 93053 Regensburg, Germany.
Eur J Dermatol. 2010 Mar-Apr;20(2):152-60. doi: 10.1684/ejd.2010.0842. Epub 2010 Jan 14.
Extracellular deposition of altered autologous protein (amyloid protein) within the dermis is the hallmark of cutaneous amyloidoses and systemic amyloidoses with cutaneous involvement. Amyloidoses may be acquired or hereditary in nature and subclassification differentiates between primary amyloidosis (no obvious predisposing disease) and secondary amyloidosis (specific underlying disease). More than 26 different proteins and peptides have been identified as amyloid precursors and these proteins are used to subclassify this heterogeneous group of diseases. The amyloid proteins show an anti-parallel beta-sheet conformation and form non-branching linear filaments of variable lengths and diameters of approximately 7.5 to 10 nm. However, the exact etiopathogenesis of amyloid formation still remains unclear. Depending on histoanatomical distribution and amount, amyloid may cause progressive and life-threatening organ dysfunction. Clinical presentation, histology, electron microscopy, and biochemical-immunological differentiation represent decisive tools for an accurate diagnosis.
皮肤淀粉样变和伴有皮肤累及的系统性淀粉样变的特征是细胞外沉积改变的自身蛋白（淀粉样蛋白）。淀粉样变可能是获得性的，也可能是遗传性的，亚分类将原发性淀粉样变（无明显诱发疾病）和继发性淀粉样变（特定基础疾病）区分开来。已经确定了超过 26 种不同的蛋白质和肽作为淀粉样前体，这些蛋白质用于对这种异质疾病组进行分类。淀粉样蛋白显示出反平行β-折叠构象，并形成具有不同长度和直径的大约 7.5 至 10nm 的非分支线性纤维。然而，淀粉样蛋白形成的确切病因仍然不清楚。根据组织解剖学分布和数量，淀粉样蛋白可能导致进行性和危及生命的器官功能障碍。临床表现、组织学、电子显微镜和生化免疫分化是准确诊断的决定性工具。
