Hol P R, van Ederen A M, Snel F W, Langeveld J P, Veerkamp J H, Gruys E
Br J Exp Pathol. 1985 Jun;66(3):279-92.
Casein-induced amyloidosis in hamsters was found to be of the AA-type, as shown by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and amino acid analysis of the major low-molecular weight component of the amyloid fibrils. Levels of serum amyloid A (SAA) and the activities of cathepsin D, beta-N-glucosaminidase, serine esterase, lactate dehydrogenase (LDH) and gamma glutamyl transpeptidase (GGT) were measured in the blood plasma during induction of amyloidosis. During the pre-amyloid phase an increase was observed in all these parameters. During the deposition of amyloid, an increase was observed in the activities of the lysosomal enzymes cathepsin D and beta-N-glucosaminidase, which was significantly correlated with amyloid deposition. Serine esterase activities did not show any relationship to amyloid deposition. LDH and GGT activities were normal in the amyloid phase. SAA levels were lower during amyloid deposition than during the pre-amyloid phase. These findings indicate that a specific release of lysosomal contents from mononuclear phagocytic cells is involved in the pathogenesis of AA-amyloidosis. Amyloid deposition may be the result of: (i) extrusion of intralysosomal protein AA or pre-amyloid, followed by extracellular formation of amyloid fibrils; (ii) secretion of lysosomal enzymes, followed by extracellular cleavage of SAA and subsequent aggregation of protein AA with other components.
如通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）以及对淀粉样纤维主要低分子量成分的氨基酸分析所示，仓鼠中的酪蛋白诱导型淀粉样变性属于AA型。在淀粉样变性诱导过程中，对血浆中的血清淀粉样蛋白A（SAA）水平以及组织蛋白酶D、β-N-氨基葡萄糖苷酶、丝氨酸酯酶、乳酸脱氢酶（LDH）和γ-谷氨酰转肽酶（GGT）的活性进行了测定。在淀粉样变前期，所有这些参数均出现升高。在淀粉样蛋白沉积期间，观察到溶酶体酶组织蛋白酶D和β-N-氨基葡萄糖苷酶的活性增加，这与淀粉样蛋白沉积显著相关。丝氨酸酯酶活性与淀粉样蛋白沉积无任何关联。在淀粉样变阶段，LDH和GGT活性正常。淀粉样蛋白沉积期间的SAA水平低于淀粉样变前期。这些发现表明，单核吞噬细胞溶酶体内容物的特异性释放参与了AA型淀粉样变性的发病机制。淀粉样蛋白沉积可能是以下结果：（i）溶酶体内蛋白质AA或淀粉样前体的挤出，随后在细胞外形成淀粉样纤维；（ii）溶酶体酶的分泌，随后SAA在细胞外被裂解，以及蛋白质AA与其他成分随后发生聚集。
