Skinner M, Stone P, Shirahama T, Connors L H, Calore J, Cohen A S
Proc Soc Exp Biol Med. 1986 Feb;181(2):211-4. doi: 10.3181/00379727-181-42242.
The fibrils of all systemic forms of amyloid (primary, AL; secondary, AA; and hereditary, AF) that had been isolated by the water extraction procedure demonstrated elastolytic enzyme activity when examined in a specific assay using tritiated elastin. The source of this fibril-bound enzyme activity was consistent with human neutrophil elastase (HNE), since it was readily extracted by high salt solutions and inhibited by an elastase-specific chloromethyl ketone inhibitor, human alpha-1-protease inhibitor or by an antibody specific for HNE. The presence of an elastase on the amyloid fibril may suggest physiologic mechanisms of amyloid precursor protein degradation.
通过水提取程序分离出的所有系统性淀粉样变形式（原发性淀粉样变，AL；继发性淀粉样变，AA；遗传性淀粉样变，AF）的纤维，在使用氚标记弹性蛋白的特定检测中进行检测时，均显示出弹性蛋白酶活性。这种与纤维结合的酶活性来源与人类中性粒细胞弹性蛋白酶（HNE）一致，因为它很容易被高盐溶液提取，并被弹性蛋白酶特异性氯甲基酮抑制剂、人类α-1蛋白酶抑制剂或针对HNE的特异性抗体所抑制。淀粉样纤维上存在弹性蛋白酶可能提示淀粉样前体蛋白降解的生理机制。
