The association of an elastase with amyloid fibrils.
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.
D000682:Amyloid / Q000032:analysis*; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D010196:Pancreatic Elastase / Q000097:blood / Q000302:isolation & purification*; D000685:Serum Amyloid A Protein / Q000032:analysis*; D012995:Solubility
D000682:Amyloid; D000685:Serum Amyloid A Protein; C035222:amyloid protein AL; D010196:Pancreatic Elastase