Characterization of amyloid fibril protein from a case of cerebral amyloid angiopathy showing immunohistochemical reactivity for both beta protein and cystatin C.
We isolated and carried out a chemical analysis of the amyloid fibril protein from the leptomeningeal vessels of a case with non-hereditary cerebral amyloid angiopathy (CAA) showing dual immunohistochemical reactivity with antibodies to both beta-protein and cystatin C. A crude amyloid fibril fraction reacted only with anti-beta-protein antibody, and cystatin C immunoreactivity was observed in the first PBS supernatant. Complete amino acid sequence of this cystatin C-immunoreactive protein showed a homologous structure to that of normal cystatin C. It is concluded that cystatin C is not an intrinsic component of the amyloid fibril in this type of CAA.
Maruyama
K
K
Department of Medicine (Neurology), Shinshu University School of Medicine, Matsumoto, Japan.
Kametani
F
F
Ikeda
S
S
Ishihara
T
T
Yanagisawa
N
N
D000368:Aged; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D016657:Cerebral Amyloid Angiopathy / Q000378:metabolism* / Q000473:pathology; D002543:Cerebral Hemorrhage / Q000473:pathology; D055316:Cystatin C; D015891:Cystatins / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D008578:Meninges / Q000473:pathology; D008969:Molecular Sequence Data
D016229:Amyloid beta-Peptides; C525030:CST3 protein, human; D055316:Cystatin C; D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors