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Characterization of amyloid fibril protein from a case of cerebral amyloid angiopathy showing immunohistochemical reactivity for both beta protein and cystatin C

Maruyama, K.; Kametani, F.; Ikeda, S.; Ishihara, T.; Yanagisawa, N.

Neuroscience Letters 144(1-2): 38-42

1992

ISSN/ISBN: 0304-3940
PMID: 1436711
Accession: 008295659
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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.

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Related References

Maruyama, K.; Kametani, F.; Ikeda, S.; Ishihara, T.; Yanagisawa, N. 1992: Characterization of amyloid fibril protein from a case of cerebral amyloid angiopathy showing immunohistochemical reactivity for both protein and cystatin C Neuroscience Letters 144(1-2): 38-42
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