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

Abstract

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.

• Authors: K Maruyama, F Kametani, S Ikeda, T Ishihara, N Yanagisawa
• Journal: Neuroscience letters (Neurosci Lett) Vol. 144 Issue 1-2 Pg. 38-42 (Sep 14 1992) ISSN: 0304-3940 [Print] Ireland
• PMID: 1436711 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amyloid beta-Peptides
• CST3 protein, human
• Cystatin C
• Cystatins
• Cysteine Proteinase Inhibitors

Topics

• Aged
• Amino Acid Sequence
• Amyloid beta-Peptides (metabolism)
• Cerebral Amyloid Angiopathy (metabolism, pathology)
• Cerebral Hemorrhage (pathology)
• Cystatin C
• Cystatins (metabolism)
• Cysteine Proteinase Inhibitors (pharmacology)
• Electrophoresis, Polyacrylamide Gel
• Humans
• Immunohistochemistry
• Male
• Meninges (pathology)
• Molecular Sequence Data