RGD Reference Report - Amyloid formation in rat transthyretin: effect of oxidative stress. - Rat Genome Database

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Amyloid formation in rat transthyretin: effect of oxidative stress.

Authors: Tajiri, T  Ando, Y  Hata, K  Kamide, K  Hashimoto, M  Nakamura, M  Terazaki, H  Yamashita, T  Kai, H  Haraoka, K  Imasato, A  Takechi, K  Nakagawa, K  Okabe, H  Ishizaki, T 
Citation: Tajiri T, etal., Clin Chim Acta 2002 Sep;323(1-2):129-37.
RGD ID: 730200
Pubmed: PMID:12135814   (View Abstract at PubMed)

BACKGROUND: Transgenic mice carrying a human mutant transthyretin (TTR) gene are too small for in vivo experiments. It is necessary to have rat TTR protein and its antibody to overcome this problem. METHODS: Posttranslational modification of purified TTR was analyzed by means of matrix-assisted laser desorption ionization/time-of-flight mass spectrometry (MALDI/TOF-MS). Production of amyloid fibrils in vitro was confirmed by thioflavin T test and electron microscopy. Amyloidogenicity of rat TTR from rats with or without challenging paraquat was compared in vitro by thioflavin T test. RESULTS: MALDI/TOF-MS for rat TTR revealed three major modified forms-sulfate-conjugated, Cys-conjugated and glutathione-conjugated-in addition to the unconjugated (free) form of TTR. Although rat TTR in buffer of pH 7.0 could not make amyloid fibrils, rat TTR at pH 2.0-3.5 significantly formed amyloid fibrils, as confirmed by the thioflavin T test and electron microscopy. TTR purified from rats administered 4 mg/kg of paraquat formed much more amyloid fibrils than that from normal rats at pH 2.0-3.5 and significant amyloid fibrils were confirmed even at pH 7.0. CONCLUSIONS: Rat TTR may be a valuable experimental tool for examination of the amyloidogenicity of senile systemic amyloidosis (SSA) as well as familial amyloidotic polyneuropathy (FAP) both in vitro and in vivo.

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Gene Ttr transthyretin Rattus norvegicus

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