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Differential solubility analysis of fractionated heart proteins in laboratory animals
Author(s) -
Suzuki Osamu,
Koura Minako,
Takano Kaoru,
Noguchi Yoko,
UchioYamada Kozue,
Matsuda Junichiro
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.902.8
Subject(s) - guinea pig , fractionation , myosin , chemistry , microbiology and biotechnology , glycoprotein , biology , solubilization , biochemistry , chromatography , endocrinology
At the EB2007 meeting, we reported an abnormality of collagen type VI in our transgenic mice with dilated cardiomyopathy based on an analysis of heart proteins fractionated using differential solubilization. To examine if this protein fractionation technique can be applied to proteomic analysis of the hearts of other laboratory animals, we compared fractionated heart proteins among four normal laboratory animals: mice, rats, guinea pigs, and rabbits. Heart proteins were extracted sequentially using differential solubilization with SB3‐10 (ReadyPrep Sequential Extraction Kit; Bio‐Rad) and the three fractions were separated independently using SDS‐PAGE. As in our previous study using mice, we obtained similar band patterns involving three fractions from rat, guinea pig, and rabbit heart proteins. In particular, bands for collagen type VI alpha‐3 subunits and cardiac myosin heavy chains in the most insoluble fractions, both of which were suggested by results in mice, were also visualized for rat, guinea pig and rabbit proteins. Our results suggest that the fractionation of heart proteins would be useful for proteomic analysis of impaired hearts in various animals, especially for analyzing the collagen type VI content. This work was supported by a Health and Labor Science Research Grant from MHLW, Japan.