Nuclear proteins in the heart of the cardiomyopathic Syrian hamster. Fractionation of phenol-soluble nonhistone proteins by two-dimensional polyacrylamide gel electrophoresis.

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Abstract
Nonhistone nuclear proteins (NHNP) were isolated from the hearts of hamsters in the myolytic, hypertrophic and failing phases of cardiomyopathy and from paired controls. These proteins were solubilized in phenol and fractionated by polyacrylamide gel electrophoresis. One-dimensional gel electrophoresis, using either isoelectrofocusing or sodium dodecyl sulfate, showed quantitative differences between the dystrophic hearts and the controls. A high resolution of NHNP was achieved by 2-dimensional gel electrophoresis, revealing both quantitative and limited qualitative differences between the 2 groups. Proteins focusing from pH 5.0-5.6 with molecular weights of 55,000 (P5) and 100,000 (P1) were strikingly increased in the cardiomyopathy. A protein (P2) with an isoelectric point of 5.1 and some NHNP from dystrophic hearts in the entire region from pH 7.0-9.0 with molecular weights ranging from 35,000 (P7)-68,000 (P4) were markedly reduced or absent. Differences in NHNP could be detected during the myolytic phase of cardiomyopathy but were most striking during the terminal phase of the disease. There were no detectable differences between the profiles of proteins derived from whole heart homogenates of dystrophic hamsters and controls. There were no significant differences at the failing phase between NHNP isolated from a purified preparation of myocardial cells and those isolated from whole heart. The differences in NHNP appear to be reflections of alterations in nuclear composition of the dystrophic myocardial cell. Some of these observations may represent changes secondary to heart disease. If NHNP interacting with DNA play a major role in genetic expression, some of the manifestations of hamster cardiomyopathy could be due to a different constitution of NHNP in the dystrophic heart.

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