Experimental systolic and diastolic overloading in rats: total proteins turnover rate. Enzymatic and structural properties of myosin

• Published in: Basic research in cardiology Vol. 75; no. 1; p. 143
• Main Authors: Swynghedauw, B, Schwartz, K, Bercovici, J, Bouveret, P, Lompre, A M, Thiem, N V, Lacombe, G
• Format: Journal Article
• Language: English
• Published: Germany 01.01.1980
• Subjects: Adenosine Triphosphatases - metabolism; Animals; Antibodies; Aortic Valve Insufficiency - physiopathology; Aortic Valve Stenosis - physiopathology; Calcium - metabolism; Cardiomegaly - physiopathology; Complement Fixation Tests; Diastole; DNA - biosynthesis; Guinea Pigs; Myocardial Contraction; Myocardium - enzymology; Myosin Subfragments - immunology; Myosins; Proteins - metabolism; Rats; RNA - biosynthesis; Systole
• ISSN: 0300-8428
• DOI: 10.1007/BF02001406

The fractional turnover rate of the total cardiac proteins has been measured by using the continuous infusion technique with 3H lysine. It augments by a factor of 3 in systolic as well as in diastolic overloading, but in the former the peak was reached within the first week after operation and in the later the peak was not reached until the 14th day. The myosin structure and enzymatic properties have been studied in several huge hypertrophic hearts (around 100% hypertrophy). In this condition the burst size of myosin is normal, as well as its K+ ATPase, but there is a sharp decline in the Ca2+ ATPase activity. Moreover, antibodies against native or defolded heavy meromyosin exhibit, a vertical shift in microcomplement fixation when made to react with molecules extracted from hypertrophied hearts. The normal isozymic pattern of rat heart myosin, as shown in non dissociating electrophoresis, was reversed.