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Creatine Kinase Activity and Isozyme Composition in Normal Tissues and Neoplasms of Rats and Mice¹

The Fels Research Institute, Temple University School of Medicine, Philadelphia, Pennsylvania 19140 [J. B. S., S. W.], and The Department of Biochemistry, Howard University School of Medicine, Washington, D. C. 20001 [H. P. M.]

Creatine kinase (EC 2.7.3.2) was assayed for total activity by a spectrophotometric procedure after removal of adenylate kinase by gel filtration and for isozyme composition by diethylaminoethyl cellulose chromatography. In addition to high activity in skeletal and heart muscle and brain of normal rats and mice, lower but significant activities were found in liver, kidney, spleen, intestine, mammary gland, lung, aorta, and adipose tissue. Except for muscle (MM), heart (MM and MB), mammary gland (MM and BB), lung (MM and BB), and aorta (MM and BB), all other tissues, including whole early (13- to 15-day) embryo had only the BB form. Although adult liver had exclusively BB, late prenatal, neonatal, and early regenerating liver had MM and BB forms.

All solid and ascites tumors had creatine kinase with activities at about the same levels as those of the respective tissues of origin. Two rat hepatomas, S-19 and 5123C, and two mouse ascites tumors, the Ehrlich and S-37, had the BB form exclusively, whereas other tumors had some MM as well as BB isozyme. There was no clear correlation between either the total activity or isozyme composition and the growth rate or degree of differentiation of hepatomas. The isozyme transitions of connective tissue tumors deviated in part toward the fetal pattern with inconsistent appearance of the BB as well as the MM forms. However, isozyme composition of hepatomas and other tumors was altered in the direction of ectopic isozyme expression, with the appearance of MM as well as the BB form characteristic of the tissue of origin. The same isozyme transition toward ectopic expression of the MM form also occurred in perinatal and regenerating liver. These results demonstrate the wide occurrence of creatine kinase in normal tissues and its survival in the neoplastic transformation. Its functional significance in these tissues has to await data on the concentrations therein of creatine.

¹ This study was supported by Grants CA-10916, CA-10729, and CA-12227 from the National Cancer Institute, Department of Health, Education, and Welfare, and Grant BC-74 from the American Cancer Society.

² To whom requests for reprints should be addressed.

Received 8/28/78. Accepted 11/ 8/78.

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