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. 1977 Jun 1;18(2):143–151. doi: 10.1186/BF03548442

Ontogenetic Development of Creatine Phosphokinase in Skeletal Muscles and Heart from Pigs

Ontogenetisk udvikling af kreatinfosfokinase i tvaerstribede muskier og hjerte hos svin

S Cepica 11,21,✉, P Fogd Jørgensen 11
PMCID: PMC8377664  PMID: 878961

Abstract

Creatine Phosphokinase (CPK) in striated muscles shows only small changes in activity before birth. After birth and during the first month of extrauterine life the activity increases rapidly. The largest increase is seen in muscles with a glycolytic energy metabolism (m. long, dorsi) and the smallest in muscles with an oxydative energy metabolism (m. flexor dig. ped. sup.). The differences between these groups of muscles are statistically significant. In heart tissue the increase in CPK activity is lower, the levels amounting to 40 to 47 % of those in striated muscles.

Early in fetal life only the BB isoenzyme is found in striated muscles. Synthesis of M subunits of GPK starts between day 76 and 65 before birth and increases rapidly after this time leading to disappearance of the BB isoenzyme 24 days prior to birth and of the MB isoenzyme at birth. In muscles with an oxydative as well as in muscles with a glycolytic metabolism all GPK activity after birth is caused by the MM isoenzyme.

All three isoenzymes are present in heart tissue at the earliest prenatal stage investigated, the pattern being dominated by the BB isoenzyme. During further differentiation the MM isoenzyme increases and the BB isoenzyme decreases. The development is completed during the first month after birth with a final isoenzyme composition of 81 % MM and 19 % MB isoenzyme. kw|Keywords|k]pigs; k]ontogenesis; k]creatine phosphokinase; k]activity; k]isoenzymes

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Acknowledgments

The authors wish to express their gratitude to Professor, dr. med. vet. J. Moustgaard on whose initiative the present investigation was undertaken.

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