Asynchronous regulation of muscle specific isozymes of creatine kinase, glycogen phosphorylase, lactic dehydrogenase and phosphoglycerate mutase in innervated and non-innervated cultured human muscle

Andrea Martinuzzi, Valerie Askanas, Takayoshi Kobayashi, W. King Engel

Research output: Contribution to journalArticlepeer-review

Abstract

Expression of muscle specific isozymes (MSIs) of creatine kinase (CK, EC 2.7.3.2), glycogen phosphorylase (GP, EC 2.4.1.1), lactate dehydrogenase (LDH, EC 1.1.1.27) and phosphoglycerate mutase (PGAM, EC 2.7.5.3) was studied both in cultured human muscle fibers which had been innervated (InnCHMFs) for 20-83 days, and in their non-innervated (non-InnCHMFs) sister control. In non-InnCHMFs, the MSI of PGAM was never detected, and there was no change in the expression of the MSI of CK during the entire period examined; the expression of MSIs of LDH and GP showed linear increase during the entire period of growth. The expression of MSIs of all 4 enzymes was significantly enhanced in InnCHMFs as compared to non-innervated control. The expression of MSIs of GP and PGAM, and to a lesser degree of LDH increased significantly in correlation with the duration of innervation; the MSI of CK increased linearly only up to 54 days of innervation and plateaued afterward. This study demonstrates: (1) innervation of cultured human muscle fibers by fetal rat spinal cord exerts a time-related maturational influence on their cellular isoenzymatic pattern; (2) to achieve induction and characteristic time-related expression of various MSIs, the requirements for neuronal influences seem to differ.

Original languageEnglish
Pages (from-to)216-222
Number of pages7
JournalNeuroscience Letters
Volume89
Issue number2
DOIs
Publication statusPublished - Jun 29 1988

Keywords

  • Creatine kinase
  • Innervated cultured human muscle
  • Lactic dehydrogenase
  • Phosphoglycerate mutase
  • Phosphorylase

ASJC Scopus subject areas

  • Neuroscience(all)

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