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Expression of muscle‐specific isozymes of phosphorylase and creatine kinase in human muscle fibers cultured aneurally in serum‐free, hormonally/chemically enriched medium
Author(s) -
Pegolo Giovanna,
Askanas Valerie,
Engel W. King
Publication year - 1990
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/0736-5748(90)90036-2
Subject(s) - biology , isozyme , glycogen phosphorylase , creatine kinase , myocyte , endocrinology , skeletal muscle , medicine , cell culture , growth factor , epidermal growth factor , chemically defined medium , biochemistry , glycogen , enzyme , in vitro , genetics , receptor
Primary cultures of muscle cells derived from a biopsied adult human skeletal muscle were grown up to 6 weeks in a hormonally/chemically enriched serum‐free medium. The expression of musclespecific isozymes of creatine kinase, glycogen phosphorylase, and phosphoglycerate mutase, indicative of muscle cell maturation, was studied after 1,4 and 6 weeks of growth. The maturation of muscle fibers cultured in serum‐free medium was comparable to that achieved by muscle fibers cultured in medium containing 10% serum and supplemented with growth factors (insulin, epidermal growth factor, and fibroblastic growth factor) and was greater than that achieved in medium containing 10% serum only. Our study demonstrates that adult human muscle can be cultured aneurally for a long period of time in a serum‐free medium, and that it can achieve a high degree of maturation. This study provides an important basis for investigations related to: (1) assessment of the influence of individual components of the medium on human muscle maturation in culture; (2) studies of regulation of abnormal gene expression in diseased human muscle cultured in serum‐free medium.