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Expression of pyruvate kinase in astrocytes induced to differentiate in vitro
Author(s) -
Ngo J. L.,
Ibsen K. H.
Publication year - 1989
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490230109
Subject(s) - pyruvate kinase , pkm2 , isozyme , biochemistry , pyruvate carboxylase , biology , microbiology and biotechnology , in vitro , pyruvate dehydrogenase phosphatase , pyruvate dehydrogenase kinase , kinase , pyruvate dehydrogenase lipoamide kinase isozyme 1 , chemistry , enzyme , glycolysis
Astrocytes maintained in a chemically defined media undergo differentiation and a parallel increase in pyruvate kinase specific activity. These changes are accompanied by a shift in the isoelectrofocusing pattern, but not by expression of pyruvate kinase M 4 the characteristic adult rat brain isozyme. Thus, this chemically defined media lacks a substance required to induce pyruvate kinase M synthesis and this function can be uncoupled from other aspects of cellular differentiation. The uncoupling of pyruvate kinase maturation from cellular differentiation and the observation of only a single, 2.3 kilobase, pyruvate kinase mRNA molecule at different stages of the postnatal development of rat brain support the concept that the K‐ to M‐isoform transformation is a posttranscriptional event. The effect of the individual components of this chemically defined medium on pyruvate kinase specific activity was studied by eliminating one component at a time. The increase in activity was found to be completely dependent upon fibroblastic growth factor and prostaglandin F 2α and was partially dependent on the simultaneous presence of insulin.