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Protein kinase C (PKC) level is increased in PC12 cells overexpressing transfected liver‐type phosphofructokinase
Author(s) -
Elson Ari,
Weiss Yael,
Groner Yoram
Publication year - 1994
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/0248-4900(94)90051-5
Subject(s) - protein kinase c , diacylglycerol kinase , phosphofructokinase , biology , transfection , glycolysis , downregulation and upregulation , microbiology and biotechnology , pyruvate kinase , protein kinase a , kinase , biochemistry , gene , enzyme
Summary— PC12 cells which overexpress transfected liver‐type phosphofructokinase (PFKL) have previously been described as a model system for PFKL overexpression in Down's syndrome and have been shown to perform glycolysis at enhanced rates. Here we report that levels of protein kinase C (PKC) in PC 12‐PFKL cells were almost doubled, as estimated from in vitro activity and phorbol ester binding experiments and from an increase found in PKC‐alpha mRNA levels. Most of the added PKC was found to be associated with the cellular membrane while the cytoplasmic levels of PKC were barely increased. The steady‐state levels of 1,2‐sn‐diacylglycerol in PC12‐PFKL cells were found to be unaltered, suggesting that enhanced glycolysis in these cells did not influence PKC by altering the amounts of this compound. PFKL is one of several genes known to be overexpressed in Down's syndrome. Upregulation of PKC due to PFKL overexpression could result in widespread disturbances of gene expression and play a part in causing some of the many symptoms of the disease.