Increased expression of alpha-enolase in c-jun transformed rat fibroblasts without increased activation of plasminogen.
Two-dimensional gel electrophoresis was used to identify polypeptides differentially expressed between normal and c-jun transformed rat fibroblasts. The level of a 49 kDa polypeptide was 3-fold elevated in c-jun transformed cells. Sequence analysis by ion trap mass spectrometry identified the polypeptide as rat alpha-enolase. Enolase functions as a cell surface receptor for plasminogen, suggesting that upregulation may increase plasminogen activation and cell surface proteolysis important for tumor growth. However, no difference was observed between normal and transformed cells in formation of plasmin, suggesting that upregulation of alpha-enolase may contribute to an increased metabolic capacity, but not to increased plasminogen activation.
Bergman
A C
AC
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Linder
C
C
Sakaguchi
K
K
Sten-Linder
M
M
Alaiya
A A
AA
Franzén
B
B
Shoshan
M C
MC
Bergman
T
T
Wiman
B
B
Auer
G
G
Appella
E
E
Jörnvall
H
H
Linder
S
S
D000818:Animals; D002461:Cell Line, Transformed; D002471:Cell Transformation, Neoplastic; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism; D015870:Gene Expression; D016758:Genes, jun; D006801:Humans; D010751:Phosphopyruvate Hydratase / Q000096:biosynthesis*; D010958:Plasminogen / Q000378:metabolism*; D016755:Proto-Oncogene Proteins c-jun / Q000235:genetics / Q000378:metabolism*; D051381:Rats
D016755:Proto-Oncogene Proteins c-jun; D010958:Plasminogen; D010751:Phosphopyruvate Hydratase