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Increased expression of α‐enolase in c‐ jun transformed rat fibroblasts without increased activation of plasminogen
Author(s) -
Bergman Ann-Charlotte,
Linder Christina,
Sakaguchi Kazuyasu,
Sten-Linder Margareta,
Alaiya Ayodele A,
Franzén Bo,
Shoshan Maria C,
Bergman Tomas,
Wiman Björn,
Auer Gert,
Appella Ettore,
Jörnvall Hans,
Linder Stig
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01247-7
Subject(s) - plasmin , enolase , downregulation and upregulation , proteolysis , microbiology and biotechnology , chemistry , receptor , messenger rna , biochemistry , biology , enzyme , gene , immunohistochemistry , immunology
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 α‐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 α‐enolase may contribute to an increased metabolic capacity, but not to increased plasminogen activation.