Increased expression of α‐enolase in c‐jun transformed rat fibroblasts without increased activation of plasminogen

FEBS Letters

Linder, Stig²  Alaiya, Ayodele A³  Franzén, Bo³  Sakaguchi, Kazuyasu¹  Appella, Ettore¹  Sten-Linder, Margareta⁴  Bergman, Ann-Charlotte⁵  Shoshan, Maria C²  Auer, Gert³  Bergman, Tomas⁵  Linder, Christina²  Wiman, Björn⁴  Jörnvall, Hans⁵ 

[1] Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA;Radiumhemmet's Research Laboratory, Department of Oncology and Pathology, Karolinska Institutet and Hospital, S-171 76 Stockholm, Sweden;Unit of Cell and Molecular Analysis, Department of Oncology and Pathology, Karolinska Institutet and Hospital, S-171 76 Stockholm, Sweden;Department of Clinical Chemistry, Department of Oncology and Pathology, Karolinska Institutet and Hospital, S-171 76 Stockholm, Sweden;Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden

关键词: Two-dimensional gel electrophoresis;    Mass spectrometry;    Cell transformation;    Plasminogen activation;   

DOI  :  10.1016/S0014-5793(97)01247-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown