Identification of proteins regulated by interferon-alpha in resistant and sensitive malignant melanoma cell lines.
Proteomics
; 4(12): 3998-4009, 2004 Dec.
Article
in En
| MEDLINE
| ID: mdl-15449380
ABSTRACT
Treatment of patients with malignant melanoma with interferon-alpha achieves a response in a small but significant subset of patients. Currently, although much is known about interferon biology, little is known about either the particular mechanisms of interferon-alpha activity that are crucial for response or why only some patients respond to interferon-alpha therapy. Two melanoma cell lines (MeWo and MM418) that are known to differ in their response to the antiproliferative activity of interferon-alpha, have been used as a model system to investigate interferon-alpha action. Using a proteomics approach based on two-dimensional polyacrylamide gel electrophoresis and mass spectrometry, several proteins induced in response to interferon-alpha have been identified. These include a number of gene products previously known to be type I interferon responsive (tryptophanyl tRNA synthetase, leucine aminopeptidase, ubiquitin cross-reactive protein, gelsolin, FUSE binding protein 2 and hPNPase) as well as a number of proteins not previously reported to be induced by type I interferon (cathepsin B, proteasomal activator 28alpha and alpha-SNAP). Although the proteins upregulated by interferon-alpha were common between the cell lines when examined at the level of Western blotting, the disparity in the basal level of cathepsin B was striking, raising the possibility that the higher level in MM418 may contribute to the sensitivity of this cell line to interferon-alpha treatment.
Search on Google
Database:
MEDLINE
Main subject:
Gene Expression Regulation, Neoplastic
/
Interferon-alpha
/
Melanoma
Type of study:
Diagnostic_studies
Limits:
Humans
Language:
En
Year:
2004
Type:
Article