RT Journal Article
SR Electronic
T1 Purification and Identification of a 7.6-kDa Protein in Media Conditioned by Superinvasive Cancer Cells
JF Anticancer Research
JO Anticancer Res
FD International Institute of Anticancer Research
SP 1309
OP 1317
VO 27
IS 3A
A1 DOWLING, P.
A1 MAURYA, P.
A1 MELEADY, P.
A1 GLYNN, S.A.
A1 DOWD, A.J.
A1 HENRY, M.
A1 CLYNES, M.
YR 2007
UL http://ar.iiarjournals.org/content/27/3A/1309.abstract
AB Background: Selection of the human drug sensitive and invasive cell line (MDA-MB-435S-F) with the chemotherapeutic agent paclitaxel, resulted in the development of drug resistant cell lines displaying enhanced invasion-related characteristics. Materials and Methods: Serum-free conditioned media from the human cancer drug-sensitive and invasive cell line (MDA-MB-435S-F) and its paclitaxel-resistant superinvasive variant (MDA-MB-435S-F/Taxol10p4pSI) were analyzed using Surface enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF MS). Results: A differentially expressed protein was observed at 7.6 kDa, which was 4-fold up-regulated in MDA-MB-435S-F/Taxol10p4pSI. The differentially expressed protein was identified using matrix-assisted laser desorption ionization tandem time-of-flight mass spectrometry (MALDI-TOF/TOF MS), as a fragment of bovine transferrin. The transferrin receptor was also found to be overexpressed in the superinvasive cell line. Conclusion: Cleavage of serum proteins such as transferrin could provide a valuable source of markers for malignant tumours and could also play a role in aspects of cancer pathogenesis, such as tumour cachexia. Copyright© 2007 International Institute of Anticancer Research (Dr. John G. Delinassios), All rights reserved