PT  - JOURNAL ARTICLE
AU  - DOWLING, P.
AU  - MAURYA, P.
AU  - MELEADY, P.
AU  - GLYNN, S.A.
AU  - DOWD, A.J.
AU  - HENRY, M.
AU  - CLYNES, M.
TI  - Purification and Identification of a 7.6-kDa Protein in Media Conditioned by Superinvasive Cancer Cells
DP  - 2007 May 01
TA  - Anticancer Research
PG  - 1309--1317
VI  - 27
IP  - 3A
4099  - http://ar.iiarjournals.org/content/27/3A/1309.short
4100  - http://ar.iiarjournals.org/content/27/3A/1309.full
SO  - Anticancer Res2007 May 01; 27
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