Document Detail


Accumulation of Cyclophilin A isoforms in conditioned medium of irradiated breast cancer cells.
MedLine Citation:
PMID:  22623065     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Secreted proteins play a key role in cell signalling and communication. We recently showed that ionizing radiations induced a delayed cell death of breast cancer cells, mediated by the death receptor pathways through the expression of soluble forms of "death ligands". Using the same cell model, the objective of our work was the identification of diffusible factors, secreted following cell irradiation, potentially involved in cell death signalling. Differential proteomic analysis of conditioned media using 2-dimensional gel electrophoresis resulted in detection of numerous spots which were significantly modulated following cell irradiation. The corresponding proteins were identified using MALDI TOF MS and LC-MS/MS approaches. Interestingly, five isoforms of cyclophilin A were observed as increased in conditioned medium of irradiated cells. These isoforms differed in iso-electric points and in accumulation levels. An increase of cyclophilin A secretion was confirmed by western-blotting of conditioned media of irradiated or radiosentive mammary cells. These isoforms displayed an interesting pattern of protein maturation and post-translational modifications, including an alternating removal of N-terminal methionine, associated with a combination of acetylations and methylations. The role of the protein is discussed in relation with its potential involvement in the mechanisms of inter-cells relationships and radiosensitivity.
Authors:
François Chevalier; Jordane Depagne; Sonia Hem; Sylvie Chevillard; Julie Bensimon; Pascale Bertrand; Jérôme Lebeau
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-5-23
Journal Detail:
Title:  Proteomics     Volume:  -     ISSN:  1615-9861     ISO Abbreviation:  -     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-5-24     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101092707     Medline TA:  Proteomics     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Affiliation:
CEA, DSV, iRCM, Plateforme de Protéomique, Fontenay-aux-Roses, France.
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