Proteomic characterisation of pancreatic islet beta-cells stimulated with pancreatic carcinoma cell conditioned medium.
OBJECTIVE
To characterise the protein expression profiles of pancreatic islet beta-cells affected by cancer cells, and to identify the potential islet molecules related to pancreatic cancer-associated diabetes.


METHODS
The cellular proteins of islet beta-cell line INS-1 in response to conditioned medium (CM) prepared from pancreatic cancer cells were analysed using fluorescence-labelled 2D gel-based proteomics (2D-DIGE).


RESULTS
10 proteins were over-expressed and five were under-expressed in cancer CM-stimulated beta-cells. Five differently expressed proteins were selected for further validation by Western blot analysis. HSP60 and peripherin, which have previously been reported to be associated with type 1 diabetes, and Prp19, a DNA repair protein, were up-regulated in INS-1 cells after cancer cell CM stimulation; HMOX1 and GRP78 were down-regulated. The islets adjacent to human pancreatic carcinomas showed increased peripherin expression than normal pancreatic islets.


CONCLUSIONS
These results provide new information regarding the regulation of protein expression in pancreatic cancer-associated diabetes.
Song
G
G
Shandong Medicinal Biotechnology Center, Shandong Academy of Medicinal Sciences, Key Laboratory for Biotech-Drugs Ministry of Health & Key Laboratory for Modern Medicine and Technology of Shandong Province, Jinan, Shandong Province, China.
Cui
Y
Y
Zhong
N
N
Han
J
J
D000230:Adenocarcinoma / Q000150:complications / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D018834:Chaperonin 60 / Q000378:metabolism; D018920:Coculture Techniques; D017077:Culture Media, Conditioned; D045643:DNA Repair Enzymes / Q000378:metabolism; D003920:Diabetes Mellitus / Q000209:etiology / Q000378:metabolism; D000091342:Endoplasmic Reticulum Chaperone BiP; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D007381:Intermediate Filament Proteins / Q000378:metabolism; D007515:Islets of Langerhans / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D010190:Pancreatic Neoplasms / Q000150:complications / Q000378:metabolism* / Q000473:pathology; D064531:Peripherins; D040901:Proteomics / Q000379:methods; D000072260:RNA Splicing Factors; D051381:Rats; D014407:Tumor Cells, Cultured
D018834:Chaperonin 60; D017077:Culture Media, Conditioned; D000091342:Endoplasmic Reticulum Chaperone BiP; C000717247:HSPA5 protein, human; D007381:Intermediate Filament Proteins; D008562:Membrane Glycoproteins; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; C578994:PRPH protein, human; D064531:Peripherins; D000072260:RNA Splicing Factors; D045643:DNA Repair Enzymes; C417041:PRPF19 protein, human