1. Volume 129, Issue 4, Pages 1187-1197 (October 2005)
Pancreatic Cancer Proteome: The Proteins That Underlie Invasion, Metastasis, and Immunologic Escape 
Ru Chen, Eugene C. Yi, Samuel Donohoe, Sheng Pan, Jimmy Eng, Kelly Cooke, David A. Crispin, Zhaoli Lane, David R. Goodlett, Mary P. Bronner, Ruedi Aebersold, Teresa A. Brentnall 
Gastroenterology 
Volume 129, Issue 4, Pages (October 2005)
DOI: /j.gastro
Copyright © 2005 American Gastroenterological Association Terms and Conditions

2. Figure 1
Global protein profiling in pancreatic cancer using the ICAT approach. (A) Protein numbers identified in 2 separate pancreatic cancer comparison studies. There were 656 unique proteins identified in 2 experiments, of which 251 were identified in both samples, 272 proteins were identified only in experiment 1, and 133 proteins were identified only in experiment 2. (B) Distribution of the identified pancreatic cancer proteins. The 656 proteins identified and quantified in pancreatic cancer were classified based on their cellular components. Cellular location was assigned according to the Gene Ontology Consortium.
Gastroenterology  , DOI: ( /j.gastro )
Copyright © 2005 American Gastroenterological Association Terms and Conditions

3. Figure 2
Protein abundance changes in pancreatic cancer. The y-axis represents the ratio of protein quantity in pancreatic cancer to normal pancreas, in Log2 scale. The x-axis is the number of the proteins. There were a total of 907 proteins identified in both cancer samples, including 251 redundant proteins between 2 samples. The ratios that are outside the bold lines (above or below) represent the proteins with at least 2-fold abundance change.
Gastroenterology  , DOI: ( /j.gastro )
Copyright © 2005 American Gastroenterological Association Terms and Conditions

4. Figure 3
Differentially expressed proteins in pancreatic cancer. (A) For cancer sample 1 and sample 2, 111 proteins and 90 proteins were differentially expressed by at least 2-fold, respectively. The ratios for the rest of the proteins were between 0.5 and 2.0, which represented <2-fold abundance change in cancer samples. (B) For the 251 proteins identified in both experiments, 50 were differentially expressed in both cancer samples by at least 2-fold, while 25 were only differentially expressed in sample 1, and 16 were only differentially expressed in sample 2. The ratios for the rest of the 160 proteins were between 0.5 and 2 for both samples. Protein ratio represents protein abundance in cancer/normal.
Gastroenterology  , DOI: ( /j.gastro )
Copyright © 2005 American Gastroenterological Association Terms and Conditions

5. Figure 4
Quantification and validation of protein overexpression in pancreatic cancer. (A) Annexin A2 was identified and quantified to be overexpressed (2.6-fold increase) in pancreatic cancer by ICAT analysis in cancer sample 2. Note that the y-axis protein quantification scale of the cancer sample is about 2-fold greater than the y-axis scale of the normal sample. (B) Western blotting confirmed that annexin A2 was overexpressed by a 2.2-fold increase in pancreatic cancer sample 2. Consistent correlation of the ICAT data and Western blot data were also presented for annexin A2 in cancer sample 1 and cathepsin D and integrin β1 in both cancer samples.
Gastroenterology  , DOI: ( /j.gastro )
Copyright © 2005 American Gastroenterological Association Terms and Conditions

6. Figure 5
IHC of integrin β1 and annexin A2 in pancreatic cancer. Positive stain is in brown. Integrin β1 was expressed marginally (1+) in the basal area of normal pancreatic ducts (A and B), but it is strongly expressed (3+) in pancreatic cancer (C and D). Annexin A2 was also expressed weakly in normal pancreatic ducts (E and F) and strongly expressed in cancer (G and H). The scale of the reading was as follows: 0, negative; 1+, mild; 2+, moderate; 3+, strong.
Gastroenterology  , DOI: ( /j.gastro )
Copyright © 2005 American Gastroenterological Association Terms and Conditions

7. Figure 6
Summary of differentially regulated proteins involved in facilitation of tumor growth, migration, angiogenesis, invasion, metastasis, and immunologic escape. (A) Pancreatic cancer cells secrete proteins that destroy extracellular matrix, which in turn secretes proteins promoting cancer cell invasion, immunologic escape, and angiogenesis. (B) The proteins that were differentially regulated in cancer are shown in blue. Through an orchestration of protein cross-talk—between cancer cells, stromal cells, and eventually neovascular cells—the initiation and progression of pancreatic cancer take place.
Gastroenterology  , DOI: ( /j.gastro )
Copyright © 2005 American Gastroenterological Association Terms and Conditions