Analysis of AGE modified proteins and RAGE expression in HER2/neu negative invasive ductal carcinoma

RAGE and its ligands in cancer – culprits, biomarkers, or therapeutic targets?

“…Cancer is associated with increased glycolysis and carbonyl stress [24]. In view of this, AGE modified proteins were, e.g.…”

“…Expression of RAGE and its splice variants increased [29] Gastric cancer A Gly82Ser polymorphism associated with gastric cancer and invasion of gatric cancer [34] Colorectal cancer RAGE highly expressed [22], ↑ RAGE expression in primary tumor correlates with the formation of metastases and reduced survival [35], Gly82Ser RAGE polymorphism associated in Chinese population with the risk and invasion of colorectal cancer [36] Inverse association between sRAGE and colorectal adenoma among pts without hypertension [13], inverse relation between sRAGE and colorectal cancer [65] Hepatocellular cancer RAGE highly expressed [22] sRAGE inversely associated with liver cancer [63], sRAGE predicted the response to transarterial chemoembolization of liver cancer [64], Pancreatic cancer In a murine model targeted ablation of RAGE delayed the development of pancreatic neoplasia [38], Absence of RAGE in mice delayed the development of pancreatic neoplasia [39], polymorphisms of RAGE not associated with pancreatic cancer [40] sRAGE levels inversely associated with pancreatic cancer [61], sRAGE levels ↓ in pacreatic cancer (↓↓ in diabetics with pancreatic cancer [40], no association between levels of esRAGE and pancreatic cancer with the exception of patients with shorter follow-up [ Estrogens induce RAGE expression on breast cancer cells and prolong their survival [49], RAGE highly expressed in breast cancer [22], RAGE expression correlated with the levels of AGE modified proteins [24], no difference in genetic polymorphisms of RAGE between breast cancer and healthy controls [50,51], rs184003 polymorphism and T-T-G-T haplotype more frequent in breast cancer compared to healthy controls [52] Lower sRAGE levels in breast [50], but increasing in pts with advanced breast cancer, lower grade, positive estrogen receptors, and intermediate positivity of Her2/neu, genetic polymorphisms of RAGE related to serum levels of RAGE [50] Melanoma RAGE silencing inhibits migration of melanoma cells [53], ↑ RAGE on human metastatic melanoma a cell line associated with metastatic phenotype [54], Anti-RAGE antibodies [55], or DNA-AGE ap...…”

Non‐enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies

“…In general, nLC‐ESI or MALDI‐TOF MS/MS experiments have been used to definitively assign the modified lysines within the glycated proteins (Morgan et al, ; Lapolla et al, ; Zheng, Wu, & Hancock, ; Ahmad, Li, & Deng, ; Dai et al, ; Zhang et al, ; Corzo‐Martínez et al, ; Frolov & Hoffmann, ; Shao et al, ; Stefanowicz et al, ; Guedes et al, ; Miller et al, ; Bai et al, ; Korwar et al, ). However, CID experiments on glucosylated peptides revealed that sequence‐informative b and y ions resulting from the peptide backbone cleavage were reduced within MS/MS spectra, hampering sequence‐derived peptide identification.…”

Glycated proteome: From reaction to intervention

“…In our previous study, AGE modified proteins were identified from clinical breast cancer tissue, including serotransferrin, fibrinogen gamma chain, glycerol‐3‐phosphate dehydrogenase, lactate dehydrogenase, annexin II, prohibitin, and peroxiredoxin 6, all of which have an established role in cancer. Further, RAGE expression and its downstream signaling proteins NADPH oxidase and NF‐kB were also found to be upregulated in clinical breast cancer tissue .…”