Identification of diagnostic upper gastrointestinal cancer tissue type‑specific urinary biomarkers

Husi, Holger; Fernandes, Marco; Skipworth, Richard J E; Miller, James; Cronshaw, Andrew D.; Fearon, Kenneth C. H.; Ross, James A.

doi:10.3892/br.2019.1190

Cited by 9 publications

(8 citation statements)

References 61 publications

(59 reference statements)

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“…45 TPI1 (triosephosphate isomerase 1) catalyzes the isomerization of glyceraldehydes 3-phosphate (G3P) and dihydroxy-acetone phosphate (DHAP) in glycolysis and gluconeogenesis. As well, it contributes largely to tumorigenesis, as documented in lung cancer, 46 gastrointestinal cancer, 47 and colon cancer. 48 We here proposed a ceRNA network constructed mainly by circ-AMOTL1/miR-22-3p/miR-1294/ENO1.…”

Section: Discussionmentioning

confidence: 99%

<p>The circ-AMOTL1/ENO1 Axis Implicated in the Tumorigenesis of OLP-Associated Oral Squamous Cell Carcinoma</p>

Liu¹,

Yang²,

Sun³

et al. 2020

CMAR

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Background: Oral squamous cell carcinoma (OSCC) may develop from a variety of oral potentially malignant disorders, but the mechanism of malignant transformation is still unknown. Among them, oral lichen planus (OLP) has a high prevalence. Previous studies have shown that α-enolase (ENO1) can promote cell proliferation and play an important role in tumorigenesis. In this study, we aim to explore the mechanism of ENO1 regulation in the process of OSCC tumorigenesis from OLP. Methods: ENO1 expression in tissues was determined by real-time quantitative PCR and immunohistochemistry. ENO1 was knocked down in cal-27 to observe the change in cell proliferation. Then, RNA-seq and bioinformatics analyses were conducted between OLP and OSCC samples. The expression of circ-AMOTL1, miRNA-22-3p, and miRNA-1294 was assessed using the real-time quantitative PCR. With knockdown and overexpression of circ-AMOTL1 in vitro, the change of ENO1 in the mRNA level was also assessed. Results: ENO1 was enhanced in the OSCC samples in comparison with OLP. Immunohistochemistry and real-time quantitative PCR results showed that ENO1 was significantly higher in OSCC tissue than in the OLP group, with a statistically significant difference (p<0.05). When ENO1 was knocked down in cal-27, cell proliferation was inhibited (p<0.05). The expression of miR-22-3p and miR-1294 was decreased in OSCC tissues, whereas ENO1 and circ-AMOTL1 increased. In an in vitro study, knockdown of circ-AMOTL1 resulted in a decrease of ENO1, while overexpression of circ-AMOTL1 led to an increase of ENO1 in the mRNA level. Conclusion: We confirmed that ENO1 expression was elevated in OSCC and increased cell proliferation. In an in vitro study, ENO1 expression was promoted by circ-AMOTL1. ENO1 may play a role as a tumor-promoting gene in OSCC through the circ-AMOTL1/miR-22-3p/ miR-1294 network. These novel findings may shed further light on the pathogenesis from OLP to OSCC and the potential precursor markers.

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Section: Discussionmentioning

confidence: 99%

<p>The circ-AMOTL1/ENO1 Axis Implicated in the Tumorigenesis of OLP-Associated Oral Squamous Cell Carcinoma</p>

Liu¹,

Yang²,

Sun³

et al. 2020

CMAR

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“…Rabenosyn-5-like protein also binds phospholipid vesicles and plays roles in regulating protein sorting and recycling to the plasma membrane (Nielsen et al, 2000;de Renzis et al, 2002;Naslavsky et al, 2004). Rabenosyn-5 was recently identified as an upregulated urinary biomarker associated with malignant upper gastrointestinal cancer (Husi et al, 2019) and found to be increased in diabetic kidney disease (Dumont et al, 2017). Rabenosyn-5 has been shown to be phosphorylated, regulating its recruitment to membranes (Macé et al, 2005).…”

mentioning

confidence: 99%

Deiminated proteins in extracellular vesicles and serum of llama (Lama glama)—Novel insights into camelid immunity

Criscitiello

Kraev

Lange

2020

Molecular Immunology

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A B S T R A C TPeptidylarginine deiminases (PADs) are phylogenetically conserved calcium-dependent enzymes which posttranslationally convert arginine into citrulline in target proteins in an irreversible manner, causing functional and structural changes in target proteins. Protein deimination causes generation of neo-epitopes, affects gene regulation and also allows for protein moonlighting. Furthermore, PADs have been found to be a phylogenetically conserved regulator for extracellular vesicle (EVs) release. EVs are found in most body fluids and participate in cellular communication via transfer of cargo proteins and genetic material. In this study, post-translationally deiminated proteins in serum and serum-EVs are described for the first time in camelids, using the llama (Lama glama L. 1758) as a model animal. We report a poly-dispersed population of llama serum EVs, positive for phylogenetically conserved EV-specific markers and characterised by TEM. In serum, 103 deiminated proteins were overall identified, including key immune and metabolic mediators including complement components, immunoglobulin-based nanobodies, adiponectin and heat shock proteins. In serum, 60 deiminated proteins were identified that were not in EVs, and 25 deiminated proteins were found to be unique to EVs, with 43 shared deiminated protein hits between both serum and EVs. Deiminated histone H3, a marker of neutrophil extracellular trap formation, was also detected in llama serum. PAD homologues were identified in llama serum by Western blotting, via cross reaction with human PAD antibodies, and detected at an expected 70 kDa size. This is the first report of deiminated proteins in serum and EVs of a camelid species, highlighting a hitherto unrecognized post-translational modification in key immune and metabolic proteins in camelids, which may be translatable to and inform a range of human metabolic and inflammatory pathologies.

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“…Husi et al. observed a potential association between CO4 A and esophageal cancer [52]. Bertuzzi et al.…”

Section: Discussionmentioning

confidence: 99%

Exploration of quantitative site‐specific serum O‐glycoproteomics with isobaric labeling for the discovery of putative O‐glycoprotein biomarkers

Zhang

Tian

2022

Proteomics Clinical Apps

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Purpose Exploration study of site‐specific isobaric‐TMT‐labeling quantitative serum O‐glycoproteomics for the discovery of putative O‐glycoprotein cancer biomarkers. Experimental design Sera of 10 breast cancer patients was used as the exploration cohort. More abundant N‐glycosylation was first removed with PNGase F. After tryptic digestion of de‐N‐glycosylated serum proteome, the TMT‐labeled O‐glycopeptides mixture was prepared and analyzed with RPLC‐MS/MS. Site‐specific qualitative and quantitative database search of O‐glycopeptides was carried out with pGlyco 3.0. The same raw datasets were also searched with intact N‐glycopeptide search engine GPSeeker to exclude possible interference of N‐glycosylation. The final IDs were checked manually with GlcNAc‐containing glycosite‐determining fragment ions for confirmation. Results With the control of spectrum‐level FDR ≤ 1% and manual validation, 299 O‐glycopeptides corresponding to 83 O‐glycosites and 66 O‐glycoproteins were identified, and 13 O‐glycopeptides were found differentially expressed. Most interestingly, differential O‐glycosylation was observed for IgG1 and IgG3, which is an interesting putative biomarker panel. Conclusion and clinical relevance Isobaric‐labeling site‐specific quantitative O‐glycoproteomics is currently a state‐of‐the‐art instrumental platform for discovery of putative seral cancer biomarkers. Differential seral O‐glycosylation was observed in the IgG1 and IgG3.

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Identification of diagnostic upper gastrointestinal cancer tissue type‑specific urinary biomarkers

Cited by 9 publications

References 61 publications

<p>The circ-AMOTL1/ENO1 Axis Implicated in the Tumorigenesis of OLP-Associated Oral Squamous Cell Carcinoma</p>

<p>The circ-AMOTL1/ENO1 Axis Implicated in the Tumorigenesis of OLP-Associated Oral Squamous Cell Carcinoma</p>

Deiminated proteins in extracellular vesicles and serum of llama (Lama glama)—Novel insights into camelid immunity

Exploration of quantitative site‐specific serum O‐glycoproteomics with isobaric labeling for the discovery of putative O‐glycoprotein biomarkers

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