O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal Cancer
Background: Aberrant glycosylation is a hallmark of cancer and thereby has an excellent potential for the discovery of novel biomarkers. Impairments in the glycan composition of lipoproteins impact their functional properties and can be associated with various diseases, including cancer. This resear...
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| Format: | Article |
| Language: | English |
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IMR Press
2024-01-01
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| Series: | Frontiers in Bioscience-Landmark |
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| Online Access: | https://www.imrpress.com/journal/FBL/29/1/10.31083/j.fbl2901032 |
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| author | Kristína Kianičková Zuzana Pakanová Filip Květoň Alena Holazová Paras H. Kundalia Peter Baráth Goran Miljuš Olgica Nedić Jaroslav Katrlík |
| author_facet | Kristína Kianičková Zuzana Pakanová Filip Květoň Alena Holazová Paras H. Kundalia Peter Baráth Goran Miljuš Olgica Nedić Jaroslav Katrlík |
| author_sort | Kristína Kianičková |
| collection | DOAJ |
| description | Background: Aberrant glycosylation is a hallmark of cancer and thereby has an excellent potential for the discovery of novel biomarkers. Impairments in the glycan composition of lipoproteins impact their functional properties and can be associated with various diseases, including cancer. This research is still in its infancy; however, it can lead to the development of new diagnostic and disease stratification approaches as well as therapeutic strategies. Therefore, we aimed to evaluate anomalies in O-glycosylation of apolipoprotein C-III (apoC-III) in colorectal carcinoma (CRC) patients’ sera, in comparison with sera from healthy individuals, and assess the disparities of O-glycoforms on apoC-III in CRC. Methods: The choice of patients (n = 42) was based on the same tumor type (adenocarcinoma) and tumor size (T3), without or with inconsiderable lymph node infiltration. Patients with comorbidities were excluded from the study. The control healthy individuals (n = 40) were age- and sex-matched with patients. We used an approach based on the MALDI-TOF MS in linear positive ion mode, allowing simple analysis of O-glycosylation on intact apoC-III molecules in the serum samples directly, without the need for specific protein isolation. This approach enables relatively simple and high-throughput analysis. Results: In CRC patients’ sera samples, we observed significantly elevated apoC-III sialylation. Fully sialylated (disialylated) O-glycans had 1.26 times higher relative abundance in CRC samples compared to controls with a p-value of Mann–Whitney U test of 0.0021. Conclusions: We found altered O-glycosylation of apoC-III in the serum of CRC patients. However, it can be non-specific as it may be associated with another process such as ongoing inflammation. Therefore, to establish it as a potential novel non-invasive biomarker for CRC in suspected patients, further studies interrogating the changes in apoC-III O-glycosylation and the robustness of this biomarker need to be performed and evaluated. |
| first_indexed | 2024-03-08T09:36:26Z |
| format | Article |
| id | doaj.art-075d9a297a504b9498dc966328556e31 |
| institution | Directory Open Access Journal |
| issn | 2768-6701 |
| language | English |
| last_indexed | 2024-03-08T09:36:26Z |
| publishDate | 2024-01-01 |
| publisher | IMR Press |
| record_format | Article |
| series | Frontiers in Bioscience-Landmark |
| spelling | doaj.art-075d9a297a504b9498dc966328556e312024-01-30T07:44:34ZengIMR PressFrontiers in Bioscience-Landmark2768-67012024-01-012913210.31083/j.fbl2901032S2768-6701(23)01108-5O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal CancerKristína Kianičková0Zuzana Pakanová1Filip Květoň2Alena Holazová3Paras H. Kundalia4Peter Baráth5Goran Miljuš6Olgica Nedić7Jaroslav Katrlík8Institute of Chemistry, Slovak Academy of Sciences, 84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, 84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, 84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, 84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, 84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, 84538 Bratislava, SlovakiaInstitute for the Application of Nuclear Energy (INEP), University of Belgrade, 11080 Belgrade, SerbiaInstitute for the Application of Nuclear Energy (INEP), University of Belgrade, 11080 Belgrade, SerbiaInstitute of Chemistry, Slovak Academy of Sciences, 84538 Bratislava, SlovakiaBackground: Aberrant glycosylation is a hallmark of cancer and thereby has an excellent potential for the discovery of novel biomarkers. Impairments in the glycan composition of lipoproteins impact their functional properties and can be associated with various diseases, including cancer. This research is still in its infancy; however, it can lead to the development of new diagnostic and disease stratification approaches as well as therapeutic strategies. Therefore, we aimed to evaluate anomalies in O-glycosylation of apolipoprotein C-III (apoC-III) in colorectal carcinoma (CRC) patients’ sera, in comparison with sera from healthy individuals, and assess the disparities of O-glycoforms on apoC-III in CRC. Methods: The choice of patients (n = 42) was based on the same tumor type (adenocarcinoma) and tumor size (T3), without or with inconsiderable lymph node infiltration. Patients with comorbidities were excluded from the study. The control healthy individuals (n = 40) were age- and sex-matched with patients. We used an approach based on the MALDI-TOF MS in linear positive ion mode, allowing simple analysis of O-glycosylation on intact apoC-III molecules in the serum samples directly, without the need for specific protein isolation. This approach enables relatively simple and high-throughput analysis. Results: In CRC patients’ sera samples, we observed significantly elevated apoC-III sialylation. Fully sialylated (disialylated) O-glycans had 1.26 times higher relative abundance in CRC samples compared to controls with a p-value of Mann–Whitney U test of 0.0021. Conclusions: We found altered O-glycosylation of apoC-III in the serum of CRC patients. However, it can be non-specific as it may be associated with another process such as ongoing inflammation. Therefore, to establish it as a potential novel non-invasive biomarker for CRC in suspected patients, further studies interrogating the changes in apoC-III O-glycosylation and the robustness of this biomarker need to be performed and evaluated.https://www.imrpress.com/journal/FBL/29/1/10.31083/j.fbl2901032o-glycoprofilingapolipoprotein c-iiiglycosylationcolorectal cancerbiomarkermass spectrometry |
| spellingShingle | Kristína Kianičková Zuzana Pakanová Filip Květoň Alena Holazová Paras H. Kundalia Peter Baráth Goran Miljuš Olgica Nedić Jaroslav Katrlík O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal Cancer Frontiers in Bioscience-Landmark o-glycoprofiling apolipoprotein c-iii glycosylation colorectal cancer biomarker mass spectrometry |
| title | O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal Cancer |
| title_full | O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal Cancer |
| title_fullStr | O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal Cancer |
| title_full_unstemmed | O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal Cancer |
| title_short | O-glycoprofiling of Serum Apolipoprotein C-III in Colorectal Cancer |
| title_sort | o glycoprofiling of serum apolipoprotein c iii in colorectal cancer |
| topic | o-glycoprofiling apolipoprotein c-iii glycosylation colorectal cancer biomarker mass spectrometry |
| url | https://www.imrpress.com/journal/FBL/29/1/10.31083/j.fbl2901032 |
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