Abstract
BackgroundCarcinoembryonic antigen (CEA) is a glycoprotein associated with colorectal cancer (CRC). While the functions of its gene and protein have been fully characterized, its post-translational modifications in the context of CRC development remain undefined.MethodsTo show the correlation between the different stages of CRC development and changes in the glycosylation patterns of CEA, we analyzed CEA in tumor tissues (CEA-T) and paired tumor-adjacent normal tissues (CEA-A) from 53 colorectal cancer patients using a high-density lectin microarray containing 56 plant lectins.ResultsWe detected higher expression levels of fucose, mannose and Thomsen–Friedenreich antigen, and lower expression levels of N-acetylgalactosamine, N-acetylglucosamine, galactose, branched and bisecting N-glycans on CEA in the tumor tissues relative to the tumor-adjacent normal tissues. Furthermore, a combinatorial assessment of 9 lectins is sufficient to distinguish CRC tumor tissues from tumor-adjacent normal tissues with 83% sensitivity and ~ 90% specificity. Moreover, the levels of N-acetylgalactosamine, mannose, galactose, N-acetylglucosamine on CEA showed a downward trend after first experiencing an increase at Stage II with the stages of CRC.ConclusionsOur insights into the changing CEA glycosylation patterns and their role in the development of CRC highlight the importance of glycan variants on CEA for early clinical detection and staging of CRC.
Highlights
Carcinoembryonic antigen (CEA) is a glycoprotein associated with colorectal cancer (CRC)
In order to optimize conditions for our lectin microarray procedure, we evaluated its sensitivity using commercial standard Carcinoembryonic Antigen (CEA) purified from human liver metastases
As shown in Additional file 2, we showed that at the highest concentration of CEA (10 μg/ml), 31 lectins interacted with CEA
Summary
Carcinoembryonic antigen (CEA) is a glycoprotein associated with colorectal cancer (CRC). While the functions of its gene and protein have been fully characterized, its post-translational modifications in the context of CRC development remain undefined. Development of CRC occurs progressively, usually spanning 5–10 years. This extended timeframe provides ample opportunities for treatment, especially during the early stage (including the high-risk stage II) [3,4,5]. Current screening methods are Glycosylation is one of the major post-translational modifications found in proteins. It alters protein function and plays an important role in many different biological processes, including protein–protein interactions, cell– cell recognition, adhesion and migration [9,10,11].
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