ArticleGland surgery2025
Serum immunoglobulin G glycosylation profiling in breast cancer using a 56-lectin microarray and subtype-specific patterns.
Article in Gland surgery, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: Protein glycosylation is the enzymatic addition of sugar chains to specific protein sites and part of this process has a crucial functional modification associated with carcinogenesis and cancer progression. This study aimed to profile and confirm aberrant immunoglobulin G (IgG) protein glycosylation in sera obtained from individuals with breast cancer (BC), with emphasis on breadth of lectin panel and subtype-specific patterns. Methods: A total of 185 sera underwent lectin microarray analysis with 56 lectins. Validation was performed on sera from an additional 20 BC patients and 6 healthy controls. Results: Differential binding intensities of IgG glycans to Agaricus bisporus lectins (ABA) and Salvia sclarea (SSA) were observed between BC patients and healthy controls (P<0.05). In hormone receptor-positive (HR Conclusions: By employing a broad 56-lectin microarray and subtype analysis, our results reveal distinct serum IgG glycosylation profiles associated with different BC molecular markers. These findings offer a novel framework for investigating disease pathogenesis and identifying candidate biomarkers for BC.
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