Journal
MOLECULES
Volume 23, Issue 6, Pages -Publisher
MDPI
DOI: 10.3390/molecules23061314
Keywords
adenocarcinoma; antigen-antibody reaction; automated latex-agglutination immunoassay; carcinoembryonic antigen; cerebrospinal fluid; immunohistochemistry; enzyme-linked immunosorbent assay; Psathyrella velutina lectin; Sambucus sieboldiana agglutinin; transferrin; sialyl alpha 2,6galactose
Funding
- Japan Agency for Medical Research and Development (AMED) [16hm0102042h0001, 17hm0102042h0002]
- Japan Science and Technology Agency [AS221Z00232F, AS231Z01053, 241FT0255, ad 149]
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [23110002, 23590367]
- Fukushima Medical University
- General Insurance Association of Japan
- Grants-in-Aid for Scientific Research [23590367] Funding Source: KAKEN
Ask authors/readers for more resources
Antibodies are useful for detecting glycoprotein antigens, but a conventional antibody recognizes only a protein epitope rather than a glycan. Thus, glycan isoform detection generally requires time-and labor-consuming processes such as lectin affinity column chromatography followed by sandwich ELISA. We recently found antigen-antibody reactions that were inhibited by lectin binding to glycans on the glycoprotein antigen, leading to a convenient glycoform-specific assay. Indeed, Sambucus sieboldiana agglutinin (SSA) lectin, a binder to sialyl alpha 2,6galactose residue, inhibited antibody binding to alpha 2,6-sialylated transferrin (Tf) (SSA inhibition). SSA inhibition was not observed with other glycoforms, such as periodate-treated, sialidase-treated and sialidase/galactosidase-treated Tf, suggesting that the assay was glycoform-specific. SSA inhibition was also applicable for visualizing localization of alpha 2,6-sialylated-Tf in a liver section. This is the first immunohistochemical demonstration of glycoform localization in a tissue section. SSA inhibition was utilized for establishing ELISA to quantify alpha 2,6-sialylated carcinoembryonic antigen (CEA), a marker for various cancers. In addition, alpha 2,6-sialylated-CEA was visualized in a colonic adenocarcinoma section by SSA inhibition. The method would further be applicable to a simple and rapid estimation of other alpha 2,6-sialylated glycoproteins and have a potential aid to histopathological diagnosis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available