ArticleThe Histochemical journal2000
Cepaea hortensis agglutinin-I, specific for O-glycosidically linked sialic acids, selectively labels endothelial cells of distinct vascular beds.
Article in The Histochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Endothelial metabolism in pulmonary vascular homeostasis and acute respiratory distress syndrome.American journal of physiology. Lung cellular and molecular physiology · 2021Review
- NEU1 sialidase regulates the sialylation state of CD31 and disrupts CD31-driven capillary-like tube formation in human lung microvascular endothelia.The Journal of biological chemistry · 2014Article
- Characterization of lectins and their specificity in carcinomas-An appraisal.Indian journal of clinical biochemistry : IJCB · 2003Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lectin Cepaea hortensis agglutinin-I (CHA-I) binds to O-glycosidically linked sialic acids with previously characterized specificity. Employing histochemistry, we demonstrate that CHA-I is a useful probe for detecting sialic acids in formalin-fixed human tissues in a specific manner. It stains the endothelium of arteries and veins in all tissues examined, and labels the capillaries in distinct vascular beds including the brain, colon, thyroid, pituitary, and adrenal. By contrast, the endothelial sinusoids in the liver, spleen, and bone marrow remained unstained. The staining pattern of CHA-I overlaps with the distribution of the sialomucin and L-selectin ligand podocalyxin, which includes positivity of podocytes and interstitial but not glomerular capillaries. CHA-I-positive epithelial structures were found in the lung, liver and kidney. Colon carcinoma cells were labelled with CHA-I but not haemangiosarcomas. In summary, CHA-I is a useful tool for detecting O-glycosidically linked sialic acids in formalin-fixed tissues, and a potentially powerful tool for the isolation and characterization of unknown sialomucins in normal and eventually in diseased tissues.
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