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Differential Lectin Binding in Giant Danio, Goldfish, and Zebrafish hearts
Author(s) -
Lafontant Pascal,
May Adam
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.552.8
Subject(s) - lectin , danio , zebrafish , biology , anatomy , microbiology and biotechnology , pathology , chemistry , biochemistry , medicine , gene
Lectins are carbohydrate‐binding proteins commonly used in the study of mammalian cells and tissues. However lectins have received little use in fish models. Here, we determine the binding patterns of three commonly used lectins: wheat germ agglutinin (WGA), Ulex europaeus agglutinin (UEA lectin), Bandeiraea simplicifolia lectin (BS lectin), in giant danio (GD), zebrafish (ZF), and goldfish (GF) hearts. Our results show that WGA stained cardiac myocyte borders of all three fish in patterns similar to that seen in mammalian hearts, with staining markedly stronger in the fish compact hearts. By contrast, UEA lectin, an endothelial cell marker in mammalian vascular beds, showed little to no binding to the coronary vasculature of these fish. Interestingly, BS lectin reacted poorly to the zebrafish coronary vasculature similar to our previously reported study in the goldfish. However BS lectin strongly stained coronary vessels of the Giant danio. Importantly, BS lectin biding was particularly strong in the vascular endothelium compared to endocardium of the Giant danio. This differential regional staining allowed for coronary angiography of the Giant danio heart and 3D reconstruction by confocal and light sheet fluorescence microscopy. In addition we were able to quantify coronary revascularization following cautery injury and during repair and regeneration of the Giant danio heart. Our results demonstrate that lectins differentially bind to coronary vasculature of fish and can be used as simple but powerful tools for the study of adult and regenerating fish hearts.