Release of β-d-galactoside-binding lectins into the cavities of aggregates of chick extraembryonic endoderm cells

Milos, Nadine C.; Zalik, Sara E.

doi:10.1016/0045-6039(86)90029-1

Cited by 11 publications

(1 citation statement)

References 15 publications

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“…Although this phenomenon was attributed to developmental processes, the mechanism may also operate in adult myocardium. Externalization of endogenous lectins is not a process restricted to this type of cell (Barondes, 1984;Milos and Zalik, 1986). Indeed, the presence of negative fibrils together with abundant, positive sarcoplasmic granulation within the same cells; the gathering of positive fibrillary structures and granulations to form clusters; and their separation from negative fibrils were observed with a number of neoglycoproteins.…”

Section: Discussionmentioning

confidence: 99%

Spatial differences of endogenous lectin expression within the cellular organization of the human heart: A glycohistochemical, immunohistochemical, and glycobiochemical study

et al. 1990

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Protein-carbohydrate recognition may be involved in an array of molecular interactions on the cellular and subcellular levels. To gain insight into the role of proteins in this type of interaction, surgically removed specimens of human endomyocardial tissue were processed for histochemical and biochemical analysis. The inherent capacity of these sections to bind individual sugar moieties, which are constituents of the carbohydrate part of cellular glycoconjugates, was assessed using a panel of biotinylated neoglycoproteins according to a standardized procedure. Together with appropriate controls, it primarily allowed localization of endogenous lectins. Differences in lectin expression were observed between layers of endocardial tissue, myocardial cell constituents, connective-tissue elements, and vascular structures. The endocardium proved to be positive with beta-galactoside-bearing probes; with neoglycoproteins carrying beta-xylosides, alpha-fucosides, and galactose-6-phosphate moieties; and with probes containing a carboxyl group within the carbohydrate structure, namely sialic acid and glucuronic acid. In contrast, only fucose-and maltose-specific receptors were apparent in the elastic layers of the endocardium. Aside from ascertaining the specificity of the protein-carbohydrate interaction by controls, i.e., lack of binding of the probe in the presence of the unlabelled neoglycoprotein and lack of binding of the labelled sugar-free carrier protein, respective sugar receptors were isolated from heart extracts by using histochemically effective carbohydrates as immobilized affinity ligand. Moreover, affinity chromatography using immobilized lactose as affinity ligand as well as the use of polyclonal antibodies against the predominant beta-galactoside-specific lectin of heart demonstrated that the lactose-specific neoglycoprotein binding was due to this lectin. Remarkably, the labelled endogenous lectin, preferred to plant lectins for detecting ligands of the endogenous lectin, localized ligands in tissue parts where the lectin itself was detected glycohistochemically as well as immunohistologically. This demonstration of receptor-ligand presence in the same system is a further step toward functional assignment of the recorded protein-carbohydrate interaction. Overall, the observed patterns of lectin expression may serve as a guideline to elucidate the precise physiological relevance of lectins and to analyze pathological conditions comparatively.

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Section: Discussionmentioning

confidence: 99%

Spatial differences of endogenous lectin expression within the cellular organization of the human heart: A glycohistochemical, immunohistochemical, and glycobiochemical study

et al. 1990

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Differentiation-associated modulation of lactoside binding lectins in cancer cells

Lotan

1991

Lectins and Cancer

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On the possible role of endogenous lectins in early animal development

Zalik

1991

Anat Embryol

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In this review I have tried to summarize the information available on the lectins of developing embryos. The emerging evidence indicates that during fertilization carbohydrate-binding proteins play a role in sperm adhesion and in the reorganization of the extracellular matrix of the fertilized egg. Results also indicate that in adult tissues lectins participate in cell recognition and adhesion, and that several galactose-binding lectins function as receptors for laminin and, in principle could also interact with polylactosamine groups of other extracellular matrix glycoproteins. Since in developing embryos lectins are located at the cell surface, and colocalize with extracellular matrix glycoproteins, they could play a role in transitory adhesive interactions and in the segregation of organ primordia. On the basis of experiments in cultured cell lines, it has been suggested that lectins are involved in lysosomal and nuclear glycoprotein transport. These carbohydrate-binding proteins could also regulate development by modulating these processes in the embryo. Since galactose-binding lectins are mitogenic, and are present in high concentration in the chick yolk sac, these proteins could be released into the embryonic circulation, bind to cells expressing appropriate receptors, and act as growth regulators, by modulating cell division of specific cell lineages.

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Release of β-d-galactoside-binding lectins into the cavities of aggregates of chick extraembryonic endoderm cells

Cited by 11 publications

References 15 publications

Spatial differences of endogenous lectin expression within the cellular organization of the human heart: A glycohistochemical, immunohistochemical, and glycobiochemical study

Spatial differences of endogenous lectin expression within the cellular organization of the human heart: A glycohistochemical, immunohistochemical, and glycobiochemical study

Differentiation-associated modulation of lactoside binding lectins in cancer cells

On the possible role of endogenous lectins in early animal development

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