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Related Concept Videos

Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or quantified.
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.

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Related Experiment Video

Updated: Jun 26, 2026

Screening Assays to Characterize Novel Endothelial Regulators Involved in the Inflammatory Response
12:50

Screening Assays to Characterize Novel Endothelial Regulators Involved in the Inflammatory Response

Published on: September 15, 2017

Lectin binding by eosinophils.

S H Pincus

    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
    |July 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Guinea pig eosinophils have specific lectin binding sites on their surface, identified using wheat germ agglutinin and concanavalin A. These interactions may be crucial for eosinophil engagement with parasites.

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    Published on: May 10, 2024

    Area of Science:

    • Immunology
    • Cell Biology
    • Parasitology

    Background:

    • Lectins are proteins that bind carbohydrates and glycoproteins.
    • Eosinophils play a role in immune responses, particularly against parasites.
    • Characterizing cell surface components is vital for understanding cell function.

    Purpose of the Study:

    • To identify and characterize lectin binding sites on guinea pig eosinophils.
    • To investigate the role of surface carbohydrates, specifically sialic acid, in eosinophil interactions.
    • To explore the potential involvement of lectin-mediated binding in eosinophil-parasite interactions.

    Main Methods:

    • Purification of guinea pig peritoneal exudate eosinophils using discontinuous metrizamide gradients.
    • Microscopic scoring of eosinophil agglutination in response to various lectins (Wheat Germ Agglutinin, Soybean Lectin, Concanavalin A).
    • Assessment of eosinophil adherence to lectin-coated Sepharose beads and plastic surfaces, with and without neuraminidase pretreatment.

    Main Results:

    • Wheat germ agglutinin (WGA) was the most potent agglutinin for eosinophils.
    • Eosinophils exhibited differential binding and adherence to lectins; they adhered to Con A-coated beads but not WGA-coated beads.
    • Neuraminidase pretreatment reduced WGA-mediated agglutination but did not affect adherence to plastic surfaces, indicating sialic acid's limited role in general adherence.
    • No significant differences in lectin binding were observed between eosinophils from infected and uninfected animals.

    Conclusions:

    • Guinea pig eosinophils possess specific lectin binding sites on their surface.
    • Lectin-type binding mechanisms may be important for eosinophil interactions with non-ingestible parasites.
    • Sialic acid appears to play a role in WGA binding but not in general eosinophil adherence to surfaces.