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Selectins

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,...

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Related Experiment Video

Updated: Mar 6, 2026

A Protocol for Immunohistochemistry and RNA In-situ Distribution within Early Drosophila Embryo

A Protocol for Immunohistochemistry and RNA In-situ Distribution within Early Drosophila Embryo

Published on: May 6, 2022

Lectin binding sites during Drosophila embryogenesis.

P Callaerts¹, V Vulsteke¹, A De Loof¹

¹Zoological Institute of the University, Naamsestraat 59, 3000, Leuven, Belgium.

Roux'S Archives of Developmental Biology : the Official Organ of the EDBO

|March 18, 2017

Summary

This summary is machine-generated.

This study maps lectin binding sites during Drosophila embryonic development, revealing complex patterns and specific markers for neural and ectodermal tissues. Differential glycosylation of Drosophila laminin is also highlighted.

Keywords:

Development Drosophila Embryogenesis Glycan structures Lectins

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Area of Science:

Developmental Biology
Glycobiology
Cell Biology

Background:

Lectin binding sites play crucial roles in cellular processes.
Understanding lectin distribution during embryonic development is key to deciphering morphogenesis.
Specific lectin interactions can serve as markers for distinct cell types and tissues.

Purpose of the Study:

To analyze the spectrum of lectin binding sites during Drosophila embryonic development.
To identify specific lectins that mark ectodermal derivatives, neural structures, and other cell types.
To investigate the differential glycosylation of Drosophila laminin and its implications.

Main Methods:

Utilized fluorescein-labeled lectins to map lectin binding sites.
Observed changes in lectin binding patterns as embryonic development and morphogenesis progressed.
Examined the specificity of various lectins, including those for mannose/glucose, mannose, N-acetylglucosamine, poly-N-acetylglucosamine, N-acetylgalactosamine, and Galβ-3-N-acetylgalactosamine.

Main Results:

Lectin binding patterns became increasingly complex during development.
Mannose/glucose-, mannose-, N-acetylglucosamine-, and poly-N-acetylglucosamine-specific lectins showed ubiquitous binding.
Wheat germ agglutinin specifically bound to nuclear envelopes; N-acetylgalactosamine-binding lectins marked ectodermal derivatives; Galβ-3-N-acetylgalactosamine-binding lectins were selective for neural structures, haemocytes, and Garland cells.
Drosophila laminin was found to be differentially glycosylated.

Conclusions:

Lectin binding patterns evolve significantly during Drosophila embryogenesis.
Specific lectins act as precise markers for germ layer derivatives and cellular structures.
Differential glycosylation of Drosophila laminin suggests complex regulatory mechanisms in development.