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Journal ArticleDOI

The Sialoadhesins — A family of sialic acid-dependent cellular recognition molecules within the immunoglobulin superfamily

TLDR
In this review, the properties, carbohydrate specificities and potential biological functions of the Sialoadhesin family of sialic acid-dependent adhesion molecules, associated with diverse biological processes, are reviewed.
Abstract
For many years evidence has accumulated that sialic acids function in cellular interactions either by masking or as a recognition site. However, receptors or adhesion molecules mediating such functions between eukaryotic cells were unknown until about 5 years ago, when it was found that the members of the Selectin family mediate adhesion of leukocytes to specific endothelia through binding to sialylated glycans like sialyl Lewis. More recently, the Sialoadhesin family of sialic acid-dependent adhesion molecules was defined within the superfamily of immunoglobulin-like molecules. So far, it has been shown that sialoadhesin (Sn), CD22, CD33, the myelin-associated glycoprotein (MAG) and the Schwann cell myelin protein (SMP) belong to this family. In contrast to the Selectins, these proteins are associated with diverse biological processes, i.e. hemopoiesis, neuronal development and immunity. In this review their properties, carbohydrate specificities and potential biological functions are discussed. Finally, we provide perspectives with respect to the nature of ligands, implications of sialic acid modifications and future research.

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Journal ArticleDOI

Biological Roles of Glycans

TL;DR: It is time for the diverse functional roles of glycans to be fully incorporated into the mainstream of biological sciences, as they are no different from other major macromolecular building blocks of life, simply more rapidly evolving and complex.
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The new human tissue kallikrein gene family: structure, function, and association to disease.

TL;DR: The recently accumulated knowledge on the human tissue kallikrein gene family is summarized, including gene and protein structure, predicted enzymatic activities, tissue expression, hormonal regulation, and alternative splicing.
Journal ArticleDOI

Sialic acids as ligands in recognition phenomena.

TL;DR: This work presents a summary of the various proteins that can recognize and bind to this family of monosaccharides, comparing and contrasting the structural requirements and mechanisms involved in binding.
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Siglecs--the major subfamily of I-type lectins.

TL;DR: Siglecs as mentioned in this paper is a family of I-type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features, which appear to have evolved by convergent evolution.
References
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Journal ArticleDOI

Biological roles of oligosaccharides: all of the theories are correct

TL;DR: The only common features of the varied functions of oligosaccharides are that they either mediate ‘specific recognition’ events or that they provide ‘modulation’ of biological processes.
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The Immunoglobulin Superfamily—Domains for Cell Surface Recognition

TL;DR: The domain hypothesis was firmly established when the structures of V and C domains were determined to reveal a common fold forming a sandwich of two p-sheets that was stabilized by the conserved disulfide bond.
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Two distinct classes of carbohydrate-recognition domains in animal lectins.

TL;DR: Describing de 2 categories de lectines animales: les lectines de type C, calcium-dependantes et les lectine de type S, thiol-dependante.
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Identification of myelin-associated glycoprotein as a major myelin-derived inhibitor of neurite growth.

TL;DR: It is established that MAG is a significant, and possibly the major, inhibitor in CNS myelin; this has broad implications for axonal regeneration in the injured mammalian CNS.
Journal ArticleDOI

A novel role for myelin-associated glycoprotein as an inhibitor of axonal regeneration

TL;DR: It is demonstrated that the myelin-associated glycoprotein (MAG), a transmembrane protein of both CNS and PNS myelin, strongly inhibits neurite outgrowth from both developing cerebellar and adult dorsal root ganglion (DRG) neurons in vitro and is reversed by an anti-MAG antibody.
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