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GALECTIN-3 EXPRESSION IN DIFFERENTIATING HUMAN MYELOID CELLS

✍ Scribed by Nadia Le Marer

Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
439 KB
Volume
24
Category
Article
ISSN
1065-6995

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✦ Synopsis

Abstract

Galectin‐3 is an endogenous mammalian carbohydrate‐binding protein with affinity for ABH group carbohydrate epitopes and polylactosamine glycans present on cell surface and extracellular matrix glycoproteins. It has been shown to play a role in cell differentiation, morphogenesis, adhesion and cell proliferation regulation. Progenitor cell proliferation in bone marrow depends on stem cell factors including those modulating their adhesion to the bone marrow stroma. The present study shows that the 32kD galectin‐3 is developmentally expressed in human myeloid cells and is strongly upregulated on the cell surface of late mature myeloid cells. Despite the fact that the expression of the galectin‐3 is very low in CD34+ early myeloid cell, a 70kD protein is found by Western blotting using antibodies specific to galectin‐3, exclusively in those cells. Finally, exogenous human recombinant galectin‐3 binds strongly to CD34+ early myeloid cells and emphasizes granulocyte‐colony stimulating factor (G‐CSF) driven proliferation in vitro.

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