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Institut National de la Santé et de la Recherche Médicale (INSERM) CJF 94-03, and INSERM Unité 311, Etablissement de Transfusion Sanguine de Strasbourg, and
Service d’Onco-Hématologie, Hôpital de Hautepierre, Strasbourg, France
The regulation and function of the CD44 family of surface
glycoproteins were investigated in human monocyte-derived dendritic
cells (DCs). Variant CD44 isoform transcripts encoding exons v3, v6,
and v9 are differently regulated during the differentiation of
monocytes into DCs. TNF-
treatment, which induces the maturation of
DCs, up-regulates the expression of all v3-, v6-, and v9-containing
isoforms examined. CD44 molecules are involved in the adhesion of DCs
to immobilized hyaluronate (HA), and v3- and v6-containing variants
participate in this function, whereas anti-CD44v9 mAbs were unable
to inhibit DC adhesion to HA. The consequences of ligand binding to
CD44 were examined by culturing DCs on dishes coated with HA or various
anti-CD44 mAbs. HA, the anti-pan CD44 mAb J173, and mAbs
directed against v6- and v9-containing (but not v3-containing) isoforms
provoked DC aggregation, phenotypic and functional maturation, and the
secretion of IL-8, TNF-, IL-1ß, and granulocyte-macrophage CSF. In
addition, IL-6, IL-10, and IL-12 were released by DCs stimulated with
either J173 or HA, although these cytokines were not detected or were
found only at low levels in the culture supernatants of DCs treated
with anti-CD44v6 or anti-CD44v9 mAbs. Our study points to
distinct capacities of the v3-, v6-, and v9-containing isoforms
expressed by human DCs to mediate cell adhesion to HA and/or a signal
inducing DC maturation and the secretion of
cytokines.
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