Glycobiology, Vol 9, 101-114, Copyright © 1999 by Oxford University Press
R Probstmeier and P Pesheva
We have previously shown that the extracellular matrix molecule tenascin-C
inhibits fibronectin-mediated cell adhesion and neurite outgrowth by an
interaction with a cellular RGD-independent receptor which interferes with
the adhesion and neurite outgrowth promoting activities of the fibronectin
receptor(s). Here we demonstrate that the inhibitory effect of tenascin-C
on beta1integrin-dependent cell adhesion and neurite outgrowth is mediated
by the interaction of the protein with membrane-associated
disialogangliosides, which interferes with protein kinase C-related
signaling pathways. First, in substratum mixtures with fibronectin, an RGD
sequence-containing fragment of the molecule or synthetic peptide,
tenascin-C inhibited cell adhesion and spreading by a
disialoganglioside-dependent, sialidase-sensitive mechanism leading to an
inhibition of protein kinase C. Second, the interaction of intact or
trypsinized, i.e., cell surface glycoprotein- free, cells with immobilized
tenascin-C was strongly inhibited by gangliosides or antibodies to
gangliosides and tenascin-C. Third, preincubation of immobilized tenascin-C
with soluble disialogangliosides resulted in a delayed cell detachment as a
function of time. Similar to tenascin-C, immobilized antibody to GD2 (3F8)
or sphingosine, a protein kinase C inhibitor, strongly inhibited RGD-
dependent cell spreading. Finally, the degree of tenascin-C-induced
inhibition of cell adhesion was proportional to the degree of
disialoganglioside levels of expression by different cells suggesting the
relevance of such mechanism in modulating integrin-mediated cell- matrix
interactions during pattern formation or tumor progression.
ORIGINAL ARTICLES
Tenascin-C inhibits beta1 integrin-dependent cell adhesion and neurite outgrowth on fibronectin by a disialoganglioside-mediated signaling mechanism
Department of Physiology, Neurophysiology, and Department of Biochemistry, Institute of Animal Anatomy and Physiology, University of Bonn, Bonn, Germany.
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