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J Biol Chem, Vol. 275, Issue 20, 15490-15497, May 19, 2000
From the Tumor Immunology Programme, 0710, German Cancer Research
Center, D-69120 Heidelberg, Germany
The ectodomain of certain transmembrane molecules
can be released by proteolysis, and the solubilized antigens often
exert important biological functions. We demonstrated before that the L1 adhesion molecule is shed from the cell surface. Here we show that
L1 release in AR breast carcinoma cells is mediated by a member of the
disintegrin metalloproteinase (ADAM) family of proteinases. Up-regulation of L1 shedding by phorbol ester or pervanadate involved distinct mechanisms. Pervanadate induced shedding and rounding-up of
cells from the substrate, which was blocked by the Src kinase inhibitor
PP2. Tyr phosphorylation of the L1 cytoplasmic tail and the Src kinase
Fyn was observed following pervanadate treatment. Up-regulation of L1
release and activation of Fyn occurred also when cells were detached by
EDTA suggesting that the regulation of L1 shedding by this pathway was
linked to cell morphology and adhesion. The phorbol 12-myristate
13-acetate-induced shedding was inhibited by the protein kinase C
inhibitor bisindolylmaleimide I and by PD98059, a specific inhibitor of
the mitogen-activated protein kinase pathway. Soluble L1 binds to the
proteoglycan neurocan and in bound form could support integrin-mediated
cell adhesion and migration. We propose that the release of
cell-associated adhesion molecules such as L1 may be relevant to
promote cell migration.
Role of Src Kinases in the ADAM-mediated Release of L1 Adhesion
Molecule from Human Tumor Cells*
,
*
This work was supported by a grant from the German-Israeli
Cooperation in Cancer Research (to P. G. and P. A.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a grant from MINERVA-Stiftung.
§
To whom correspondence should be addressed: Tumor Immunology
Programme, G0100, German Cancer Research Center, Im Neuenheimer Feld
280, D-69120 Heidelberg, Germany. Tel.: 06221-423714; Fax: 06221-423702; E-mail: P.Altevogt@dkfz-heidelberg.de.
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