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Vol. 11, Issue 4, 1457-1469, April 2000
v
3 Integrin through an
RGD-independent Mechanism
and
Departamentos de *Bioquímica y Biología Molecular
and ADAM 23 (a disintegrin and metalloproteinase domain)/MDC3
(metalloprotease, disintegrin, and cysteine-rich domain) is a
member of the disintegrin family of proteins expressed in fetal
and adult brain. In this work we show that the disintegrin-like
domain of ADAM 23 produced in Escherichia coli and
immobilized on culture dishes promotes attachment of different human
cells of neural origin, such as neuroblastoma cells (NB100 and
SH-Sy5y) or astrocytoma cells (U373 and U87
MG). Analysis of ADAM 23 binding to integrins revealed a
specific interaction with Morfología y Biología Celular,
Instituto Universitario de Oncología, Facultad de Medicina,
Universidad de Oviedo, 33006 Oviedo, Spain; and
Department of Vascular Biology, The Scripps Research
Institute, La Jolla, California 92037
v
3, mediated by a short amino acid
sequence present in its putative disintegrin loop. This
sequence lacks any RGD motif, which is a common structural determinant
supporting v3-mediated interactions of diverse proteins, including other disintegrins. v3 also supported adhesion
of HeLa cells transfected with a full-length cDNA for ADAM 23, extending the results obtained with the recombinant protein containing
the disintegrin domain of ADAM 23. On the basis of these
results, we propose that ADAM 23, through its disintegrin-like
domain, may function as an adhesion molecule involved in
v3-mediated cell interactions occurring in normal and
pathological processes, including progression of malignant tumors from
neural origin.
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