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(Received for publication, May 6, 1996, and in revised form, August 6, 1996)
From the Max-Planck-Institut für Biochemie, Am Klopferspitz
18a, 82152 Martinsried, Germany
Neurocan is a brain-specific chondroitin sulfate
proteoglycan, which has been shown to bind to the neural cell adhesion
molecule N-CAM and to inhibit its homophilic interaction. To
study in more detail the structures of neurocan responsible for this
interaction, various recombinant neurocan fragments were generated. The
ability of these fragments to interact with N-CAM was investigated in
several different in vitro assay systems, enzyme-linked
immunosorbent assay-type binding assays, Covasphere-aggregation assays,
and assays based on an optical biosensor (BIAcoreTM) system. The
analysis of the homophilic N-CAM interaction in the BIAcore system
revealed a KD of 64 nM. This homophilic
interaction could be reduced by preincubation of soluble N-CAM with
neurocan. Direct binding of N-CAM to immobilized neurocan core protein
and recombinant neurocan fragments could also be demonstrated, and
KD values between 25 and 100 nM were
obtained. In addition, direct binding of N-CAM to chondroitin sulfate
could be demonstrated.
Binding of N-CAM to the immobilized neurocan core protein could be
inhibited with all recombinant fragments containing chondroitin sulfate
or major parts of the mucin-like central region of neurocan. For the
inhibition of homophilic N-CAM interactions, however, a combination of
globular and extended structures was required.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27304-27310
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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