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(Received for publication, May 22, 1995; and in revised form, August 21, 1995) Monoclonal antibodies were raised to membrane-bound
proteoglycans derived from rat brain, and four monoclonal antibodies
that recognized a 150-kDa chondroitin sulfate proteoglycan with a core
glycoprotein of 120 kDa were obtained. Immunohistological study
revealed that the proteoglycan was associated with developing neurons.
We screened rat brain cDNA libraries using the four monoclonal
antibodies and isolated overlapping cDNA clones that encoded the entire
core protein of 514 amino acids plus a 30-residue signal peptide. The
deduced amino acid sequence suggested an integral membrane protein
divided into five structurally different domains: an N-terminal domain
to which chondroitin sulfate chains might be attached, a basic amino
acid cluster consisting of seven arginine and two lysine residues, a
cysteine-containing domain, a membrane-spanning segment, and a
C-terminal cytoplasmic domain of 95 amino acids. On Northern blots, the
cDNA hybridized with a single mRNA of 3.1 kilobases that was detectable
in brains of neonatal and adult rats but not in kidney, liver, lung,
and muscle of either. The sequence of the proteoglycan did not exhibit
significant homology to any other known protein, indicating that the
proteoglycan, designated neuroglycan C, is a novel integral membrane
proteoglycan.
Volume 270,
Number 45,
Issue of November 10, 1995 pp. 26876-26882
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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