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J Biol Chem, Vol. 274, Issue 35, 25004-25017, August 27, 1999
From the Departments of A monoclonal antibody was used in early studies
to identify a novel chondroitin sulfate proteoglycan, secreted by
L-2 cells, the core protein of which was approximately 100 kDa.
To characterize this proteoglycan core protein at the molecular level,
an L-2 cell cDNA library was probed by expression screening and
solution hybridization. Northern blot analysis assigned transcript size to approximately 3.1 kilobases and, after contig assembly, the coding
region of the mRNA corresponded to 2.18 kilobases. Immunoassays were performed to confirm the identity of this sequence, using a
polyclonal antibody raised against an expressed fusion protein encoded
by sequence representing the carboxyl half of the molecule. The
antibody recognized the core protein in Western blots after prior
digestion of the intact proteoglycan with chondroitinase ABC.
Immunostaining tissue sections with the same antibody localized the
proteoglycan to basement membranes, and expression of the entire
sequence in Chinese hamster ovary K-1 cells showed that the protein
encoded by the sequence secreted as a chondroitin sulfate proteoglycan.
The core protein not only has motifs permitting glycosylation as a
proteoglycan, but also possesses the endoplasmic reticulum retrieval
signal, KDEL, which suggests that, in addition to its role as a
basement membrane component, it may also participate in the secretory
pathway of cells.
Molecular Characterization of a Novel Basement
Membrane-associated Proteoglycan, Leprecan
and§
Pathology and
§ Cell Biology and Anatomy, School of Medicine, Louisiana
State University Medical Center, Shreveport, Louisiana 71130
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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