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On the existence of a cartilage‐like proteoglycan and link proteins in the central nervous system
Author(s) -
Asher Richard A.,
Scheibe Renate J.,
Keiser Harold D.,
Bignami Amico
Publication year - 1995
Publication title -
glia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.954
H-Index - 164
eISSN - 1098-1136
pISSN - 0894-1491
DOI - 10.1002/glia.440130406
Subject(s) - aggrecan , chondroitin sulfate proteoglycan , proteoglycan , cartilage , perineuronal net , biology , extracellular matrix , microbiology and biotechnology , versican , spinal cord , chondroitin , biochemistry , anatomy , pathology , glycosaminoglycan , neuroscience , osteoarthritis , medicine , alternative medicine , articular cartilage
Monoclonal antibodies (mAbs) against the major constituents of cartilage extracellular matrix, aggrecan and link protein, were screened by indirect immunofluorescence on frozen sections of bovine spinal cord. Antibodies against aggrecan and link protein gave rise to very similar perineuronal labeling in spinal cord gray matter. Aggrecan and link protein reactivities were seen in other regions of the central nervous system (CNS), although their distributions were not always coincident. Pretreatment of the tissue section with Streptomyces hyaluronidase, which is hyaluronate‐specific, led to the loss of both reactivities. On Western blots, anti‐aggrecan mAbs reacted with a large chondroitin sulfate proteoglycan. The chondroitinase‐treated CNS proteoglycan co‐migrated with the chondroitinase‐ and keratanase‐treated cartilage proteoglycan. In CNS tissue homogenates, the addition of Streptomyces hyaluronidase brought about the release of the proteoglycan from the tissue. Anti‐link protein mAbs were reactive with two species in the bovine CNS, the mobilities of which were very similar to those of the cartilage link proteins. The release of these species from the tissue required hyaluronidase. A rabbit antiserum against aggrecan was used to identify a similar proteoglycan in the rat CNS. In spinal cord‐derived cell cultures, the labeled material was associated with astrocytes. An aggrecan cDNA hybridized to a 9.5 kb mRNA in the rat CNS. We conclude that the perineuronal matrix consists, in part, of a hyaluronate‐bound aggrecan‐like proteoglycan and link proteins, and that the former is produced by astrocytes. © 1995 Wiley‐Liss, Inc.