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PMID: 1374409 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

The high molecular weight Cat-301 chondroitin sulfate proteoglycan from brain is related to the large aggregating proteoglycan from cartilage, aggrecan.

The Journal of biological chemistry ·Vol. 267 ·No. 14 ·1992-05-15 ·Pages 9874-83

Fryer HJ, Kelly GM, Molinaro L, Hockfield S

Abstract

Monoclonal antibodies Cat-301 and Cat-304 recognize a neuronal cell surface-associated chondroitin sulfate proteoglycan (CSPG), which is expressed during critical periods of postnatal development in the mammalian central nervous system (CNS). In the present study we show that the CNS CSPG identified by Cat-301/304 is similar to aggrecan, the high molecular weight CSPG from cartilage. By Western blot analysis, cartilaginous tissues, which are rich sources of aggrecan, have a high concentration of a high molecular weight CSPG which is immunoreactive with Cat-301 and 304. The Cat-301 and 304 epitopes, however, are partially masked by chondroitin sulfate glycosamino-glycan and are unmasked by digestion of the antigen with chondroitinase ABC. Although the antigen from both cartilage and CNS can be purified by CsCl buoyant density gradient centrifugation, a standard technique for purifying aggrecan, most of the antigen from the CNS has a lower buoyant density than that of cartilage. This may be due, in part, to the paucity of keratan sulfate substitution on the CNS antigen compared with that of the cartilage antigen. Both the CNS and cartilage antigens bind to hyaluronic acid, a feature characteristic of aggrecan. The physiochemical, biochemical, and functional properties of the Cat-301/304 antigen from cartilage are identical to aggrecan. The CNS antigen is similar, but not identical, to the cartilage antigen, and may thus represent another member of the family of high molecular weight CSPGs which bind to and aggregate with hyaluronic acid.

MeSH Terms
Aggrecans Animals Brain Chemistry Cartilage/chemistry Cats Cattle Centrifugation, Density Gradient Chondroitin Sulfate Proteoglycans/chemistry,isolation & purification,metabolism Chondroitinases and Chondroitin Lyases Enzyme-Linked Immunosorbent Assay Epitopes/analysis Extracellular Matrix Proteins Hyaluronic Acid/metabolism Immunohistochemistry Lectins, C-Type Molecular Weight Organ Specificity Proteoglycans/chemistry,isolation & purification Visual Cortex/cytology
Chemicals
Aggrecans Chondroitin Sulfate Proteoglycans Epitopes Extracellular Matrix Proteins Lectins, C-Type Proteoglycans Hyaluronic Acid Chondroitinases and Chondroitin Lyases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Fryer H J
Section of Neurobiology, Yale University School of Medicine, New Haven, Connecticut 06510.
Kelly G M
Molinaro L
Hockfield S
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1992-05-15
Pages
9874-83
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NEI NIH HHS · EY06511 · United States
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