The high molecular weight Cat-301 chondroitin sulfate proteoglycan from brain is related to the large aggregating proteoglycan from cartilage, aggrecan.
Open accessAbstract
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.
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The cat-301 antibody labels a distinct glycosylated form of the aggrecan core protein, whereas other glycosylated forms may be only partially recognized.
“This antibody labels a distinct glycosylated form of the aggrecan core protein, whereas other glycosylated forms may be only partially recognized.56, 75”
From Aggrecan and chondroitin-6-sulfate abnormalities in schizophrenia and bipolar disorder: a postmortem study on the amygdala (2015) · cites this paper as [75]
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- Authors
- Fryer, H. J., Kelly, G. M., Molinaro, L., & Hockfield, S.
- Affiliations
- Yale University (US)
- ORCID
- Fryer, H.J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-05
- Volume
- 267
- Issue
- 14
- Pages
- 9874-9883
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1579361735
- Cited by
- 92
- References
- 36
- Citations by year
- 2024: 2 · 2021: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2015: 2 · 2014: 1 · 2012: 5
- FWCI
- 5.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Eye Institute (EY 06511)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- chondroitin sulfate proteoglycans, aggrecan, brain, cartilage, hyaluronan binding, keratan sulfate, chondroitinase ABC, proteoglycan aggregation
- MeSH terms
- Animals, Epitopes, Brain Chemistry, Cartilage, Cats, Cattle, Centrifugation, Density Gradient, Chondroitinases and Chondroitin Lyases, Enzyme-Linked Immunosorbent Assay, Hyaluronic Acid, Immunohistochemistry, Molecular Weight, Organ Specificity, Chondroitin Sulfate Proteoglycans, Proteoglycans, Visual Cortex, Extracellular Matrix Proteins, Lectins, C-Type, Aggrecans
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