| First Author | Rostand KS | Year | 1986 |
| Journal | Arthritis Rheum | Volume | 29 |
| Issue | 1 | Pages | 95-105 |
| PubMed ID | 3947420 | Mgi Jnum | J:38357 |
| Mgi Id | MGI:85851 | Doi | 10.1002/art.1780290113 |
| Citation | Rostand KS, et al. (1986) Articular cartilage proteoglycans from normal and osteoarthritic mice. Arthritis Rheum 29(1):95-105 |
| abstractText | Articular cartilage proteoglycans from an osteoarthritic mouse strain, STR/IN, were labeled in vivo with 35S-sulfate and characterized with respect to extractability, ability to aggregate, size of monomer and glycosaminoglycan chains, sulfation of glycosaminoglycans, relative amounts of chondroitin-4 sulfate and chondroitin-6 sulfate, and link proteins. The proportion of 35S-labeled proteoglycans extractable by 0.4M guanidine hydrochloride was the same in control and osteoarthritic animals. However, a greater proportion was extractable by 4M guanidine hydrochloride in the STR/IN animals as compared with the control mice. The ability of the 35S-proteoglycans to aggregate was comparable in controls and osteoarthritic mice, as judged by their exclusion on Sepharose CL-2B. Monomers from both controls and osteoarthritic animals eluted from Sepharose CL-2B with a KAV of 0.47. Glycosaminoglycans from control and osteoarthritic animals eluted from Sepharose CL-6B with a KAV of 0.63, and no differences in sulfation or chondroitin-4 sulfate content were found. Aggregates were immunoprecipitated with link protein-specific antiserum, and only link protein 2 was found in aggregates from control and osteoarthritic animals. |
