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- Shen, Z, et al.
(författare)
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Chondroadherin expression changes in skeletal development
- 1998
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Ingår i: The Biochemical journal. - 0264-6021. ; 330, s. 549-557
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Tidskriftsartikel (refereegranskat)abstract
- Chondroadherin is a cartilage protein with cell binding properties. The expression of chondroadherin was studied in rat tissues and during postnatal femoral head development. For design of oligonucleotide probes and primers a 1664 bp, full length, rat chondroadherin cDNA was isolated from a rat chondrosarcoma library and sequenced. Northern blot analysis showed chondroadherin mRNA to be present in femoral head and rib cartilage, as well as in tendon. More sensitive reverse-transcriptase PCR additionally identified the mRNA in calvaria, long bone and bone marrow. Localization of chondroadherin by immunocytochemistry in the developing femoral head from postnatal day 14 to day 60 showed presence of the protein in cartilaginous regions. With increasing age a very distinct localization of chondroadherin was seen in the territorial matrix around late proliferative cells in the growth plate as well as in the developing articular cartilage in the maturing femoral head. Localization of chondroadherin mRNA by in situ hybridization was in agreement with immunocytochemistry with strong hybridization signals in late proliferative cells in the growth plate. In the articular cartilage the expression was restricted to cells in the lower regions. A three-fold increase of cartilage chondroadherin content in the growing femoral head was demonstrated by Western blot analysis. The high expression of this cell binding protein in a dynamic region of cartilage suggests an important role for chondroadherin in the regulation of chondrocyte growth and proliferation.
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| 5. |
- Lohmander, Stefan, et al.
(författare)
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Transient synovitis of the hip in the child : Increased levels of proteoglycan fragments in joint fluid
- 1988
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Ingår i: Journal of Orthopaedic Research. - 0736-0266. ; 6:3, s. 420-424
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Tidskriftsartikel (refereegranskat)abstract
- The levels of proteoglycan antigen were measured in joint aspirates from the hip of children with transient synovitis, septic arthritis, Legg-Calve-Perthes' disease and congenital and traumatic dislocation. Significantly increased levels were found in children with transient synovitis and septic arthritis as compared with other conditions. We propose that the proteoglycan antigens in the joint fluid were released form the articular cartilage in a partially degraded from as a result of an increased rate of proteolytic degradation. In transient synovitis, the source of proteolytic activity may be chondrocytes activated by factors released by synovial cells. The release of joint proteoglycan may cause a temporary increase in deformability of the hip cartilage of the child that could be an important pathogenetic mechanism in some of the sequelae of these diseases.
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| 6. |
- Thyberg, J., et al.
(författare)
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Proteoglycans of hyaline cartilage. Electron microscopic studies on isolated molecules
- 1975
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Ingår i: Biochemical Journal. - 0264-6021. ; 151:1, s. 157-166
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Tidskriftsartikel (refereegranskat)abstract
- Proteoglycan monomers from guinea pig costal cartilage, bovine nasal and bovine tracheal cartilage were observed in the electron microscope after being spread in a monomolecular layer with cytochrome c. The proteoglycan molecule appeared as an extended central core filament to which side chain filaments were attached at various intervals. The molecules from the three sources displayed great ultrastructural similarities. On average, the core filament was about 290 nm long, there were about 25 side chain filaments per core filament, the side chain filaments were about 45 nm long, and the distance between the attachment points of the side chain filaments to the core filament was about 11 nm. With regard to overall size of the molecules, no evidence of distinct subpopulations was obtained. Good correlation was found between ultrastructural data for the proteoglycan molecules and chemical data obtained by enzyme digestions and gel chromatography. Together these data strongly support the interpretation of the electron microscopic pictures as indicating a central filament corresponding to the protein core and side chain filaments corresponding to the chondroitin sulphate chain clusters of the proteoglycan monomers.
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