| 1. |
- Heinegård, Dick, et al.
(författare)
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Articular cartilage
- 2014. - 6
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Ingår i: Rheumatology. - 9780323091381 ; , s. 33-41
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Bokkapitel (övrigt vetenskapligt/konstnärligt)
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| 2. |
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| 3. |
- Heinegård, Dick, et al.
(författare)
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Glycosylated matrix protein
- 2002
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Ingår i: Connective tissue and its heritable disorders: molecular, genetic, and medical aspects, 2nd edition. - Hoboken, NJ, USA : John Wiley & Sons, Inc.. - 9780471251859 ; , s. 271-291
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- Connective tissues have many features in common, including resisting and dissipating mechanical load and providing shape, as well as acting to provide barriers regulating water flow and diffusibility of macromolecules. In this chapter we have chosen to focus on cartilage and bone, covering many aspects of connective tissues. We give special focus to the noncollagenous proteins in their matrices.
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| 4. |
- Heinegård, Dick, et al.
(författare)
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Glycosylated Matrix Proteins
- 2002
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Ingår i: Connective Tissue and Its Heritable Disorders: Molecular, Genetic and Medical Aspects. - Hoboken, NJ, USA : John Wiley & Sons, Inc.. - 9780471251859 - 9780471221920 ; , s. 271-291
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- Connective tissues have many features in common, including resisting and dissipating mechanical load and providing shape, as well as acting to provide barriers regulating water flow and diffusibility of macromolecules. In this chapter we have chosen to focus on cartilage and bone, covering many aspects of connective tissues. We give special focus to the noncollagenous proteins in their matrices.
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| 5. |
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| 6. |
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| 7. |
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| 8. |
- Lorenzo, Pilar, et al.
(författare)
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Altered patterns and synthesis of extracellular matrix macromolecules in early osteoarthritis.
- 2004
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Ingår i: Matrix Biology. - : Elsevier BV. - 1569-1802 .- 0945-053X. ; 23:6, s. 381-391
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Tidskriftsartikel (refereegranskat)abstract
- The synthesis and contents of extracellular non-collagenous matrix macromolecules was studied in early and late human osteoarthritic (OA) cartilage obtained at surgery for sarcomas in the lower extremities (normal and early OA) or for total knee replacement (late stage OA). The early OA samples were those that had some fibrillation in the joint by visual examination. One group had fibrillation in the area sampled and the other group had no fibrillation. Cartilage was taken from the same topographical area on the medial femoral condyle in all the samples, labeled with [3H]leucine and [35S]sulfate for 4 h at 37 °C and extracted with 4 M guanidine–HCl. Analysis of the extracts showed that the total amount of proteoglycans relative to hydroxyproline content was higher in the early and late OA than in the normal cartilage. These proteoglycans showed a relatively lower [35S]sulfate incorporation into GAG chains and a higher [3H]leucine incorporation. The pattern of newly synthesized proteins was altered similarly in early and late OA. Notably, synthesis of cartilage oligomeric matrix protein (COMP), fibronectin, and cartilage intermediate layer protein (CILP) was increased, also reflected in their abundance as determined by enzyme-linked immunosorbent assay (ELISA). Collagen synthesis appeared significantly increased only in the late stage OA. The observed altered composition and pattern of biosynthesis indicate that the joint undergoes metabolic alterations early in the disease process, even before there is overt fibrillation of the tissue. The early OA samples studied appear to represent two distinct groups of early lesions in different stages of the process of cartilage deterioration as shown by their differences in relative rates of synthesis and abundance of proteins.
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| 9. |
- Lorenzo, Pilar, et al.
(författare)
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Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan
- 2001
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Ingår i: Journal of Biological Chemistry. - 1083-351X. ; 276:15, s. 12201-12211
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Tidskriftsartikel (refereegranskat)abstract
- Asporin, a novel member of the leucine-rich repeat family of proteins, was partially purified from human articular cartilage and meniscus. Cloning of human and mouse asporin cDNAs revealed that the protein is closely related to decorin and biglycan. It contains a putative propeptide, 4 amino-terminal cysteines, 10 leucine-rich repeats, and 2 C-terminal cysteines. In contrast to decorin and biglycan, asporin is not a proteoglycan. Instead, asporin contains a unique stretch of aspartic acid residues in its amino-terminal region. A polymorphism was identified in that the number of consecutive aspartate residues varied from 11 to 15. The 8 exons of the human asporin gene span 26 kilobases on chromosome 9q31.1-32, and the putative promoter region lacks TATA consensus sequences. The asporin mRNA is expressed in a variety of human tissues with higher levels in osteoarthritic articular cartilage, aorta, uterus, heart, and liver. The deduced amino acid sequence of asporin was confirmed by mass spectrometry of the isolated protein resulting in 84% sequence coverage. The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). The name asporin reflects the aspartate-rich amino terminus and the overall similarity to decorin.
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