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- Aspberg, A., et al.
(författare)
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Cartilage oligomeric matrix protein forms protein complexes with synovial lubricin via non-covalent and covalent interactions
- 2017
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Ingår i: Osteoarthritis and Cartilage. - : Elsevier BV. - 1063-4584. ; 25:9, s. 1496-1504
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Tidskriftsartikel (refereegranskat)abstract
- Objective: Understanding the cartilage surface structure, lost in arthritic disease, is essential for developing strategies to effectively restore it. Given that adherence of the lubricating protein, lubricin, to the cartilage surface is critical for boundary lubrication, an interaction with cartilage oligomeric matrix protein (COMP) was investigated. COMP, an abundant cartilage protein, is known to be important for matrix formation. Design: Synovial fluid (SF) from arthritic patients was used to detect possible COMP-lubricin complexes by immunological methods. Recombinant (RC) COMP and lubricin fragments were expressed to characterize this bonding and mass spectrometry employed to specifically identify the cysteines involved in inter-protein disulfide bonds. Results: COMP-lubricin complexes were identified in the SF of arthritic patients by Western blot, co-immunoprecipitation and sandwich ELISA. RC fragment solid-phase binding assays showed that the C-terminal (amino acids (AA) 518-757) of COMP bound non-covalently to the N-terminal of lubricin (AA 105-202). Mass spectrometry determined that although cysteines throughout COMP were involved in binding with lubricin, the cysteines in lubricin were primarily focused to an N-terminal region (AA 64-86). The close proximity of the non-covalent and disulfide binding domains on lubricin suggest a two-step mechanism to strongly bind lubricin to COMP. Conclusion: These data demonstrate that lubricin forms a complex network with COMP involving both non-covalent and covalent bonds. This complex between lubricin and the cartilage protein COMP can be identified in the SF of patients with arthritis conditions including osteoarthritis (OA) and rheumatoid arthritis (RA). (C) 2017 Osteoarthritis Research Society International. Published by Elsevier Ltd. All rights reserved.
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- Bengtsson, B., et al.
(författare)
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Comparison of disease severity in glaucoma patients identified by screening in the 1990s and in routine clinical care in the 2010s in Sweden
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Ingår i: Acta Ophthalmologica. - 1755-3768. ; , s. 1-8
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Tidskriftsartikel (refereegranskat)abstract
- Background and PurposeIn a previous study comparing the amount of visual field damage at presentation in patients having open-angle glaucoma (OAG) identified through screening and in patients diagnosed in routine clinical practice in the 1990s, the damage was considerably worse in the clinically diagnosed patients. In the present study we compare visual field damage at presentation in the same 402 screened patients with that seen in 281 newly detected previously untreated patients clinically diagnosed in the 2010s.MethodsThe perimetric visual field index mean deviation (MD) was compared in the two groups of patients.ResultsIn the clinical patients diagnosed with bilateral visual field damage the median MD was −5.1 dB in the better eye and −13.0 dB in the worse eye. In the screened patients the median MD in the better eye was −6.5 dB and −11.5 dB in the worse eye. The differences between the clinical and screened patients were non-significant, p = 0.28 and p = 0.67 respectively. More clinical patients had severe visual field loss, defined as MD less than −20 dB, in the worse eye than in the screened patients, 18.5% versus 12.7% respectively, p = 0.037.ConclusionThe visual field damage at presentation in clinically diagnosed OAG patients has improved in the past 20 years, but the proportion of patients with severe visual field loss in at least one eye, almost 20%, is still unacceptably high considering that severe visual field damage at presentation is the most important risk factor for later development of glaucoma blindness.
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- Dimberg, Y, et al.
(författare)
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Effects of low-dose X-irradiation on mouse-brain aggregation cultures
- 1992
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Ingår i: International Journal of Radiation Biology. - : Informa UK Limited. - 0955-3002 .- 1362-3095. ; 61:3, s. 355-363
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Tidskriftsartikel (refereegranskat)abstract
- Biochemical and morphological differentiation in reaggregating mouse-brain cell cultures after low-dose radiation (0.5 Gy) in vitro was studied. Cells were irradiated on culture day 2, corresponding to embryonic day 15-16, and different glial and neuronal markers were followed through development to postnatal day 40. The shape and size of irradiated aggregates were more irregular and smaller compared with controls. Total amounts of DNA and protein were significantly lower in irradiated aggregates than in controls between days 8 and 20. After 30 days in culture activities of the glial markers glutamine synthetase (GS) and 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP) were lower in X-irradiated aggregates than in controls. However, after 40 days the CNP activity in irradiated aggregates increased to levels above those of the controls. Irradiated and control aggregates did not differ significantly in neuronal marker enzyme activities, i.e. choline acetyltransferase (ChAT), acetylcholine esterase (AChE) and glutamic acid decarboxylase (GAD) measured on a per mg protein basis. On days 20 and 30 the amount of nerve growth factor (NGF) was two-fold higher in irradiated aggregates compared with non-irradiated ones, suggesting that, after irradiation, surviving cells in culture were induced to produce more NGF. After 40 days the amount of NGF in irradiated aggregates had decreased to the level found in the control aggregates.
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| 6. |
- 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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