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Titolo:
RELATIVE INCREASE OF BIGLYCAN AND DECORIN AND ALTERED CHONDROITIN SULFATE EPITOPES IN THE DEGENERATING HUMAN INTERVERTEBRAL DISC
Autore:
INKINEN RI; LAMMI MJ; LEHMONEN S; PUUSTJARVI K; KAAPA E; TAMMI MI;
Indirizzi:
UNIV KUOPIO,DEPT ANAT,POB 1627 FIN-70211 KUOPIO FINLAND UNIV OULU,DEPT PHYS MED & REHABIL OULU FINLAND
Titolo Testata:
Journal of rheumatology
fascicolo: 3, volume: 25, anno: 1998,
pagine: 506 - 514
SICI:
0315-162X(1998)25:3<506:RIOBAD>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ARTICULAR-CARTILAGE; SMALL PROTEOGLYCAN-I; MONOCLONAL-ANTIBODIES; COLLAGEN INTERACTIONS; CONNECTIVE TISSUES; NUCLEUS PULPOSUS; ANNULUS FIBROSUS; CORE PROTEIN; PG-I; AGE;
Keywords:
INTERVERTEBRAL DISC; DEGENERATION; PROTEOGLYCANS; GLYCOSYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
R.I. Inkinen et al., "RELATIVE INCREASE OF BIGLYCAN AND DECORIN AND ALTERED CHONDROITIN SULFATE EPITOPES IN THE DEGENERATING HUMAN INTERVERTEBRAL DISC", Journal of rheumatology, 25(3), 1998, pp. 506-514

Abstract

Objective. Proteoglycans are major components of the extracellular matrix of the intervertebral disc. They are vital for the biomechanical properties of the tissue, and are subject to changes in disc degeneration. We aimed to further define these changes and their relationship to normal aging. Methods. Normal discs (age 13-53 years, n = 6) were analyzed from 5 different sites across the sagittal anterior-posterior direction. Degenerated anterior annulus fibrosus was collected from 7 patients aged 39-46 years. Extracted proteoglycans were separated usingagarose and polyacrylamide gel electrophoresis and detected with toluidine blue staining and Western blotting. Results. The center of the disc showed the highest level of total proteoglycans, but lowest levelsof decorin and biglycan. Western blots displayed reduced signal for both glycanated and nonglycanated biglycan and decorin after adolescence, while an increased signal of biglycan was observed in degenerated annuli. The 7D4(-) and 3B3(-) epitopes on native chondroitin sulfate chains were present in the large proteoglycans of intervertebral discs, but their signal intensity had no correlation to degeneration. Chondroitinase ABC digestion of the blots brought up 7D4(+) signal in the small proteoglycans of degenerated, but not in healthy tissue. Decrease or total loss of 2B6(+) epitope (indicating 4-sulfated stubs of chondroitin sulfate chains) were found in the large proteoglycans of all degenerated annuli. Conclusion. Human intervertebral disc degeneration involves the accumulation of decorin and biglycan relative to other uronic acid containing proteoglycans, the disappearance of 4-sulfated core region in aggrecan-like large proteoglycans, and the emergence of a core structure in the chains of small proteoglycans reacting with the 7D4 antibody; these findings indicate a fundamental alteration in matrixproperties that may contribute to the pathogenesis of the disease.

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Documento generato il 30/09/20 alle ore 02:53:05