Disassembly of the vimentin cytoskeleton disrupts articular cartilage chondrocyte homeostasis.

Blain, Emma Jane ORCID: https://orcid.org/0000-0001-8944-4254, Gilbert, Sophie Jane, Hayes, Anthony Joseph and Duance, Victor Colin ORCID: https://orcid.org/0000-0002-7555-2016 2006. Disassembly of the vimentin cytoskeleton disrupts articular cartilage chondrocyte homeostasis. Matrix biology 25 (7) , pp. 398-408. 10.1016/j.matbio.2006.06.002

Full text not available from this repository.

Abstract

Articular cartilage functions in dissipating forces applied across joints. It comprises an extracellular matrix containing primarily collagens, proteoglycans and water to maintain its functional properties, and is interspersed with chondrocytes. The chondrocyte cytoskeleton comprises actin microfilaments, tubulin microtubules and vimentin intermediate filaments. Previous studies have determined the contribution of actin and tubulin in regulating the synthesis of the extracellular matrix components aggrecan and type II collagen. The contribution of vimentin to extracellular matrix biosynthesis in any cell type has not previously been addressed. Therefore the aim of this study was to assess the role of vimentin in cartilage chondrocyte metabolism. Vimentin intermediate filaments were disrupted in high-density monolayer articular chondrocyte cultures using acrylamide for 7 days. De novo protein and collagen synthesis were measured by adding [3H]-proline, and sulphated glycosaminoglycan (sGAG) synthesis measured by adding [35S]-sulphate to cultures. Vimentin disruption resulted in decreased collagen synthesis, whilst sGAG synthesis was unaffected. In addition, there was a significant reduction in type II collagen and aggrecan gene transcription suggesting that the effects observed occur at both the transcriptional and translational levels. A 3-day cold chase demonstrated a significant inhibition of collagen and sGAG degradation; the reduction in collagen degradation was corroborated by the observed reduction in both pro-MMP 2 expression and activation. We have demonstrated that an intact vimentin intermediate filament network contributes to the maintenance of the chondrocyte phenotype and thus an imbalance favouring filament disassembly can disturb the integrity of the articular cartilage, and may ultimately lead to the development of pathologies such as osteoarthritis.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Uncontrolled Keywords:	Articular chondrocyte; Vimentin; Glycosaminoglycans; Collagen; Matrix metalloproteinases
Publisher:	Elsevier
ISSN:	0945-053X
Last Modified:	17 Oct 2022 08:47
URI:	https://orca.cardiff.ac.uk/id/eprint/1046

Citation Data

Cited 61 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item