The University of Southampton
University of Southampton Institutional Repository

Expression of matrix metalloproteinase-2 and -14 persists during early resolution of experimental liver fibrosis and might contribute to fibrolysis

Zhou, Xiaoying, Hovell, Christopher J., Pawley, Susannah, Hutchings, Matthew I., Arthur, Michael J., Iredale, John P. and Benyon, R. Christopher (2004) Expression of matrix metalloproteinase-2 and -14 persists during early resolution of experimental liver fibrosis and might contribute to fibrolysis Liver International, 24, (5), pp. 492-501. (doi:10.1111/j.1478-3231.2004.0946.x).

Record type: Article

Abstract

Abstract: Background/Aims: Resolution of liver fibrosis is possible but the identity of the matrix metalloproteinases (MMPs) which degrade the accumulated collagens is uncertain. We examined MMP-2 and MMP-14 expression in established and resolving fibrosis to assess their role in resolution of liver fibrosis.
Methods: MMP and tissue inhibitor of metalloproteinase (TIMP)-2 expression in liver extracts was examined by ribonuclease protection assay, Western blotting and gelatin zymography. MMP activity was examined by 14C gelatin degradation.
Results: In human cirrhotic liver, MMP-14 mRNA was increased to 230–330% of normal liver expression. Both 63 kDa proenzyme and 60 kDa activated form were present. Cirrhotic livers had 270–320% of normal liver expression of MMP-2 protein with 20–25% being the 62 Da activated form. Protein and mRNA for MMP-2 and MMP-14 progressively increased during 8 weeks of CCl4 treatment in rats. Between 3 and 7 days of resolution from CCl4 liver fibrosis, MMP-2 and MMP-14 persisted at elevated levels. Gelatinolytic activity in liver homogenates peaked at 7 days of recovery, being 140% above that in livers at peak fibrosis.
Conclusions: Increased expression and activation of MMP-2 and -14 occurs even under conditions of elevated TIMPs during liver fibrogenesis. During liver fibrosis resolution, as TIMP expression decays, the persistence of MMP-2 and MMP-14 may permit collagen degradation.

Full text not available from this repository.

More information

Submitted date: 16 December 2003
Published date: October 2004
Additional Information: Basic study
Keywords: collagenase, hepatic stellate cell, liver fibrosis, matrix metalloproteinase, tissue inhibitor of metalloproteinase

Identifiers

Local EPrints ID: 27509
URI: http://eprints.soton.ac.uk/id/eprint/27509
ISSN: 1478-3223
PURE UUID: 19d63b20-33fa-4aaf-ae9e-5c7806ad9007

Catalogue record

Date deposited: 27 Apr 2006
Last modified: 17 Jul 2017 16:04

Export record

Altmetrics

Contributors

Author: Xiaoying Zhou
Author: Christopher J. Hovell
Author: Susannah Pawley
Author: Matthew I. Hutchings
Author: Michael J. Arthur
Author: John P. Iredale
Author: R. Christopher Benyon

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×