N-Cadherin cleavage during activated hepatic stellate cell apoptosis is inhibited by tissue inhibitor of metalloproteinase-1. [In supplement: 11th International Symposium on the Cells of the Hepatic Sinusoid and their Relation to Other Cells]


Murphy, Frank, Waung, Julian, Collins, Jane, Arthur, Michael J.P., Nagase, Hideaki, Mann, Derek, Benyon, R. Christopher and Iredale, John P. (2004) N-Cadherin cleavage during activated hepatic stellate cell apoptosis is inhibited by tissue inhibitor of metalloproteinase-1. [In supplement: 11th International Symposium on the Cells of the Hepatic Sinusoid and their Relation to Other Cells]. Comparative Hepatology, 3, (Suppl 1), p.S8. (doi:10.1186/1476-5926-2-S1-S8).

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Description/Abstract

Apoptosis of hepatic stellate cells (HSC) has previously been shown to occur during spontaneous resolution of experimental liver fibrosis. TIMP-1 has also been shown to have a key role because of its ability to inhibit apoptosis of HSC via matrix metalloproteinase (MMP) inhibition. This has led to further study of novel substrates for MMPs that might impact on HSC survival. N-Cadherin is known to mediate cell-cell contacts in fibroblasts. In this study we demonstrate that N-Cadherin is expressed by activated rat HSC. Furthermore, during apoptosis of HSC, the N-Cadherin is cleaved into smaller fragments. Apoptosis of HSC may be inhibited by TIMP-1. This is associated with reduced fragmentation of N-Cadherin. N-Cadherin may have an important role in supporting HSC survival while N-Cadherin cleavage may play a part in promoting HSC apoptosis in recovery from liver fibrosis.

Item Type: Article
Additional Information: 11th International Symposium on the Cells of the Hepatic Sinusoid and their Relation to Other Cells Tucson, Arizona, USA, 25–29 August, 2002.
ISSNs: 1476-5926 (print)
Related URLs:
Subjects: R Medicine > RM Therapeutics. Pharmacology
Q Science > QP Physiology
Q Science > QH Natural history > QH301 Biology
Divisions: University Structure - Pre August 2011 > School of Medicine
ePrint ID: 8191
Date Deposited: 10 Aug 2004
Last Modified: 27 Mar 2014 18:01
Contact Email Address: jec3@soton.ac.uk
URI: http://eprints.soton.ac.uk/id/eprint/8191

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