AI Article Synopsis
- The study analyzes how muscle proteins in cows are broken down by proteasomes and calpains using 2D gel proteome analysis, focusing on the effects of specific inhibitors.
- Inhibiting the proteasome stops the breakdown of key muscle proteins like actin and myosin, indicating that proteasomes play a major role in protein degradation after death.
- Calpain's role appears less significant, causing only minor changes, suggesting that another form of calpain (p94) may be responsible for degradation that continues after the cow has died.
Article Abstract
The degradation of bovine muscle proteins by proteasome and ubiquitous calpains was explored via 2D gel proteome analysis by inhibition of the physiological level of the proteases by specific inhibitors. The inhibition of the proteasome chymotrypsin- and trypsin-like activity results in the lack of degradation of several fragments of structural proteins such as actin, troponin T, myosin light chain and nebulin. In addition the degradation of several sarcoplasmatic proteins was eliminated when proteasome was inhibited. The inhibition of the ubiquitous calpain only resulted in minor changes in the degradation pattern, which might indicate that p94, which is not inhibited by calpastatin, is involved in the degradation post-mortem. The results of the present study indicate a sequential degradation of the structural proteins post-mortem, where calpain initiates the disruption and destabilisation of the myofibrillar structure, and thereby allows the proteasome to act.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.meatsci.2007.08.003 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!