Bovine muscle 20S proteasome. II: Contribution of the 20S proteasome to meat tenderization as revealed by an ultrastructural approach
- Resource Type
- Authors
- Laurent Aubry; Gabriel Monin; Ahmed Ouali; D. Dutaud; Xavier Vignon; Florence Guignot
- Source
- Meat Science
Meat Science, Elsevier, 2006, 74 (2), pp.337-344
- Subject
- Cathepsin
biology
0402 animal and dairy science
Calpain
04 agricultural and veterinary sciences
[SDV.IDA] Life Sciences [q-bio]/Food engineering
040401 food science
040201 dairy & animal science
Cell biology
0404 agricultural biotechnology
Protein structure
Biochemistry
Proteasome
Ageing
[SDV.IDA]Life Sciences [q-bio]/Food engineering
biology.protein
Ultrastructure
Fragmentation (cell biology)
Myofibril
PROTEASOME
ComputingMilieux_MISCELLANEOUS
Food Science
HIGH pH MEAT
- Language
- ISSN
- 0309-1740
The role of the 20S proteasome proteolytic effects was revisited using an ultrastructural approach with the aim to explain some particular structural changes identified in type I muscles and in high pH meat. In both types of meat, major changes observed after ageing are an increase in the thickness of the Z-line followed by the appearance of an amorphous protein structure spreading out over the I-band. This was followed by a total degradation of this amorphous structure and of the Z-line. Partial transversal fragmentation of the myofibrils within the I-band can also be detected. The data reported clearly demonstrate that the 20S proteasome was able to mimic these sequential structural changes, a feature never obtained with either calpains or cathepsins. It is the first time that a direct implication of this complex in postmortem muscle is postulated.