Reovirus 3 and neonatal biliary disease: Discussion of divergent results
✍ Scribed by Rachel Morecki; Joy Glaser
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 407 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0270-9139
No coin nor oath required. For personal study only.
✦ Synopsis
visioned (i) lack of protein degradation may result from a defect of the protease(s) involved (ii) modified (crosslinked?) cytoskeletal structures, even if adequately ubiquitinated, may be more stable to degradation than other cellular proteins. Competition of more readily degradable substrates for the protease may favor the persistence of less degradable proteins (3); (iii) Ub-aldehyde (eventually arising in alcoholic liver disease) may inhibit hydrolysis of Ub conjugates and regeneration of TJb (4); (iv) the ATP concentration in the injured cells may also be a limiting factor.
The data so far provided seem to indicate that ubiquitination is a secondary event destined to salvage cells from injury by abnormal proteins. With respect to liver disorders associated with MB formation, studies on the ubiquitination of different stages of MB development in relation to the ethanol-or drug-induced stress response and the activities of the Ub-dependent proteolytic pathways should help to clarify the role of Ub in MB pathogenesis.