Abstract
Macroautophagy, an intracellular bulk degradation process in eukaryotes, is sensitive to nutrient supply and deprivation. Microtubule-associated protein 1 light chain 3 (LC3), a mammalian homologue of yeast Atg8, plays an indispensable role in macroautophagy formation and is a suitable marker for this process. Through analysis of the subcellular distribution of LC3, we determined that the cytosolic fraction contained not only a precursor form (LC3-I), but also an apparent active form (LC3-IIs). Both cytosolic LC3-I and LC3-IIs were more responsive to amino acids than those of total homogenate. Moreover, changes in the LC3-IIs/I ratio reflected those in the total proteolytic flux remarkably in both fresh rat hepatocytes and H4-II-E cell lines. Thus, in addition to a sensitive index of macroautophagy, calculating the cytosolic LC3 ratio became an easy and quick quantitative method for monitoring its regulation in hepatocytes and H4-II-E cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 553-560 |
| Number of pages | 8 |
| Journal | Autophagy |
| Volume | 3 |
| Issue number | 6 |
| DOIs | |
| State | Published - 2007 |
| Externally published | Yes |
Keywords
- Amino acids
- H4-II-E cells
- Hepatocytes
- LC3
- Macroautophagy
- Proteolysis