Microtubule-associated protein 1 light chain 3 (LC3) is a unique modifier protein. LC3-I, the cytosolic form, is modified to LC3-II, the membrane-bound form, by a mechanism similar to ubiquitylation by E1- and E2-like enzymes, Apg7p and Apg3p, respectively. In the present study, we found that LC3-I is processed to LC3-II during the differentiation and recovery from @entity8424 -induced @entity3450 of podocytes. LC3 is especially expressed in the podocytes of @entity35 kidney as the membrane-bound form LC3-II. Biochemical analysis using a conditionally immortalized @entity19 podocyte clone (MPC) revealed that LC3-I is processed to LC3-II during the differentiation of cells into mature podocytes and accumulates in the membrane-rich fraction of the cell lysate. LC3-II-localized vesicles, which differ from lysosomes and endosomes, in differentiated MPC cells are morphologically similar to autophagic vacuoles during starvation-induced autophagy. During starvation-induced autophagy, autophagosomes fuses with lysosome and LC3-II on autophagosomes is finally degraded by lysosomal proteases. However, in differentiated MPC cells, little LC3-II on the vesicles is degraded by lysosomal proteases, suggesting that little LC3-II-localized vesicles in differentiated MPC cells fuse with lysosome. Furthermore, the LC3-II level in differentiated MPC cells increases with recovery from damage caused by experimental @entity8424 -induced @entity3450 . These results suggest that LC3-II-localized vesicles play an important role in the physiological function of podocytes.

MAP-LC3, a promising autophagosomal marker, is processed during the differentiation and recovery of podocytes from PAN XXXX .

@entity35 :: ('10116', 'Species') :: ['rat'] @entity19 :: ('10090', 'Species') :: ['mouse'] @entity8424 :: ('MESH:D011692', 'Chemical') :: ['puromycin aminonucleoside'] @entity3450 :: ('MESH:D009401', 'Disease') :: ['nephrosis']
@entity3450 :: (MESH:D009401,Disease) :: ['nephrosis']
