Source:http://linkedlifedata.com/resource/pubmed/id/12709412
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2003-5-29
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pubmed:abstractText |
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 puromycin aminonucleoside-induced nephrosis of podocytes. LC3 is especially expressed in the podocytes of rat kidney as the membrane-bound form LC3-II. Biochemical analysis using a conditionally immortalized mouse 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 puromycin aminonucleoside-induced nephrosis. These results suggest that LC3-II-localized vesicles play an important role in the physiological function of podocytes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1530-6860
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1165-7
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:12709412-Animals,
pubmed-meshheading:12709412-Autophagy,
pubmed-meshheading:12709412-Biological Markers,
pubmed-meshheading:12709412-Cell Differentiation,
pubmed-meshheading:12709412-Clone Cells,
pubmed-meshheading:12709412-Kidney,
pubmed-meshheading:12709412-Mice,
pubmed-meshheading:12709412-Microtubule-Associated Proteins,
pubmed-meshheading:12709412-Models, Biological,
pubmed-meshheading:12709412-Nephrosis,
pubmed-meshheading:12709412-Phagosomes,
pubmed-meshheading:12709412-Protein Processing, Post-Translational,
pubmed-meshheading:12709412-Puromycin Aminonucleoside,
pubmed-meshheading:12709412-Rats,
pubmed-meshheading:12709412-Vacuoles
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pubmed:year |
2003
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pubmed:articleTitle |
MAP-LC3, a promising autophagosomal marker, is processed during the differentiation and recovery of podocytes from PAN nephrosis.
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pubmed:affiliation |
Division of Nephrology, Department of Internal Medicine, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan.
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pubmed:publicationType |
Journal Article
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