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Literature summary for 3.4.11.21 extracted from

  • Lee, A.; Slattery, C.; Nikolic-Paterson, D.J.; Hryciw, D.H.; Wilk, S.; Wilk, E.; Zhang, Y.; Valova, V.A.; Robinson, P.J.; Kelly, D.J.; Poronnik, P.
    Chloride channel ClC-5 binds to aspartyl aminopeptidase to regulate renal albumin endocytosis (2015), Am. J. Physiol. Renal Physiol., 308, F784-F792.
    View publication on PubMed
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Application

Application Comment Organism
medicine enzyme is not present in the urine of healthy rats, however, it is readily detected in the urine in rat models of mild and heavy proteinuria. Urinary levels correlate with the severity of proteinuria Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rattus norvegicus 5829
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cytosol
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 Didelphis sp. 5829
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Organism

Organism UniProt Comment Textmining
Didelphis sp.
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Rattus norvegicus
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kidney
-
 Didelphis sp.
-

General Information

General Information Comment Organism
physiological function aspartyl aminopeptidase immunoprecipitates with beta-actin and tubulin, suggesting a role in cytoskeletal maintenance. Enzyme is not present in the urine of healthy rats, however, it is readily detected in the urine in rat models of mild and heavy proteinuria. Urinary levels correlate with the severity of proteinuria Rattus norvegicus
physiological function aspartyl aminopeptidase interacts with ClC-5, a chloride/proton exchanger that plays an obligate role in albumin uptake by the renal proximal tubule. ClC-5 forms an endocytic complex with the albumin receptor megalin/cubilin. Aspartyl aminopeptidase and ClC-5 associate in cells. The two proteins bind directly to each other. Overexpression of wild-type aspartyl aminopeptidase increases cell-surface levels of ClC-5 and albumin uptake. Overexpression results in significant decrease in the amount of G actin, suggesting a role for aspartyl aminopeptidase in stabilizing the cytoskeleton Didelphis sp.