Glycosylation of a key cubilin Asn residue results in reduced binding to albumin.

ABSTRACT: Kidney disease often manifests with an increase in proteinuria, which can result from both glomerular and/or proximal tubule injury. The proximal tubules are the major site of protein and peptide endocytosis of the glomerular filtrate, and cubilin is the proximal tubule brush border membrane glycoprotein receptor that binds filtered albumin and initiates its processing in proximal tubules. Albumin also undergoes multiple modifications depending upon the physiologic state. We previously documented that carbamylated albumin had reduced cubilin binding, but the effects of cubilin modifications on binding albumin remain unclear. Here, we investigate the cubilin-albumin binding interaction to define the impact of cubilin glycosylation and map the key glycosylation sites while also targeting spe

SUBMITTER: Yadav SPS 

PROVIDER: S-EPMC9485058 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature