ArticleBMC nephrology2013
Characterization of a short isoform of the kidney protein podocin in human kidney.
Article in BMC nephrology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- In vivo characterization of a podocyte-expressed short podocin isoform.BMC nephrology · 2023Article
- Peptide Charge Derivatization as a Tool for Early Detection of Preeclampsia by Mass Spectrometry-A Comparison with the ELISA Test.Molecules (Basel, Switzerland) · 2021Article
- Review
- Detection of Podocin in Human Urine Sediment Samples by Charge Derivatization and LC-MS-MRM Method.International journal of molecular sciences · 2020Article
- Rigorous characterization of urinary extracellular vesicles (uEVs) in the low centrifugation pellet - a neglected source for uEVs.Scientific reports · 2020Article
- Article
- Article
- Endoplasmic reticulum-retained podocin mutants are massively degraded by the proteasome.The Journal of biological chemistry · 2018Article
- N-Degradomic Analysis Reveals a Proteolytic Network Processing the Podocyte Cytoskeleton.Journal of the American Society of Nephrology : JASN · 2017Article
- Article
- Phosphoproteomic analysis reveals regulatory mechanisms at the kidney filtration barrier.Journal of the American Society of Nephrology : JASN · 2014Article
- A disease-causing mutation illuminates the protein membrane topology of the kidney-expressed prohibitin homology (PHB) domain protein podocin.The Journal of biological chemistry · 2014Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSteroid resistant nephrotic syndrome is a severe hereditary disease often caused by mutations in the NPHS2 gene. This gene encodes the lipid binding protein podocin which localizes to the slit diaphragm of podocytes and is essential for the maintenance of an intact glomerular filtration barrier. Podocin is a hairpin-like membrane-associated protein that multimerizes to recruit lipids of the plasma membrane. Recent evidence suggested that podocin may exist in a canonical, well-studied large isoform and an ill-defined short isoform. Conclusive proof of the presence of this new podocin protein in the human system is still lacking.
methodsWe used database analyses to identify organisms for which an alternative splice variant has been annotated. Mass spectrometry was employed to prove the presence of the shorter isoform of podocin in human kidney lysates. Immunofluorescence, sucrose density gradient fractionation and PNGase-F assays were used to characterize this short isoform of human podocin.
resultsMass spectrometry revealed the existence of the short isoform of human podocin on protein level. We cloned the coding sequence from a human kidney cDNA library and showed that the expressed short variant was retained in the endoplasmic reticulum while still associating with detergent-resistant membrane fractions in sucrose gradient density centrifugation. The protein is partially N-glycosylated which implies the presence of a transmembranous form of the short isoform.
conclusionsA second isoform of human podocin is expressed in the kidney. This isoform lacks part of the PHB domain. It can be detected on protein level. Distinct subcellular localization suggests a physiological role for this isoform which may be different from the well-studied canonical variant. Possibly, the short isoform influences lipid and protein composition of the slit diaphragm complex by sequestration of lipid and protein interactors into the endoplasmic reticulum.
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