ArticleAmerican journal of physiology. Cell physiology2015
Deep proteomic profiling of vasopressin-sensitive collecting duct cells. I. Virtual Western blots and molecular weight distributions.
Article in American journal of physiology. Cell physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- LRBA is essential for urinary concentration and body water homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bayesian analysis of dynamic phosphoproteomic data identifies protein kinases mediating GPCR responses.Cell communication and signaling : CCS · 2022Article
- Activation of AQP2 water channels by protein kinase A: therapeutic strategies for congenital nephrogenic diabetes insipidus.Clinical and experimental nephrology · 2021Review
- Phosphoproteomic identification of vasopressin-regulated protein kinases in collecting duct cells.British journal of pharmacology · 2021Article
- α-Actinin 4 Links Vasopressin Short-Term and Long-Term Regulation of Aquaporin-2 in Kidney Collecting Duct Cells.Frontiers in physiology · 2021Article
- Phosphoproteomic identification of vasopressin V2 receptor-dependent signaling in the renal collecting duct.American journal of physiology. Renal physiology · 2019Article
- Enhanced validation of antibodies for research applications.Nature communications · 2018Article
- From Molecules to Mechanisms: Functional Proteomics and Its Application to Renal Tubule Physiology.Physiological reviews · 2018Review
- Protein phosphatase 2C is responsible for VP-induced dephosphorylation of AQP2 serine 261.American journal of physiology. Renal physiology · 2017Article
- Vasopressin-induced serine 269 phosphorylation reduces Sipa1l1 (signal-induced proliferation-associated 1 like 1)-mediated aquaporin-2 endocytosis.The Journal of biological chemistry · 2017Article
- Molecular mechanisms regulating aquaporin-2 in kidney collecting duct.American journal of physiology. Renal physiology · 2016Review
- BIG: a large-scale data integration tool for renal physiology.American journal of physiology. Renal physiology · 2016Article
- Comprehensive database of human E3 ubiquitin ligases: application to aquaporin-2 regulation.Physiological genomics · 2016Article
- Proteomic profiling of nuclear fractions from native renal inner medullary collecting duct cells.Physiological genomics · 2016Article
- Deep proteomic profiling of vasopressin-sensitive collecting duct cells. II. Bioinformatic analysis of vasopressin signaling.American journal of physiology. Cell physiology · 2015Article
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6 authors at 2 institutions in 2 countries.
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Abstract
The mouse mpkCCD cell line is a continuous cultured epithelial cell line with characteristics of renal collecting duct principal cells. This line is widely used to study epithelial transport and its regulation. To provide a data resource useful for experimental design and interpretation in studies using mpkCCD cells, we have carried out "deep" proteomic profiling of these cells using three levels of fractionation (differential centrifugation, SDS-PAGE, and HPLC) followed by tandem mass spectrometry to identify and quantify proteins. The analysis of all resulting samples generated 34.6 gigabytes of spectral data. As a result, we identified 6,766 proteins in mpkCCD cells at a high level of stringency. These proteins are expressed over eight orders of magnitude of protein abundance. The data are provided to users as a public data base (https://helixweb.nih.gov/ESBL/Database/mpkFractions/). The mass spectrometry data were mapped back to their gel slices to generate "virtual Western blots" for each protein. For most of the 6,766 proteins, the apparent molecular weight from SDS-PAGE agreed closely with the calculated molecular weight. However, a substantial fraction (>15%) of proteins was found to run aberrantly, with much higher or much lower mobilities than predicted. These proteins were analyzed to identify mechanisms responsible for altered mobility on SDS-PAGE, including high or low isoelectric point, high or low hydrophobicity, physiological cleavage, residence in the lysosome, posttranslational modifications, and expression of alternative isoforms due to alternative exon usage. Additionally, this analysis identified a previously unrecognized isoform of aquaporin-2 with apparent molecular mass <20 kDa.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.