ArticleHistochemistry and cell biology2010
Prominin-2 is a novel marker of distal tubules and collecting ducts of the human and murine kidney.
Article in Histochemistry and cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- The role of ferroptosis in acute kidney injury: the preemptive mode of cell death and the bridging effect.Renal failure · 2025Review
- Whole Exome Sequencing in 26 Saudi Patients Expands the Mutational and Clinical Spectrum of Diabetic Nephropathy.Medicina (Kaunas, Lithuania) · 2025Article
- Prominosomes - a particular class of extracellular vesicles containing prominin-1/CD133?Journal of nanobiotechnology · 2025Review
- Emerging roles of prominin-1 (CD133) in the dynamics of plasma membrane architecture and cell signaling pathways in health and disease.Cellular & molecular biology letters · 2024Review
- PROM2 overexpression induces metastatic potential through epithelial-to-mesenchymal transition and ferroptosis resistance in human cancers.Clinical and translational medicine · 2024Article
- Contemporary Biomarkers for Renal Transplantation: A Narrative Overview.Journal of personalized medicine · 2023Review
- Ferroptotic mechanisms and therapeutic targeting of iron metabolism and lipid peroxidation in the kidney.Nature reviews. Nephrology · 2023Review
- Bioinformatics, RNA sequencing, and targeted bisulfite sequencing analyses identify the role of PROM2 as a diagnostic and prognostic biomarker.American journal of translational research · 2023Article
- Prominins control ciliary length throughout the animal kingdom: New lessons from human prominin-1 and zebrafish prominin-3.The Journal of biological chemistry · 2020Article
- PROM2 promotes gemcitabine chemoresistance via activating the Akt signaling pathway in pancreatic cancer.Experimental & molecular medicine · 2020Article
- Prominin2 Drives Ferroptosis Resistance by Stimulating Iron Export.Developmental cell · 2019Article
- Senescent Kidney Cells in Hypertensive Patients Release Urinary Extracellular Vesicles.Journal of the American Heart Association · 2019Article
- Article
- Non-Hsp genes are essential for HSF1-mediated maintenance of whole body homeostasis.Experimental animals · 2015Article
- Prominin-2 expression increases protrusions, decreases caveolae and inhibits Cdc42 dependent fluid phase endocytosis.Biochemical and biophysical research communications · 2013Article
- Histochemistry and cell biology: the annual review 2010.Histochemistry and cell biology · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prominin-1 (CD133) and its paralogue, prominin-2, are pentaspan membrane glycoproteins that are strongly expressed in the kidney where they have been originally cloned from. Previously, we have described the localization of prominin-1 in proximal tubules of the nephron. The spatial distribution of prominin-2, however, has not yet been documented in the kidney. We therefore examined the expression of this molecule along distinct tubular segments of the human and murine nephron using in situ hybridization and immunohistochemistry. Our findings indicated that human prominin-2 transcripts and protein were confined to distal tubules of the nephron including the thick ascending limb of Henle's loop and the distal convoluted tubule, the connecting duct and to the collecting duct system. Therein, this glycoprotein was enriched at the basolateral plasma membrane of the tubular epithelial cells with exception of the thick ascending limb where it was also found in the apical domain. This is in contrast with the exclusive apical localization of prominin-1 in epithelial cells of proximal nephron tubules. The distribution of murine prominin-2 transcripts was reminiscent of its human orthologue. In addition, a marked enrichment in the epithelium covering the papilla and in the urothelium of the renal pelvis was noted in mice. Finally, our biochemical analysis revealed that prominin-2 was released into the clinically healthy human urine as a constituent of small membrane vesicles. Collectively our data show the distribution and subcellular localization of prominin-2 within the kidney in situ and its release into the urine. Urinary detection of this protein might offer novel diagnostic approaches for studying renal diseases affecting distal segments of the nephron.
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