Differential expression and targeting of endogenous Arf1 and Arf6 small GTPases in kidney epithelial cells in situ

Annan, Jaafar El; Brown, Dennis; Breton, Sylvie; Bourgoin, Sylvain G.; Ausiello, Dennis A.; Marshansky, Vladimir

doi:10.1152/ajpcell.00250.2003

Cited by 33 publications

(10 citation statements)

References 52 publications

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“…2a-aЉ, b-bЉ; hollow arrows and white arrowheads, respectively). A partial co-localization of prominin-2 and calbindin-D28k, a calcium-binding protein enriched in connecting tubules (Kojima et al 2002;El-Annan et al 2004), was also observed suggesting the presence of prominin-2 in the distal-most segment of the nephron (Fig. 1e; hollow arrows and white arrowheads, respectively).…”

Section: Localization Of Human Prominin-2 Protein and Transcript In Tmentioning

confidence: 85%

Prominin-2 is a novel marker of distal tubules and collecting ducts of the human and murine kidney

Jászai

Farkas

Fargeas

et al. 2010

Histochem Cell Biol

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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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Section: Localization Of Human Prominin-2 Protein and Transcript In Tmentioning

confidence: 85%

Prominin-2 is a novel marker of distal tubules and collecting ducts of the human and murine kidney

Jászai

Farkas

Fargeas

et al. 2010

Histochem Cell Biol

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“…Hence renal PT CdMT uptake and cell death are mediated, at least in part, by megalin and cubilin. The significance of megalin/cubilin mediated RME for CdMT toxicity in PT cells was further confirmed by investigating the role of the small GTPase ARF6 (ADP-ribosylation factor 6), which is involved in internalization of ligands by RME and endocytic vesicular trafficking in rat PT cells (Maranda et al 2001;El-Annan et al 2004). Transfection of a dominant-negative form of ARF6 prevented recycling of megalin to the cell surface.…”

Section: Megalin and Cubilinmentioning

confidence: 87%

Catch me if you can! Novel aspects of cadmium transport in mammalian cells

Thévenod

2010

Biometals

159

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Cadmium (Cd(2+)) is a nonessential divalent metal ion that causes toxicity in multiple organs in humans. In order for toxicity to occur Cd(2+) must first enter cells by utilizing transport pathways for essential metals. This review focuses on studies in which Cd(2+) transport was directly demonstrated by electrophysiological, radiotracer or Cd(2+)-sensitive fluorescent dye techniques. The chemistry of Cd(2+) and metal ions in general is addressed in the context of properties relevant for transport through membrane proteins, such as hydration energy. Apart from transport by the ZIP transporters SLC39A8 and SLC39A14, which is not topic of the review, uptake of free Cd(2+) has been demonstrated for the Fe(2+)/H(+) cotransporter divalent metal transporter 1. Moreover, the multiligand endocytic receptors megalin and cubilin take up cadmium-metallothionein complexes via receptor-mediated endocytosis. The role of ATP binding cassette transporters in Cd(2+) efflux from cells is also discussed. Both the multidrug resistance-associated protein 1 and cystic fibrosis transmembrane conductance regulator are likely to transport cadmium-glutathione complexes out of cells, whereas transport of free Cd(2+) by the multidrug resistance P-glycoprotein remains controversial. Finally, arguments for and against Cd(2+) transport by Ca(2+) channels are presented. Most N- and L-type Ca(2+) channels are closed at resting membrane potential (with the exception of CaV1.3 channels) and therefore unlikely to allow significant Cd(2+) influx under physiological conditions. CaV3.1 and CaV3.2 T-type calcium channels are permeated by divalent metal ions, such as Fe(2+) and Mn(2+) because of considerable "window" currents close to resting membrane potential and could be responsible for tonic Cd(2+) entry. TRPM7 and the mitochondrial Ca(2+) uniporter are other likely candidates for Cd(2+) transporters, whereas the role of Orai proteins, the store-operated calcium channels carrying Ca(2+) release-activated Ca(2+) current, in Cd(2+) influx remains to be investigated.

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“…Arfs are participating in the formation of coated transport vesicles. El-Annan et al have shown abundant expression of Arf1 and Arf6 in the distal nephron and the collecting duct and have demonstrated that Arf1 is mostly localized to the apical membrane whereas Arf6 appeared to be mainly expressed at the basolateral membrane [43]. Arf6 was further demonstrated as a factor promoting Avpr2 recycling [44].…”

Section: Small Gtp-binding Proteinsmentioning

confidence: 99%

A comprehensive analysis of gene expression profiles in distal parts of the mouse renal tubule

Pradervand

Mercier

Centeno

et al. 2010

Pflugers Arch - Eur J Physiol

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The distal parts of the renal tubule play a critical role in maintaining homeostasis of extracellular fluids. In this review, we present an in-depth analysis of microarray-based gene expression profiles available for microdissected mouse distal nephron segments, i.e., the distal convoluted tubule (DCT) and the connecting tubule (CNT), and for the cortical portion of the collecting duct (CCD; Zuber et al., Proc Natl Acad Sci USA 106: [16523][16524][16525][16526][16527][16528] 2009). Classification of expressed transcripts in 14 major functional gene categories demonstrated that all principal proteins involved in maintaining the salt and water balance are represented by highly abundant transcripts. However, a significant number of transcripts belonging, for instance, to categories of Gprotein-coupled receptors or serine/threonine kinases exhibit high expression levels but remain unassigned to a specific renal function. We also established a list of genes differentially expressed between the DCT/CNT and the CCD. This list is enriched by genes related to segment-specific transport functions and by transcription factors directing the development of the distal nephron or collecting ducts. Collectively, this in silico analysis provides comprehensive information about relative abundance and tissue specificity of the DCT/ CNT and the CCD expressed transcripts and identifies new candidate genes for renal homeostasis.

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Differential expression and targeting of endogenous Arf1 and Arf6 small GTPases in kidney epithelial cells in situ

Cited by 33 publications

References 52 publications

Prominin-2 is a novel marker of distal tubules and collecting ducts of the human and murine kidney

Prominin-2 is a novel marker of distal tubules and collecting ducts of the human and murine kidney

Catch me if you can! Novel aspects of cadmium transport in mammalian cells

A comprehensive analysis of gene expression profiles in distal parts of the mouse renal tubule

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