Decreased abundance of urinary exosomal aquaporin-1 in renal ischemia-reperfusion injury

Sonoda, Hiroko; Yokota-Ikeda, Naoko; Oshikawa, Sayaka; Kanno, Yosuke; Yoshinaga, Kazuya; Uchida, Katsuhisa; Ueda, Yuuji; Kimiya, Kouichi; Uezono, Shigehiro; Ueda, Akira; Ito, Katsuaki; Ikeda, Masahiro

doi:10.1152/ajprenal.00200.2009

Cited by 132 publications

(117 citation statements)

References 27 publications

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“…Urinary exosomes, on the other hand, are derived from the kidney and mostly contain proteins secreted by the kidney tissue. Based on this rationale, several recent papers have reported potential new markers of kidney disease in urinary exosomes [1][2][3][4] . However, there is still lack of experimental confirmation that urinary exosomes indeed represent changes in the kidney tissue, which may not be detectable in whole urine.…”

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confidence: 99%

In Diabetic Kidney Disease Urinary Exosomes Better Represent Kidney Specific Protein Alterations Than Whole Urine

et al. 2015

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Background: Predicting or diagnosing underlying kidney disease by analyzing whole urine remains the mainstay of nephrology practice. However, whole urine is a poor compartment to assess many structural changes in the kidney because whole urine contains only a few proteins derived from the kidney itself. Urinary exosomes, on the other hand, which are derived from the kidney, contain proteins secreted by the kidney. We experimentally tested the hypothesis that ‘urinary exosomes more faithfully represent changes in the kidney tissue than whole urine'. A direct comparison between whole urine and urine exosomal levels of two chosen kidney disease markers, gelatinase and ceruloplasmin, was carried out on diabetic kidney disease patients. Methods: Urinary exosomes were separated from whole urine by sequential centrifugation including ultra-centrifugation. Gelatinase activity was measured using fluorosceinated gelatin as the substrate, and ceruloplasmin was measured by sandwich ELISA. A few kidney specimens from patients biopsied for atypical features were histochemically stained for validation of the biochemical results. Results: We found that changes in both, gelatinase (decreased activity) and ceruloplasmin (increased levels), in the urinary exosomes of diabetic kidney patients were in agreement with the alterations of these two proteins in the kidney tissue. In contrast, the levels of these two proteins in whole urine were highly variable and did not correlate with levels in the diabetic kidney tissue. Conclusion: In conclusion, these results confirmed our hypothesis that protein markers in urinary exosomes better reflected the underlying protein changes in the kidney than in whole urine samples.

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confidence: 99%

In Diabetic Kidney Disease Urinary Exosomes Better Represent Kidney Specific Protein Alterations Than Whole Urine

et al. 2015

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“…Recently, Rutkovskiy et al showed that hyperosmolarity increased myocardial AQP1 mRNA and protein glycosylation, but did not influence the total AQP1 protein (28). An isolated change in AQP1 glycosylation in the kidney was also recently reported by Sonoda et al (29). However, until now the functional significance of AQP1 glycosylation has not been conclusively determined.…”

Section: Discussionmentioning

confidence: 89%

The expression profile of aquaporin 1 in rat myocardium after severe burns

Li¹,

Zha²,

Li³

et al. 2015

Turk J Med Sci

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Background/aim: To investigate the myocardial expression profile of aquaporin 1 (AQP1) in rats after severe burns.Materials and methods: Ninety healthy male adult Wistar rats were randomly assigned to the following treatments: sham operation (control group, n = 6), immediate fluid resuscitation treatment post scalding (IF group, n = 42), and delayed fluid resuscitation treatment after scalding (DF group, n = 42). At 3, 6, 12, 24, 48, 72, and 120 h after scalding, myocardial water contents were assayed and AQP1 expressions were detected by real-time polymerase chain reaction and western blot. The AQP levels in the myocardium at 12 h after scalding were assayed by gene microarrays.Results: Scald injuries resulted in significantly synchronized increases in the myocardial water contents and the myocardial mRNA and protein expression of AQP1, with a peak at 12 h after scalding. Rats receiving delayed fluid resuscitation treatment had more severe myocardial edema and significantly higher myocardial AQP1 expressions than the rats receiving immediate fluid resuscitation treatment. The mRNAs of 6 other AQPs (AQP2, 3, 4, 6, 7, and 12b) were found to be changed in the myocardium among rats with different treatments. Conclusion:AQP1 may play a functional role in the development of myocardial edema after scalding. Targeting AQP1 may provide opportunities for therapeutic intervention in myocardial edema following severe burns.

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“…8 Renal cell carcinomas have been found to shed particularly high numbers of exosomes. 9 It seems plausible-and proven in the case of AQP1-that these exosomes contain AQP1 and ADFP.…”

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confidence: 97%

Screening for Kidney Cancer: Is There a Role for Aquaporin-1 and Adipophilin?

Grebe

Erickson²

2010

Mayo Clinic Proceedings

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For personal use. Mass reproduce only with permission from Mayo Clinic Proceedings a .However, the nature of the analyte, urine, and the biology of renal epithelium tilt the balance in favor of these markers. Urine contains very low concentrations of circulating proteins in the absence of renal disease. In addition, neither AQP1 nor ADFP is a secreted protein. Aquaporin-1 is a membrane protein, and ADFP is an intracellular protein associated with lipid droplets. Therefore, AQP1 or ADFP found in urine can be expected to originate from epithelium facing the filtrate side, rather than the blood side, of the nephron. Within the nephron, concentrations are highest in the proximal tubules. Thus, with urine testing, AQP1 and ADFP not only are organ specific for the kidney but also are localized to the structures that give rise to most renal cell carcinomas. [2][3][4] In addition, AQP1 and ADFP are greatly overexpressed in renal cell carcinomas compared with normal tubules, albeit more so in clear cell carcinomas than in the papillary morphotype. [5][6][7] The diagnostic feature that has given rise to the term clear cell carcinoma is in fact caused by lipid droplet accumulation within the tumor cells, all of which contain copious amounts of ADFP. Cancer cell shedding alone might consequently be expected to elevate urinary AQP1 and ADFP concentrations, but many cells cast off significant numbers of exosomes during their life cycle. These 50-to 90-nm diameter vesicles allow cells to selectively shed certain membrane portions, which can serve a role in cell-to-cell nutrient transport, signaling, and even exchange of nucleic acids and pathogens, as well as allowing selective export of lipids, proteins, peptides, cytokines, and various cellular structures and components. 8 Renal cell carcinomas have been found to shed particularly high numbers of exosomes. 9 It seems plausible-and proven in the case of AQP1-that these exosomes contain AQP1 and ADFP.Thus, AQP1 and ADFP in urine might make surprisingly good candidate tumor markers for the main renal Editorial

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Decreased abundance of urinary exosomal aquaporin-1 in renal ischemia-reperfusion injury

Cited by 132 publications

References 27 publications

In Diabetic Kidney Disease Urinary Exosomes Better Represent Kidney Specific Protein Alterations Than Whole Urine

In Diabetic Kidney Disease Urinary Exosomes Better Represent Kidney Specific Protein Alterations Than Whole Urine

The expression profile of aquaporin 1 in rat myocardium after severe burns

Screening for Kidney Cancer: Is There a Role for Aquaporin-1 and Adipophilin?

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