Renalase in Peritoneal Dialysis Patients is Not Related to Blood Pressure, but to Dialysis Vintage

Zbroch, Edyta; Małyszko, Jolanta; Małyszko, J.; Koc-Żórawska, Ewa; Myśliwiec, M

doi:10.3747/pdi.2011.00118

Cited by 34 publications

(23 citation statements)

References 12 publications

(22 reference statements)

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“…Some studies suggested that blood renalase level is positively correlated with glomerular filtration rate and is markedly reduced in patients with CKD and end-stage renal disease (ESRD) [22,23,24,25]. In contrast, other studies revealed that serum renalase increased in parallel to the stage of CKD [26,27,28,29,30]. There are several possible explanations of this apparent contradiction.…”

Section: Discussionmentioning

confidence: 75%

Lisinopril Protects Against the Adriamycin Nephropathy and Reverses the Renalase Reduction: Potential Role of Renalase in Adriamycin Nephropathy

Han

Sun

et al. 2013

Kidney Blood Press Res

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Aims: To investigate the potential role of renalase in adriamycin nephropathy and the effect of lisinopril on the regulation of renalase. Methods: Adriamycin nephropathy was induced in male Wistar rats (n=12) by a single injection of adriamycin at 2 mg/kg body weight. Rats were then randomly assigned to a model group or a treatment group, to which were administered distilled water or the angiotensin converting enzyme inhibitor lisinopril, respectively, for 12 weeks. Six normal rats served as controls. At the end of study, physiological parameters and systolic blood pressure were measured. Glomerulosclerosis and tubulointerstitial injury were assessed by histopathology Renalase protein expression in kidney was quantified by immunohistochemistry and immunoblotting. The serum concentration and urinary excretion of renalase were determined by enzyme-linked immunosorbent assay. Results: In model group rats, proteinuria and systolic blood pressure were elevated. Increased serum renalase concentration was observed; however, renalase protein expression in the kidney was significantly decreased. Compared with the model group, decreased proteinuria, lower systolic blood pressure, and fewer morphologic lesions were detected in the treatment group. Although levels of serum renalase were similar, accumulation of renalase in urine and kidney tissue increased notably in the treatment group compared with the model group. Conclusions: This study suggests that renalase may be involved in the process of adriamycin-induced renal injuries. Lisinopril may attenuate adriamycin-induced kidney injury by controlling blood pressure, which may be partially attributed to the renalase expression and secretion.

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Section: Discussionmentioning

confidence: 75%

Lisinopril Protects Against the Adriamycin Nephropathy and Reverses the Renalase Reduction: Potential Role of Renalase in Adriamycin Nephropathy

Han

Sun

et al. 2013

Kidney Blood Press Res

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“…Previous studies have demonstrated the possible effects of renalase in chronic renal failure and cardiovascular diseases [11]. Data from clinical studies has shown that renalase level significantly decrease in patients with stroke and chronic kidney diseases [12,13,14,15,16,17], whereas elevated levels of renalase in heart and kidney transplant recipients were observed. The increased levels of renalase were predominantly dependent on kidney function, which deteriorates with time after transplantation [12,13,14].…”

Section: Discussionmentioning

confidence: 99%

Renalase Gene Polymorphism in Patients After Renal Allograft Transplantation

Pawlik¹,

Serdynska²,

Dąbrowska-Żamojcin³

et al. 2014

Kidney Blood Press Res

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Background/Aims: Renalase is a recently discovered protein, which is likely involved in regulation of blood pressure in humans and animals. Previous studies suggest that renalase reflects kidney functioning. A common missense polymorphism in the flavin-adenine dinucleotide-binding domain of human renalase (Glu37Asp) has been described. In this study we examined the association between (Glu37Asp) polymorphism (rs2296545) in renalase gene and kidney allograft function. Methods: The study enrolled 270 Caucasian kidney allograft recipients. SNP within the renalase was genotyped using TaqMan genotyping assays. Results: There were no statistically significant associations between renalase gene rs2296545 polymorphism and delayed graft function, acute rejection, chronic allograft dysfunction as well as creatinine serum concentrations and blood pressure values after transplantation. Conclusions: The results of this study suggest, that renalase gene rs2296545 polymorphism is not important factor determining renal allograft function.

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“…The same authors also investigated in chronic kidney disease patients the impact of hemodialysis and peritoneal dialysis 16 on blood serum renalase They concluded that impairment of renal function correlates with increased renalase levels [26][27][28], which was found up to 10-fold higher in anuric patients that underwent bilater nephrectomy in comparison to healthy subjects [26]. Finally, it was reported that stroke and hypertensions were associated to lower serum renalase concentrations in a hemodialysis population [27].…”

Section: Nadph-dependent Diaphorase Reactions With Various Artificialmentioning

confidence: 99%

“…A renalase concentration of 0.1 mg per gram wet tissue has been estimated in the kidneys by immunoblotting [10]. Data on the absolute concentration of renalase in human blood plasma have been explicitly reported only recently, as determined by ELISA, showing that it is about 4 g/ml in healthy individuals, corresponding to 0.1 M [23][24][25][26][27][28]. Murine renalase gene expression was observed by reverse transcriptase PCR in kidney, testicle, liver, heart, 12.5-days whole embryo, brain, and skeletal muscle [16].…”

Section: Renalase Isoforms and Gene Expression Patternmentioning

confidence: 99%

Is Renalase a Novel Player in Catecholaminergic Signaling? The Mystery of the Catalytic Activity of an Intriguing New Flavoenzyme

Baroni¹,

Milani²,

Pandini³

et al. 2013

CPD

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Renalase is a flavoprotein recently discovered in humans, preferentially expressed in the proximal tubules of the kidney and secreted in blood and urine. It is highly conserved in vertebrates, with homologs identified in eukaryotic and prokaryotic organisms. Several genetic, epidemiological, clinical and experimental studies show that renalase plays a role in the modulation of the functions of the cardiovascular system, being particularly active in decreasing the catecholaminergic tone, in lowering blood pressure and in exerting a protective action against myocardial ischemic damage. Deficient renalase synthesis might be the cause of the high occurrence of hypertension and adverse cardiac events in kidney disease patients. Very recently, recombinant human renalase has been structurally and functionally characterized in vitro. Results show that it belongs to the p-hydroxybenzoate hydroxylase structural family of flavoenzymes, contains non-covalently bound FAD with redox features suggestive of a dehydrogenase activity, and is not a catecholamine-degrading enzyme, either through oxidase or NAD(P)H-dependent monooxygenase reactions. The biochemical data now available will hopefully provide the basis for a systematic and rational quest toward the identification of the reaction catalyzed by renalase and of the molecular mechanism of its physiological action, which in turn are expected to favor the development of novel therapeutic tools for the treatment of kidney and cardiovascular diseases.

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Renalase in Peritoneal Dialysis Patients is Not Related to Blood Pressure, but to Dialysis Vintage

Cited by 34 publications

References 12 publications

Lisinopril Protects Against the Adriamycin Nephropathy and Reverses the Renalase Reduction: Potential Role of Renalase in Adriamycin Nephropathy

Lisinopril Protects Against the Adriamycin Nephropathy and Reverses the Renalase Reduction: Potential Role of Renalase in Adriamycin Nephropathy

Renalase Gene Polymorphism in Patients After Renal Allograft Transplantation

Is Renalase a Novel Player in Catecholaminergic Signaling? The Mystery of the Catalytic Activity of an Intriguing New Flavoenzyme

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