Demonstration of induction of erythrocyte inosine monophosphate dehydrogenase activity in Ribavirin-treated patients using a high performance liquid chromatography linked method

Montero, Celia; Duley, John A.; Fairbanks, Lynette D.; McBride, M. B.; Micheli, Vanna; Cant, AJ; Morgan, Graeme

doi:10.1016/0009-8981(95)06088-u

Cited by 48 publications

(53 citation statements)

References 17 publications

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“…They observed both a wide range and a higher mean of IMPDH activities in children with leukaemia compared to healthy controls [17]. By contrast, Montero used a nonradioactive high-performance liquid chromatographic (HPLC)-based assay to determine the IMPDH enzyme activity in erythrocytes of patients with leukaemia and lymphomas and detected no enzyme activity differences compared to healthy controls [18].…”

Section: Introductionmentioning

confidence: 93%

RETRACTED: Validation and application of a high-performance liquid chromatographic-based assay for determination of the inosine 5′-monophosphate dehydrogenase activity in erythrocytes

Khalil¹,

Erb

Khalil

et al. 2006

Journal of Chromatography B

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Section: Introductionmentioning

confidence: 93%

RETRACTED: Validation and application of a high-performance liquid chromatographic-based assay for determination of the inosine 5′-monophosphate dehydrogenase activity in erythrocytes

Khalil¹,

Erb

Khalil

et al. 2006

Journal of Chromatography B

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“…In this study, IMPDH activity was measured in peripheral blood mononuclear cells using a modified version of an assay reported by Glander et al 17 Several different assay methodologies have been reported for the measurement of IMPDH activity in different cell types (ie, red blood, mononuclear or CD3+ cells) 17,[31][32][33][34][35] ; however, because of differences in the assay conditions, it is difficult to compare the values of IMPDH activity between publications. Initially, we have tried to follow the assay published by Glander et al 17 ;…”

Section: Discussionmentioning

confidence: 99%

Effect of Diabetes Mellitus on Mycophenolate Sodium Pharmacokinetics and Inosine Monophosphate Dehydrogenase Activity in Stable Kidney Transplant Recipients

Patel¹,

Richman²,

Yang³

et al. 2007

Therapeutic Drug Monitoring

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Effect of diabetes mellitus on mycophenolic acid (MPA) pharmacokinetics and catalytic activity of inosine monophosphate dehydrogenase (IMPDH) was investigated in maintenance kidney transplant recipients. Demographically matched diabetic (n = 9) and nondiabetic (n = 9) patients were included in a 12-hour open-label, steady-state study after oral administration of entericcoated mycophenolate sodium. Concentrations of total MPA and free MPA, MPA-glucuronide, and acyl-MPA-glucuronide were measured and oral acetaminophen absorption was used as a marker for gastric-emptying rate. Median (range) of MPA area under the curve 0-12 was 36.7 (range, 16.4-116.4) mg * h/L in diabetic and 48.2 (range, 34.9-80.1) mg * h/L in nondiabetic patients (P = 0.49). All other primary pharmacokinetic parameters, including time to maximum concentration, for total or unbound MPA as well as MPA metabolites were comparable. In contrast, IMPDH activity was 17.5 ± 2.8 versus 46.6 ± 2.5 nmol XMP/h/mg protein in diabetics and nondiabetics, respectively (P < 0.0001) and was significantly lower in the diabetics irrespective of concomitant therapy with cyclosporine or tacrolimus. This study demonstrated that diabetes does not alter MPA pharmacokinetics when administered as enteric-coated mycophenolate sodium; however, IMPDH activity appeared to be significantly lower in patients with diabetes independent of the unbound or total concentrations of MPA. Further investigations are warranted to investigate the regulation of IMPDH enzyme in patients with diabetes.

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“…IMPDH activity assay was carried essentially as described previously 60 with the following modifications. 293-NPH cells were cultured in DMEM containing 25 or 5.5 mM glucose in the absence or presence of 50 g/ml mizoribine for 48 h at 37°C.…”

Section: Impdh Activity Assaymentioning

confidence: 99%

Mizoribine Corrects Defective Nephrin Biogenesis by Restoring Intracellular Energy Balance

Nakajo

Khoshnoodi

Takenaka

et al. 2007

Journal of the American Society of Nephrology

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Proteins are modified and folded within the endoplasmic reticulum (ER). When the influx of proteins exceeds the capacity of the ER to handle the load, the ER is "stressed" and protein biogenesis is affected. We have previously shown that the induction of ER stress by ATP depletion in podocytes leads to mislocalization of nephrin and subsequent injury of podocytes. The aim of the present study was to determine whether ER stress is associated with proteinuria in vivo and whether the immunosuppressant mizoribine may exert its antiproteinuric effect by restoring normal nephrin biogenesis. Induction of nephrotic-range proteinuria with puromycin aminonucleoside in mice increased expression of the ER stress marker GRP78 in podocytes, and led to the mislocalization of nephrin to the cytoplasm. In vitro, mizoribine, through a mechanism likely dependent on the inhibition of inosine 5Ј-monophosphate dehydrogenase (IMPDH) activity in podocytes, restored the intracellular energy balance by increasing levels of ATP and corrected the posttranslational processing of nephrin. Therefore, we speculate that mizoribine may induce remission of proteinuria, at least in part, by restoring the biogenesis of slit diaphragm proteins in injured podocytes. Further understanding of the ER microenvironment may lead to novel approaches to treat diseases in which abnormal handling of proteins plays a role in pathogenesis.

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Demonstration of induction of erythrocyte inosine monophosphate dehydrogenase activity in Ribavirin-treated patients using a high performance liquid chromatography linked method

Cited by 48 publications

References 17 publications

RETRACTED: Validation and application of a high-performance liquid chromatographic-based assay for determination of the inosine 5′-monophosphate dehydrogenase activity in erythrocytes

RETRACTED: Validation and application of a high-performance liquid chromatographic-based assay for determination of the inosine 5′-monophosphate dehydrogenase activity in erythrocytes

Effect of Diabetes Mellitus on Mycophenolate Sodium Pharmacokinetics and Inosine Monophosphate Dehydrogenase Activity in Stable Kidney Transplant Recipients

Mizoribine Corrects Defective Nephrin Biogenesis by Restoring Intracellular Energy Balance

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