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Takatsuki, Japan

Shimizu T.,Gout Clinic | Kitada H.,Midorigaoka Hospital | Umeyama M.,Nippon Chemiphar Co. | Hori H.,Midorigaoka Hospital | Takasaki N.,Midorigaoka Hospital
Journal of Urology | Year: 2013

Purpose: We clarified whether the clinical profiles of patients with a history of urolithiasis (stone formers) truly reflect those of patients who currently have renal stones (stone carriers). Materials and Methods: We evaluated 463 patients with gout using helical computerized tomography, urolithiasis history and relevant clinical parameters. Results: Nephrolithiasis was observed in 157 of the 463 patients (34%) on helical computerized tomography but only 75 (16%) had a urolithiasis history. Of the 157 stone carriers 107 (68%) did not have a urolithiasis history. In those 157 patients serum urate and serum creatinine were higher than in the 306 nonstone carriers (p = 0.017), and the estimated glomerular filtration rate and urinary pH were lower (p = 0.0096 and 0.0249, respectively). However, there was no significant difference in laboratory findings between the 75 stone formers and 388 nonstone formers. Serum urate and creatinine were higher, and the estimated glomerular filtration rate and urine pH in bilateral stone carriers were lower than in unilateral stone carriers. According to HU density attenuation values on computerized tomography, an estimated third of the calculi that complicated 31 recent gout cases was uric acid. Conclusions: The concept of stone formers may lead to underestimating the prevalence of urolithiasis. Our analysis of stone carriers showed that a higher stone burden is associated with greater renal derangement, as determined by serum urate and creatinine, the estimated glomerular filtration rate and urine pH. To accurately clarify the correlation of gout and urolithiasis, it is advantageous to select stone carriers as subjects of study. © 2013 American Urological Association Education and Research, Inc.

Ochi Y.,Research Institute for Production Development | Kajita Y.,Nantan General Hospital | Hachiya T.,Midorigaoka Hospital | Hamaoki M.,Yamasa Ltd.
Endocrine Journal | Year: 2012

Previously we reported neutralization and partial purifcation of TSAb and TBAb activity using heterophilic antibody (Ab) to animal IgG from Graves' disease. Thus, we examined immunological similarity of TSAb and TBAb with animal IgG using experimentally generated anti-animal IgG [dog (d), bovine (b), porcine (p) and rabbit (rb)] Abs. TBII activity of TSAb- and TBAb-positive serum was neutralized by these anti-animal IgG Abs. Applied TSAb- or TBAb-IgG protein (purifed by Protein A) on these anti-animal IgG Abs-bound column was found mainly in the unbound fraction (UF) (>65%) and partially in the bound fraction (BF) (<35%). The TBII and TSAb activity of TSAb-IgG in the BF showed signifcantly higher than the UF. Thus, the ratio of TBII activity (U/L)/mg protein in the BF/UF was high. TBII activity of TBAb-IgG was similarly purifed by this column. We examined immunological characteristics of TSAb- and TBAb-Fab or F(ab') 2 using goat anti-bF(ab') 2 Ab. TBII and TSAb activity of TSAb-Fab or- F(ab') 2 and TBII activity of TBAb-Fab or -F(ab') 2 were neutralized by anti-bF(ab') 2 Ab. Partial purifcation of TSAb- or TBAb-Fab and -F(ab') 2 by anti-bF(ab') 2 Ab-bound column was also possible. Immunological similarity of TSAb- and TBAb-IgG with animal IgG such as d, b, p, rb by anti-animal IgG Ab, and TSAb- or TBAb-Fab and -F(ab') 2 with bFab by anti-bF(ab') 2 Ab were demonstrated. These facts suggest that both Fab and Fc portions of TSAb- and TBAb-IgG molecule have immunological similarity with animal IgG. © The Japan Endocrine Society.

Ichida K.,Tokyo University of Pharmacy and Life Science | Ichida K.,Jikei University School of Medicine | Matsuo H.,National Defense Medical College | Takada T.,University of Tokyo | And 23 more authors.
Nature Communications | Year: 2012

ABCG2, also known as BCRP, is a high-capacity urate exporter, the dysfunction of which raises gout/hyperuricemia risk. Generally, hyperuricemia has been classified into urate 'overproduction type' and/or 'underexcretion type' based solely on renal urate excretion, without considering an extra-renal pathway. Here we show that decreased extra-renal urate excretion caused by ABCG2 dysfunction is a common mechanism of hyperuricemia. Clinical parameters, including urinary urate excretion, are examined in 644 male outpatients with hyperuricemia. Paradoxically, ABCG2 export dysfunction significantly increases urinary urate excretion and risk ratio of urate overproduction. Abcg2-knockout mice show increased serum uric acid levels and renal urate excretion, and decreased intestinal urate excretion. Together with high ABCG2 expression in extra-renal tissues, our data suggest that the 'overproduction type' in the current concept of hyperuricemia be renamed 'renal overload type', which consists of two subtypes-'extra-renal urate underexcretion' and genuine 'urate overproduction'-providing a new concept valuable for the treatment of hyperuricemia and gout. © 2012 Macmillan Publishers Limited. All rights reserved.

Ochi Y.,Research Institute for Production Development | Kajita Y.,Nantan General Hospital | achiya T.,Midorigaoka Hospital | amaoki M.,Yamasa Ltd.
Endocrine Journal | Year: 2012

There are several reports that sera from Graves' patients contain heterophilic antibody (Ab) to animal IgG such as human anti-mouse antibody (HAMA). We examined the binding of TSAb and TBAb with heterophilic Ab. The binding of animal IgG with patient's IgG was examined by the inhibition of animal IgG on the binding of labeled bovine (b) IgG with patient's IgG. The binding to labeled bIgG was detected in the serum of 5 patients (2.7%) among 185 patients with Graves' disease. The binding of the labeled bIgG with patient's IgG was inhibited by animal serum or the crude IgG (45% ammonium sulfate fraction of serum) (such as dog, horse, bovine, porcine, goat, ovine, rabbit, guinea-pig, rat, mouse) except human, monkey and chick. This heterophilic Ab which had cross-reaction with mammalian IgG (except human, monkey) was used as human anti-animal IgG Ab. TBII and TSAb activity of TSAb-positive serum, and TBII activity of TBAb-positive serum were neutralized by incubation with this Ab-bound column. Partial purifcation of TSAb- or TBAb-IgG from Protein A-purifed TSAb- or TBAb-IgG was possible using this Ab-bound column. TBII and TSAb activity of TSAb-IgG and TBII activity of TBAb-IgG were neutralized by incubation with rabbit anti-human (h) IgG Ab (having cross-reaction with animal IgG). Further purification of Protein A-purifed TSAb-IgG or TBAb-IgG by rabbit anti-hIgG Ab-bound column was impossible. The binding of TSAb and TBAb with heterophlic Ab means that TSAb-and TBAb-specifc IgG have immunological similarity with mammalian species IgG compared to human IgG. © The Japan Endocrine Society.

Sakiyama M.,National Defense Medical College | Matsuo H.,National Defense Medical College | Shimizu S.,National Defense Medical College | Nakashima H.,National Defense Medical College | And 10 more authors.
Drug Metabolism and Pharmacokinetics | Year: 2014

Gout, a common disease, is a consequence of hyperuricemia, and increases the risks of hypertension, cardiovascular diseases, cerebrovascular diseases and renal failure. Gout can be classified into 3 types: the renal underexcretion (RUE) type, renal overload type and combined type. RUE type is a major type of gout; however, its genetic causes are still unclear. Since human organic anion transporter 4 (OAT4/SLC22A11) is expressed in the kidney and mediates urate transport, we investigated the effects of a common variant of OAT4/SLC22A11 on the susceptibility to gout. Five hundred and forty-five Japanese male gout cases and 1,115 male individuals as a control group were genotyped with rs17300741, a single nucleotide polymorphism in the OAT4/SLC22A11 gene. The association analysis of rs17300741 showed no significant association for all gout cases; however, there was a slight but significant association for RUE type gout cases (p = 0.049). These results also suggest that OAT4 contributes to urate transport at the apical membrane of renal proximal tubule cells in humans. Our findings make it clear for the first time that a common variant of OAT4/SLC22A11 is associated with RUE type gout, a major gout subtype. Copyright © 2014 by the Japanese Society for the Study of Xenobiotics (JSSX).

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