Faculty Profiles - ARIYOSHI Noritaka

Papers - ARIYOSHI Noritaka

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Significant suppression of aldolase B, carbonic anhydrase III and alcohol dehydrogenase in liver cytosol of rats treated with a highly toxic coplanar PCB Reviewed

H Kato, Y Ishii, M Hatsumura, T Ishida, Nakayama, I, N Ariyoshi, K Oguri

JAPANESE JOURNAL OF TOXICOLOGY AND ENVIRONMENTAL HEALTH 43 ( 1 ) P20 - P20 1997.2

Significant suppression of rat liver aldolase B by a toxic coplanar polychlorinated biphenyl, 3,3',4,4',5-pentachlorobiphenyl

Y Ishii, H Kato, M Hatsumura, T Ishida, N Ariyoshi, K Oguri

TOXICOLOGY 116 ( 1-3 ) 193 - 199 1997.1

Language：English Publishing type：Research paper (scientific journal) Publisher：ELSEVIER SCI IRELAND LTD

A toxic coplanar polychlorinated biphenyl, 3,3',4,4',5-pentachlorobiphenyl (PenCB), significantly suppresses the expression of liver aldolase B in rats, Hepatic aldolase activity in PenCB-treated rats was significantly reduced to about 50% of that in free- and pair-fed control groups. The reduced aldolase activity following PenCB-treatment was due to the marked suppression of the expression of aldolase B shown by immunoblot analysis after SDS-polyacrylamide gel electrophoresis and two-dimensional gel electrophoresis. The suppression of rat liver aldolase B could be a key biochemical lesion caused by PenCB. Copyright (C) 1997 Elsevier Science Ireland Ltd.

DOI： 10.1016/S0300-483X(96)03543-3

Cytochrome P450scc in rat adrenal cells mediated by regulation of the steroidogenic acute regulatory protein

YC Kim, N Ariyoshi, Artemenko, I, ME Elliott, KK Bhattacharyya, CR Jefcoate

STEROIDS 62 ( 1 ) 10 - 20 1997.1

Language：English Publishing type：Research paper (scientific journal) Publisher：ELSEVIER SCIENCE INC

Cholesterol conversion to pregnenolone by cytochrome P450scc in steroidogenic cells, including those of the adrenal cortex is determined by hormonal control of cholesterol availability. Intramitochondrial cholesterol movement to P450scc, which retains hormonal activation in isolated mitochondria, is apparently dependent an peripheral benzodiazepine receptor and the recently cloned steroidogenic acute regulatory (SrARJ protein. In rat adrenal cells, StAR is formed as a 37-kDa precursor that is transferred to the mitochondrial inner membrane following phosphorylation by hormonally activated protein kinase A, and processed to multiple forms, some of which turn over very rapidly. In bovine cells, StAR undergoes three modifications for ming a set of eight proteins seen in both glomerulosa and fasciculata cells. In the former, cyclic AMP and angiotensin ii each decrease two forms and elevate six forms. Significantly, the major change seen after activation may not involve phosphorylation of StAR. Cholesterol transfer across mitochondrial membranes is also activated in isolated mitochondria by GTP and low concentrations of Ca2+, apparently prior to activation by StAR. Depletion of StAR by cyclohexmide inhibits cholesterol transfer but is overcome by uptake of Ca2+ into the matrix. This activation of cellular- cholesterol transport is sustained in adrenal cells pereabilized by Streptolysin 0. In rat adrenal cells cAMP elevates 3.5- and 1.6-kb mRNA, hybridized by a 1.O-kb StAR cDNA. A 3.5-kb rat adrenal cDNA that encodes all except the 5' end of the longest StAR mRNA has been characterized. The corresponding gene sequence is distributed across seven exons. The shorter mRNA may arise from polyadeylation signals early in exon 7. However, the 3.5-kb mRNA comprises 80-90% of untreated rat adrenal StAR mRNA and may therefore provide the prime source for in vivo translation of StAR protein. (C) 1997 by Elsevier Science, Inc.

DOI： 10.1016/S0039-128X(96)00153-5

Effect of co-planar polychlorinated biphenyl on the hepatic glutathione peroxidase redox system in rats and guinea pigs

M. Hori, N. Ariyoshi, H. Yamada, K. Oguri

Fukuoka Acta Medica 88 ( 5 ) 12 - 16 1997

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Kyushu University School of Medicine

The effect of 3,3',4,4',5-pentachlorobiphenyl (PCB 126) on hepatic glutathione peroxidase (GPx) redox system was studied in vivo in rats and guinea pigs. PCB 126 treatment caused significant reduction of Se-dependent and -non-dependent GPx activity in rats. In agreement with this, the content of glutathione (GSH) and the activities of GSH reductase (GR) and γ-glutamyl transpeptidase (γ-GTP) were also decreased in this species. On the contrary, guinea pig liver Se-non-dependent GPx activity was significantly enhanced by PCB 126 treatment, while no effect on Se-dependent activity was observed. Neither the content of GSH nor the enzyme activities responsible for GSH supply in guinea pig liver was affected by PCB 126. These result suggested that the damage on GPx redox system is, at least, one of mechanisms by which co-planar PCB induces the toxicity in rats. However, in guinea pigs, this is not the case, and different mechanism from the damage on active oxygen quenching system is likely to be involved.

Metabolism of 2,4,5,2',4',5'-hexachlorobiphenyl (PCB153) in guinea pig Reviewed

N. Ariyoshi, N. Koga, H. Yoshimura, K. Oguri

Xenobiotica 27 ( 9 ) 973 - 983 1997

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal)

1. The in vitro and vivo metabolism of 2,4,5,2',4',5'-hexachlorobiphenyl (PCB153) in guinea pig has been studied. 2. Seven metabolites were detected in the faeces of PCB153-treated animals and three were identical to those produced by dog liver microsomes. The detection of a metabolite where a chlorine atom was shifted from the 2- to 3-position strongly suggested the involvement of 2,3-arene oxide intermediate, and evidence for the concomitant formation of a 3,4-arene oxide intermediate was provided by identifying other two minor metabolites which were dechlorinated at the 4-position. 3. In vitro studies using liver microsomes from guinea pigs revealed that the 2,3-arene oxide and 5-hydroxylation pathways are the predominant metabolic routes compared with the 3,4-arene oxide pathway. Although the guinea pig is an another species that can metabolize PCB153 mainly to the 2,3-arene oxide intermediate, the rate of formation was only about one-tenth of the dog. 4. These results indicate that the ability to form this unusual 2,3-arene oxide intermediate may not be responsible for high excretion rate of this congener. Our data also suggest that the cytochrome P450-catalysed metabolism of PCB153 in the guinea pig and dog are similar, whereas for post-cytochrome P450 metabolism, the guinea pig resembles the rabbit.

DOI： 10.1080/004982597240136

Production of antibody against cytosolic 54kDa protein in rat liver evidence of the significant induction by a highly toxic coplanar polychlorinated biphenyl

T. Ishida, Y. Ishii, K. Tasaki, N. Ariyoshi, K. Oguri

Fukuoka Acta Medica 88 ( 5 ) 3 - 11 1997

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Kyushu University School of Medicine

We have reported that a 54kDa protein in rat liver cytosol is highly inducible by treatment with 3,3',4,4',5-pentachlorobiphenyl (PenCB) or 3- methylcholanthrene (MC) using SDS-polyacrylamide gel electrophoresis. Internal amino acid sequences of this protein in the rat liver were highly homologous to those of selenium binding protein (SeBP) or acetaminophen binding protein (APBP) in mouse liver cytosol. In this paper, the purification and characterization of this protein were demonstrated MC was given at a dose of 20 mg/kg for 3 consecutive days. The liver cytosolic 54kDa protein was purified twice from the MC-treated male Wistar rats by Rotofore Cell(TM) procedure to apparent single on SDS-polyacrylamide gel electrophoresis, and the rabbit antiserum against this protein was obtained. Male Wistar rats were given PenCB in corn oil at a single dose of 25 mg/kg i.p. The liver cytosol was prepared on the 5th day after the treatment and subjected to immunoblot analysis. The 54kDa protein was markedly induced in the liver cytosol of PenCB-treated rats. Immunoblot analysis after two- dimensional gel electrophoresis suggested that there could be isoforms of 54kDa protein. The induction of the 54kDa protein with PenCB was assumed to be mediated through Ah-receptor. The physiological role of the 54kDa protein was discussed together with SeBP and APBP, the role of which has not yet been elucidated.

Significant induction of a 54-kDa protein in rat liver with homologous alignment to mouse selenium binding protein by a coplanar polychlorinated biphenyl, 3,4,5,3',4'-pentachlorobiphenyl and 3-methylcholanthrene

Y Ishii, M Hatsumura, T Ishida, N Ariyoshi, K Oguri

TOXICOLOGY LETTERS 87 ( 1 ) 1 - 9 1996.9

Language：English Publishing type：Research paper (scientific journal) Publisher：ELSEVIER SCI IRELAND LTD

A 54-kDa protein in rat liver cytosol was significantly induced by treatment with 3,4,5,3',4'-pentachlorobiphenyl (25 mg/kg, single i.p.) and 3-methylcholanthrene (20 mg/kg, once a day for 3 days, i.p.). The protein exhibited pi of 6.8 on two-dimensional gel electrophoresis. The amino acid sequences of peptide fragments from the protein digested in situ were highly similar to a selenium binding protein in mice and to the isoform acetaminophen binding protein in mice. The present result clearly demonstrates that a coplanar polychlorinated biphenyl and 3-methylcholanthrene are responsible for induction of selenium binding protein homologues. The physiological role of the mouse proteins, however, is not yet elucidated.

DOI： 10.1016/0378-4274(96)03668-5

Hamster liver cytochrome P450 (CYP2A8) as a 4-hydroxylase for 2,5,2',5'-tetrachlorabiphenyl Reviewed

N Koga, N Kikuichi, T Kanamaru, N Ariyoshi, K Oguri, H Yoshimura

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 225 ( 2 ) 685 - 688 1996.8

Language：English Publishing type：Research paper (scientific journal) Publisher：ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS

Metabolism of 2,5,2',5'-tetrachlorobiphenyl (TCB) was studied using liver microsomes of hamsters and two hamster P450 isoforms, CYP1A2 and 2A8. CYP2A8 catalyzed selectively 4-hydroxylation of 2,5,2',5-TCB at a rate of 21.7 pmol/min/nmol P450. In contrast, CYP1A2 showed no activity for hydroxylation of 2,5,2',5'-TCB. Immunological study revealed that rabbit antiserum against CYP2A8 almost completely inhibited the microsomal 4-hydroxylation but that against CYP1A2 did not. It was also shown that the induction pattern of CYP2A8 protein by P450 inducer was similar to that of the 4-hydroxylase activity in hamster liver microsomes. These results suggest that CYP2A8 plays a major role in the 4-hydroxylation of 2,5,2',5'-TCB in hamster liver. (C) 1996 Academic Press, Inc.

A coplanar PCB induces a selenium binding protein as a major cytosolic protein in rat liver

Y Ishii, M Hatsumura, T Ishida, N Ariyoshi, K Oguri

CHEMOSPHERE 32 ( 3 ) 509 - 515 1996.2

Language：English Publishing type：Research paper (scientific journal) Publisher：PERGAMON-ELSEVIER SCIENCE LTD

We obtained evidence that a toxic coplanar polychlorinated biphenyl (PCB) induces a counterpart of murine 56kDa selenium binding protein in rat liver cytosol. A 54kDa protein in the liver cytosol was significantly induced by 3,3',4,4',5-pentachlorobiphenyl and proved to be a major cytosolic protein in the rat liver. The protein exhibited pi of 6.8 on two-dimensional gel electrophoresis. The amino acid sequence of peptide fragments from the protein digested in situ, was highly similar to a 56kDa selenium binding protein and similar to an acetaminophen binding protein in mice.

DOI： 10.1016/0045-6535(95)00316-9

Involvement of cytochrome b(5) in the metabolism of tetrachlorobiphenyls catalyzed by CYP2B1 and CYP1A1

K Matsusue, N Ariyoshi, K Oguri, N Koga, H Yoshimura

CHEMOSPHERE 32 ( 3 ) 517 - 523 1996.2

Language：English Publishing type：Research paper (scientific journal) Publisher：PERGAMON-ELSEVIER SCIENCE LTD

The role of cytochrome b(5) in the cytochrome P450 (CYP)-dependent hydroxylation of tetrachlorobiphenyl (TCB) isomers was examined using a reconstituted mixed function oxygenase (MFO) system containing purified CYP2B1 or 1A1, and rat liver microsomes. Hydroxylations of 2,2',5,5'- and 3,3',4,4'-TCBs were catalyzed mainly by CYP2B1 and 1A1, respectively, in the reconstituted MFO system and those of 2,3',4',5- and 2,3',4,4'-TCBs were mediated by both cytochrome P450 systems. The activity toward 2,2',5,5'- and 2,3',4',5-TCB was significantly increased 6.5- and 5.5-fold, respectively, by addition of cytochrome b, in the reconstituted MFO system containing of CY2B1. Either hydroxylation activity toward 2,3',4,4'-TCB with the CYP2B1 system was very low or decreased by addition of cytochrome b(5). These results suggest that the involvement of cytochrome b(5) to the hydroxylation of TCBs is dependent on the TCB congener being metabolized, and the cytochrome P450 isoform involved in its metabolism.

DOI： 10.1016/0045-6535(95)00318-5

METABOLISM OF HIGHLY PERSISTENT PCB CONGENER, 2,4,5,2',4',5'-HEXACHLOROBIPHENYL, BY HUMAN CYP2B6

N ARIYOSHI, K OGURI, N KOGA, H YOSHIMURA, Y FUNAE

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 212 ( 2 ) 455 - 460 1995.7

Language：English Publishing type：Research paper (scientific journal) Publisher：ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS

Metabolism of 2,4,5,2',4',5'-hexachlorobiphenyl was studied with cDNA-expressed human P450 2B isoform, CYP2B6. 3-Hydroxy-2,4,5,2',4',5'-hexachlorobiphenyl was identified as a major metabolite, and the formation activity was compared with that of dog CYP2B11 and guinea pig P450(GP-1). The activity of 3-hydroxylation was comparable with that of P450(GP-1), but one-tenth of CYP2B11. These results indicate that P450 2B in humans as well as other animal species can metabolize 2,4,5,2',4',5'-hexachlorobiphenyl, and the reason why this PCB congener remained most abundantly in human bodies is discussed. (C) 1995 Academic Press, Inc.

DOI： 10.1006/bbrc.1995.1991

EFFECT OF HIGHLY TOXIC COPLANAR PCB ON PEROXISOMAL ENZYME-ACTIVITY - THE SPECIES-DIFFERENCE BETWEEN RATS AND GUINEA-PIGS Reviewed

M IWASAKI, H KATO, N ARIYOSHI, K OGURI

JAPANESE JOURNAL OF TOXICOLOGY AND ENVIRONMENTAL HEALTH 41 ( 1 ) P32 - P32 1995.2

Effect of a coplanar PCB on lipid metabolism ; The remarkable difference between rats and Guinea pigs(共著)

Fukuoka Acta Media 86 ( 5 ) 135 1995

Alteration of perixosomal enzyme activities in the liver of guinea pigs caused by coplanar PCB

M. Iwasaki, H. Kato, N. Ariyoshi, K. Oguri

Fukuoka Acta Medica 86 ( 5 ) 12 - 20 1995

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Kyushu University School of Medicine

The hyperlipidemia is a well-known typical symptom in Yusho patients and experimental animals treated with PCBs. We have found a significant induction of CYP4A1, which catalyzes ω-hydroxylation of fatty acids, in guinea pigs by the treatment with a coplanar PCB, 3,4,5,3',4'-pentachlorobiphenyl (PenCB), though the P450 is reduced in the treated rats. Peroxisome has β-oxidation enzymes distinct from mitochondrial enzymes, and also play an important role in lipid metabolism. Peroxisome proliferators have been shown to regulate the expression of CYP4A1 and peroxisomal enzymes by the same mechanism in the rat. In the present study, we examined the effect of PenCB treatment on peroxisomal enzymes in the liver of guinea pigs. As a result, the enzyme activities of hepatic peroxisome, e.g. fatty acid oxidizing system, catalase and urate oxidase, had a rising tendency by the treatment with PenCB in the animal. The results suggest that the regulation of peroxisomal enzymes and CYP4A1 is also associated in guinea pigs, and PenCB provides a similar effect of peroxisomal proliferators to the animal. The possible toxicity through the peroxisomal alteration was discussed.

Studies on PCB toxicity involving 2C subfamily cytochrome P450

N. Ariyoshi, S. Ito, A. Okudaira, M. Mise, K. Matsusue, H. Yamada, K. Oguri

Fukuoka Acta Medica 86 ( 5 ) 21 - 30 1995

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Kyushu University School of Medicine

It has been demonstrated that PCB metabolism is mainly catalyzed by 1A and 2B subfamily cytochrome P450s, CYP 1A1/2 and CYP 2B1/2. These studies were conducted mostly with hepatic enzymes in rodents. The 1A and 2B subfamily P450s are constitutively expressed little, but markedly induced by xenobiotics such as 3-methylcholanthrene and phenobarbital in rodents. On the other hand, the recent studies showed that cytochrome P450s in human liver are remarkably different from isoform of rodents in constitution and enzyme activities. In the present study, we first tried to metabolize some PCBs with 2C subfamily cytochrome P450 (CYP2C) purified from dog liver microsomes. The data suggested that CYP2C may not be involved in PCB metabolism. Since CYP2C is the same most abundant enzyme as 3A subfamily P450 in human liver and plays a major role for metabolism of many drugs used clinically, and may also play an important role for metabolism of some steroid hormones, we further studied the inhibition of CYP2C-catalyzed steroid metabolism by typical PCB congeners. CYP2C-mediated steroid metabolism is greatly inhibited by 2,4,5,2',4',5'-hexachlorobiphenyl, but not by 3,4,5,3',4'-pentachlorobiphenyl. On the contrary, 3,4,5,3',4'-pentachlorobiphenyl markedly suppressed CYP2C expression in the dog liver. These results suggest that residual PCBs may affect the current situation of steroid hormones in Yusho patients, and may cause PCB-drug interactions.

PURIFICATION AND CHARACTERIZATION OF DOG LIVER MICROSOMAL EPOXIDE HYDROLASE Reviewed

N ARIYOSHI, M TANAKA, Y ISHII, K OGURI

JOURNAL OF BIOCHEMISTRY 115 ( 5 ) 985 - 990 1994.5

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：JAPANESE BIOCHEMICAL SOC

An epoxide hydrolase (mEH) in liver microsomes was purified to apparent homogeneity from a dog treated with phenobarbital. The purified enzyme had a minimum molecular weight of 47,000 as determined by SDS-PAGE. The dog mEH activity was characterized by use of a substrate, 7-glycidoxycoumarin (GOC), and some effecters of this enzyme. In vitro activators, metyrapone, and isoquinoline, stimulated the microsomal activity, but the former had no such effect on the purified enzyme in case of this substrate. All mEH inhibitors, 1,1,1-trichloropropene 2,3-oxide (TCPO), cyclohexene oxide, and 2-bromo-4'-nitroacetophenone (BrNAP), suppressed hydrolase activity. The NH2-terminal amino acid sequence of the purified enzyme was highly homologous (90%) to the sequences deduced from a cDNA clone of rat enzyme. Antiserum to the purified enzyme raised in rabbits cross-reacted with rat and guinea pig epoxide hydrolases. No gender-difference in this enzyme in liver microsomes was observed in dogs.

EFFECT OF COPLANAR PCB ON GLUCONEOGENESIS AND LIPID-METABOLISM - COMPARISON BETWEEN RATS AND GUINEA-PIGS Reviewed

M HATSUMURA, T ISHIDA, Y ISHII, N ARIYOSHI, Y KOGA, K OGURI, H YOSHIMURA

JAPANESE JOURNAL OF TOXICOLOGY AND ENVIRONMENTAL HEALTH 40 ( 1 ) P27 - P27 1994.2

INDUCTION OF BILIRUBIN UDP-GLUCURONOSYLTRANSFERASE AND CYP4A1 P450 BY COPLANAR PCBS - DIFFERENT RESPONSIVENESS OF GUINEA-PIGS AND RATS

Y KOGA, M TSUDA, N ARIYOSHI, Y ISHII, H YAMADA, K OGURI, Y FUNAE, H YOSHIMURA

CHEMOSPHERE 28 ( 3 ) 639 - 645 1994.2

Language：English Publishing type：Research paper (scientific journal) Publisher：PERGAMON-ELSEVIER SCIENCE LTD

Induction of hepatic microsomal bilirubin UDP-glucuronyltransferase and CYP4A1 P450 by 3,4,3',4'-tetrachlorobiphenyl (TCB) and 3,4,5,3',4'-pentachlorobiphenyl (PenCB) was studied in guinea pigs and rats. Both enzyme activities in guinea pigs were increased 4-fold or more over the control by PenCB treatment, while by treatment with a less toxic congener, TCB, these were increased to a lesser extent. On the contrary, the rat enzymes were significantly decreased by treatment with these co-planar polychlorinated biphenyls. These results suggest that the alterations of both bilirubin UDP-glucuronyltransferase and CYP4A P450 are the characteristic indices for the toxicities of polychlorinated hydrocarbons.

DOI： 10.1016/0045-6535(94)90305-0

MODIFICATION OF THE GLUCONEOGENESIS IS NOT INVOLVED IN THE COPLANAR PCB TOXICITY IN HIGHLY SENSITIVE GUINEA-PIGS Reviewed

K OGURI, M HATSUMURA, Y ISHII, Y KOGA, N ARIYOSHI, H YOSHIMURA

CHEMOSPHERE 27 ( 11 ) 2295 - 2303 1993.12

Language：English Publishing type：Research paper (scientific journal) Publisher：PERGAMON-ELSEVIER SCIENCE LTD

Effect of a co-planar PCB, 3,4,5,3',4'-pentachlorobiphenyl (PenCB) on gluconeogenesis in guinea pigs was compared with that in rats. The key enzyme of gluconeogenesis, phosphoenolpyruvate carboxykinase (PEPCK), in liver cytosol of rats was reduced by PenCB treatment to about 50% of control level. Hypoglycemia was also seen in the rat. On the contrary, the liver cytosol PEPCK activity in guinea pigs was slightly increased by PenCB treatment. Plasma levels of alanine and tryptophan were increased in the rat treated with PenCB, but the level of glycogenic amino acid, alanine, was not raised significantly-in the guinea pig. Thus the modification of the gluconeogenesis was not involved in the PenCB toxicity in highly sensitive guinea pigs.

DOI： 10.1016/0045-6535(93)90140-Z

IDENTIFICATION OF IN-VITRO METABOLITES OF 2,4,6,2',4',6'-HEXACHLOROBIPHENYL FROM PHENOBARBITAL-TREATED DOG LIVER-MICROSOMES Reviewed

N ARIYOSHI, H YOSHIMURA, K OGURI

BIOLOGICAL & PHARMACEUTICAL BULLETIN 16 ( 9 ) 852 - 857 1993.9

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：PHARMACEUTICAL SOC JAPAN

We studied in vitro metabolites of 2,4,6,2',4',6'-hexachlorobiphenyl (HCB, IUPAC PCB No. 155) produced by liver microsomes of a phenobarbital (PB)-treated beagle dog. The major metabolites were 3-hydroxy-2,4,6,2',4',6'-HCB (M-1), 4-hydroxy-2,6,2',4',6'-pentachlorobiphenyl (PenCB, M-2) and 3,4-dihydroxy-2,6,2',4',6'-PenCB (M-3). Furthermore, 4-hydroxy-2,3,6,2',4',6'-HCB (M4), which could be formed via the 3,4-epoxidation and the subsequent NIH-shift of the chlorine from the 4 to the 3 position, was also detected. We found that M-3 is a common secondary metabolite of the two major monohydroxy metabolites, M-1 and M-2. These results indicate that the dog seems to metabolize and eliminate this congener not only by a mechanism involving direct insertion of a hydroxyl group but also via an arene oxide intermediate.

DOI： 10.1248/bpb.16.852

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