Comparison of the Inhibition Capability of Baicalin and Baicalein towards Intestinal UDP-Glucuronosyltransferase (UGT) 1A10

被引：0

作者：

Gong, Hong-Yan ^{[1
]}

Cheng, Wei-Cai ^{[1
]}

Wang, Yong ^{[1
]}

Wan, Yong ^{[1
]}

Niu, Jun ^{[1
]}

机构：

[1] Yantaishan Hosp, Yantai, Shandong, Peoples R China

来源：

LATIN AMERICAN JOURNAL OF PHARMACY | 2013年 / 32卷 / 04期

关键词：

Baicalein; Baicalin; UDP-glucuronosyltransferases (UGTs); UGT1A10; GLUCURONIDATION; METABOLISM; RALOXIFENE; LIVER; RATS;

D O I：

暂无

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Baicalin, the important flavonoid component isolated from Scutellariae radix, has been demonstrated to exhibit multiple pharmacological activities, and its anti-tumor activity has been drawing more and more attention in recent years: Baicalin can be metabolized into baicalein in intestine. The present study aims to compare the inhibition capability of baicalin and baicalein towards the specific intestinal drug metabolizing enzyme UDP-glucuronosyltransferase (UGT) 1A10. Baicalein showed stronger inhibition than baicalin towards UGT1A10, with the residual activity to be 46.5 and 5.5% of control activity for 100 mu M of baicalin and baicalein, respectively. Noncompetitive inhibition was demonstrated for the inhibition of baicalein towards UGT1A10, and the inhibition kinetic parameter (K-i) was calculated to be 8.1 mu M. All these results showed the stronger inhibition capability of baicalin than baicalein towards intestinal UDP-glucuronosyltransferase (UGT) 1A10.

引用

页码：610 / 612

页数：3

共 50 条

[21] Inhibition potential of glimepiride (gli) towards important UDP-glucuronosyltransferase (UGT) isoforms in human liver
Fu, Jian-Fang
Ren, Qin-You
Zhang, Nan-Yan
Gao, Bin
Tu, Yan-Yang
Fu, Guo-Qiang
Li, Dao-Hai
Zhang, Yong-Sheng
PHARMAZIE, 2012, 67 (08): : 715 - 717
[22] Structure-inhibition relationship of podophyllotoxin (PT) analogues towards UDP-glucuronosyltransferase (UGT) isoforms
Qi, Jia-Qi
Cao, Yun-Feng
Sun, Xiao-Yu
Hong, Mo
Fang, Zhong-Ze
Meng, Da-Li
Sun, Dong-Xue
PHARMAZIE, 2015, 70 (04): : 239 - 243
[23] Identification of UDP-glucuronosyltransferase 1A10 in non-malignant and malignant human breast tissues
Starlard-Davenport, Athena
Lyn-Cook, Beverly
Radominska-Pandya, Anna
STEROIDS, 2008, 73 (06) : 611 - 620
[24] Oligomerization and Catalytic Parameters of Human UDP-Glucuronosyltransferase 1A10: Expression and Characterization of the Recombinant Protein
Kim, Kyungbo
Zheng, Fang
Zhan, Chang-Guo
DRUG METABOLISM AND DISPOSITION, 2018, 46 (10) : 1446 - 1452
[25] Inhibition of UDP-glucuronosyltransferase (UGT) enzymes by protein kinase C inhibitors
Volak, Laurie P.
Court, Michael H.
FASEB JOURNAL, 2008, 22
[26] In vitro stereoselective inhibition of ginsenosides toward UDP-glucuronosyltransferase (UGT) isoforms
Kim, Doyun
Zheng, Yu Fen
Min, Jee Sun
Park, Jung Bae
Bae, Soo Hyeon
Yoon, Kee Dong
Chin, Young-Won
Oh, Euichaul
Bae, Soo Kyung
TOXICOLOGY LETTERS, 2016, 259 : 1 - 10
[27] Influence of Anti-Tumor Drugs Praeruptorins A and B Towards Intestinal UDP-Glucuronosyltransferase (UGT) 1A7
Liu, Sheng
Liu, Xiao-Gang
Wang, Tao
Tan, Gui-Ping
LATIN AMERICAN JOURNAL OF PHARMACY, 2016, 35 (06): : 1292 - 1296
[28] IN VITRO EVALUATION OF UDP-GLUCURONOSYLTRANSFERASE (UGT) 1A3 AND UGT2B4 INHIBITION
Lapham, Kimberly
Ferguson, Nicholas
Novak, Jonathan
Niosi, Mark
Goosen, Theunis
DRUG METABOLISM AND PHARMACOKINETICS, 2020, 35 (01) : S52 - S53
[29] Dopamine Is a Low-Affinity and High-Specificity Substrate for the Human UDP-Glucuronosyltransferase 1A10
Itaaho, Katriina
Court, Michael H.
Uutela, Paivi
Kostiainen, Risto
Radominska-Pandya, Anna
Finel, Moshe
DRUG METABOLISM AND DISPOSITION, 2009, 37 (04) : 768 - 775
[30] 20(S)-Protopanaxatriol (Ppt) Exhibits Inhibition Towards UDP-Glucuronosyltransferase (UGT)-Catalyzed Zidovudine Glucuronidation
Xing, Jin
Che, Wen
LATIN AMERICAN JOURNAL OF PHARMACY, 2012, 31 (04): : 628 - 631

← 1 2 3 4 5 →