Adenine-related compounds modulate UDP-glucuronosyltransferase (UGT) activity in mouse liver microsomes

Xenobiotica ◽  
2021 ◽  
pp. 1-25
Author(s):  
Shoji Nakamura ◽  
Ryohei Yamashita ◽  
Yuu Miyauchi ◽  
Yoshitaka Tanaka ◽  
Yuji Ishii
Keyword(s):  
Mouse Liver ◽  
Liver Microsomes ◽  
Udp Glucuronosyltransferase ◽  
Related Compounds

scholarly journals Metabolism of 20-hydroxyvitamin D3 by mouse liver microsomes

2014 ◽  
Vol 144 ◽  
pp. 286-293 ◽  
Author(s):  
Chloe Y.S. Cheng ◽  
Andrzej T. Slominski ◽  
Robert C. Tuckey
Keyword(s):  
Mouse Liver ◽  
Liver Microsomes

scholarly journals Identifying Metabolic Pathways of c‐MET Tyrosine Kinase Inhibitor Tepotinib in Human and Mouse Liver Microsomes

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1 ◽  
Author(s):  
Feng Li ◽  
Kevin R. MacKenzie ◽  
Pranavanand Nyshadham ◽  
Kimberly A. Kerlec ◽  
Martin M. Matzuk
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Kinase Inhibitor ◽  
Metabolic Pathways ◽  
Mouse Liver ◽  
Kinase Inhibitor ◽  
Liver Microsomes ◽  
Human And Mouse

scholarly journals Design, Synthesis, and Evaluation of Potential Carbamate Prodrugs of 5′-methylthioadenosine (MTA)*

2021 ◽  
Author(s):  
Ashwini Sadanand Ranade ◽  
Joseph R Bertino ◽  
Longqin Hu
Keyword(s):  
Solid Tumors ◽  
Tumor Cells ◽  
Phosphate Buffer ◽  
Mouse Liver ◽  
Therapeutic Strategy ◽  
Liver Microsomes ◽  
Hematologic Malignancies ◽  
Natural Substrate ◽  
Salvage Pathway ◽  
Design Synthesis

Abstract 5′-Methylthioadenosine (MTA) is a natural substrate of MTA phosphorylase (MTAP) and is converted to adenine via a salvage pathway for AMP production in normal healthy cells. The lack of MTAP expression in many solid tumors and hematologic malignancies compared to normal healthy cells has been explored in a potential therapeutic strategy to selectively target tumor cells using antimetabolites such as 5-fluorouracil (5-FU) and 6-thioguanine (6-TG) while protecting normal healthy cells with MTA. Herein, a series of carbamate prodrugs, namely the N-(alkyloxy)carbonyl-MTA derivatives 2a-f, was designed, synthesized, and evaluated as potential prodrugs of MTA. All carbamate prodrugs were stable in phosphate buffer, pH 7.4 at 37 °C. In the presence of mouse liver microsomes, the prodrugs were converted to MTA at varying rates with the hexyl and butyl carbamates 2a and 2b most readily activated (t1/2 of 1.2 and 9.4 h, respectively). The activation was shown to be mediated by carboxyesterases present in mouse liver microsomes.

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