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Article ; Online: Synthesis of carbon-14, carbon-13 and deuterium labeled forms of thioacetamide and thioacetamide

Sarma, Diganta / Hanzlik, Robert P

Journal of labelled compounds & radiopharmaceuticals

2011 Volume 54, Issue 13, Page(s) 795–798

Abstract: Thioacetamide (TA) is a model hepatotoxin that undergoes metabolic activation via two ... ...

Abstract	Thioacetamide (TA) is a model hepatotoxin that undergoes metabolic activation via two successive
Language	English
Publishing date	2011-11
Publishing country	England
Document type	Journal Article
ZDB-ID	196095-7
ISSN	1099-1344 ; 0362-4803 ; 0022-2135
ISSN (online)	1099-1344
ISSN	0362-4803 ; 0022-2135
DOI	10.1002/jlcr.1933
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Article ; Online: Human oncoprotein Musashi-2 N-terminal RNA recognition motif backbone assignment and identification of RNA-binding pocket.

Lan, Lan / Xing, Minli / Douglas, Justin T / Gao, Philip / Hanzlik, Robert P / Xu, Liang

Oncotarget

2017 Volume 8, Issue 63, Page(s) 106587–106597

Abstract: RNA-binding protein Musashi-2 (MSI2) is a key regulator in stem cells, it is over-expressed in a variety of cancers and its higher expression is associated with poor prognosis. Like Musashi-1, it contains two N-terminal RRMs (RNA-recognition Motifs, also ...

Abstract	RNA-binding protein Musashi-2 (MSI2) is a key regulator in stem cells, it is over-expressed in a variety of cancers and its higher expression is associated with poor prognosis. Like Musashi-1, it contains two N-terminal RRMs (RNA-recognition Motifs, also called RBDs (RNA-binding Domains)), RRM1 and RRM2, which mediate the binding to their target mRNAs. Previous studies have obtained the three-dimensional structures of the RBDs of Musashi-1 and the RBD1:RNA complex. Here we show the binding of MSI2-RRM1 to a 15nt
Language	English
Publishing date	2017-12-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.22540
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Article ; Online: Bioinformatic analysis of 302 reactive metabolite target proteins. Which ones are important for cell death?

Hanzlik, Robert P / Koen, Yakov M / Fang, Jianwen

Toxicological sciences : an official journal of the Society of Toxicology

2013 Volume 135, Issue 2, Page(s) 390–401

Abstract: Many low molecular weight compounds undergo biotransformation to chemically reactive metabolites (CRMs) that covalently modify cellular proteins. However, the mechanisms by which this covalent binding leads to cytotoxicity are not understood. Prior ... ...

Abstract	Many low molecular weight compounds undergo biotransformation to chemically reactive metabolites (CRMs) that covalently modify cellular proteins. However, the mechanisms by which this covalent binding leads to cytotoxicity are not understood. Prior analyses of lists of target proteins sorted by functional categories or hit frequency have not proven informative. In an attempt to move beyond covalent binding, we hypothesized that xenobiotic posttranslational modification of proteins might disrupt important protein-protein interactions (PPIs) and thereby direct cells from homeostasis into cell death pathways. To test this hypothesis, we analyzed a list of 302 proteins (66% rat, 26% mouse, 5% human) known to be targeted by 41 different cytotoxic CRMs. Human orthologs of rodent proteins were found by blast sequence alignment, and their interacting partners were found using the Human Protein Reference Database. The combined set of target orthologs and partners was sorted into KEGG pathways and Gene Ontology categories. Those most highly ranked based on sorting statistics and toxicological relevance were heavily involved with intracellular signaling pathways, protein folding, unfolded protein response, and regulation of apoptosis. Detailed examination revealed that many of the categories were flagged primarily by partner proteins rather than target proteins and that a majority of these partners interacted with just a small number of proteins in the CRM target set. A similar analysis performed without the partner proteins flagged very few categories as significant. These results support the hypothesis that disruption of important PPIs may be a major mechanism contributing to CRM-induced acute cytotoxicity.
MeSH term(s)	Animals ; Cell Death ; Computational Biology ; Humans ; Mice ; Proteins/metabolism ; Rats
Chemical Substances	Proteins
Language	English
Publishing date	2013-07-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1420885-4
ISSN	1096-0929 ; 1096-6080
ISSN (online)	1096-0929
ISSN	1096-6080
DOI	10.1093/toxsci/kft166
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Article ; Online: Comparative Toxicity and Metabolism of N-Acyl Homologues of Acetaminophen and Its Isomer 3'-Hydroxyacetanilide.

Koen, Yakov M / Liu, Ke / Shinogle, Heather / Williams, Todd D / Hanzlik, Robert P

Chemical research in toxicology

2016 Volume 29, Issue 11, Page(s) 1857–1864

Abstract: The hepatotoxicity of acetaminophen (APAP) is generally attributed to the formation of a reactive quinoneimine metabolite (NAPQI) that depletes glutathione and covalently binds to hepatocellular proteins. To explore the importance of the N-acyl group in ... ...

Abstract	The hepatotoxicity of acetaminophen (APAP) is generally attributed to the formation of a reactive quinoneimine metabolite (NAPQI) that depletes glutathione and covalently binds to hepatocellular proteins. To explore the importance of the N-acyl group in APAP metabolism and toxicity, we synthesized 12 acyl side chain homologues of acetaminophen (APAP) and its 3'-regioisomer (AMAP), including the respective N-(4-pentynoyl) analogues PYPAP and PYMAP. Rat hepatocytes converted APAP, AMAP, PYPAP, and PYMAP extensively to O-glucuronide and O-sulfate conjugates in varying proportions, whereas glutathione or cysteine conjugates were observed only for APAP and PYPAP. PYPAP and PYMAP also underwent N-deacylation followed by O-sulfation and/or N-acetylation to a modest extent. The overall rates of metabolism in hepatocytes varied approximately 2-fold in the order APAP < AMAP ≈ PYPAP < PYMAP. Rat liver microsomes supplemented with NADPH and GSH converted APAP and PYPAP to their respective glutathione conjugates (formed via a reactive quinoneimine intermediate). With PYPAP only, a hydroxylated GSH conjugate was also observed. Thus, differences in biotransformation among these analogues were modest and mostly quantitative in nature. Cytotoxicity was evaluated in cultured hepatocytes by monitoring cell death using time-lapse photomicrography coupled with Hoechst 33342 and CellTox Green dyes to facilitate counting live cells vs dead cells, respectively. Progress curves for cell death and the areas under those curves showed that toxicity was markedly dependent on compound, concentration, and time. AMAP was essentially equipotent with APAP. Homologating the acyl side chain from C-2 to C-5 led to progressive increases in toxicity up to 80-fold in the para series. In conclusion, whereas N- or ring-substitution on APAP decrease metabolism and toxicity, homologating the N-acyl side chain increases metabolism about 2-fold, preserves the chemical reactivity of quinoneimine metabolites, and increases toxicity by up to 80-fold.
MeSH term(s)	Acetaminophen/metabolism ; Acetaminophen/toxicity ; Animals ; Biotransformation ; Hepatocytes/drug effects ; Hepatocytes/metabolism ; Isomerism ; Male ; Microsomes, Liver/drug effects ; Microsomes, Liver/metabolism ; Rats ; Rats, Sprague-Dawley
Chemical Substances	Acetaminophen (362O9ITL9D)
Language	English
Publishing date	2016-11-21
Publishing country	United States
Document type	Comparative Study ; Journal Article
ZDB-ID	639353-6
ISSN	1520-5010 ; 0893-228X
ISSN (online)	1520-5010
ISSN	0893-228X
DOI	10.1021/acs.chemrestox.6b00270
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Article ; Online: Protein Targets of Isoniazid-Reactive Metabolites in Mouse Liver in Vivo.

Koen, Yakov M / Galeva, Nadezhda A / Metushi, Imir G / Uetrecht, Jack / Hanzlik, Robert P

Chemical research in toxicology

2016 Volume 29, Issue 6, Page(s) 1064–1072

Abstract: Isoniazid (INH) has been a first-line drug for the treatment of tuberculosis for more than 40 years. INH is well-tolerated by most patients, but some patients develop hepatitis that can be severe in rare cases or after overdose. The mechanisms underlying ...

Abstract	Isoniazid (INH) has been a first-line drug for the treatment of tuberculosis for more than 40 years. INH is well-tolerated by most patients, but some patients develop hepatitis that can be severe in rare cases or after overdose. The mechanisms underlying the hepatotoxicity of INH are not known, but covalent binding of reactive metabolites is known to occur in animals and is suspected in human cases. A major unresolved question is the identity of the liver proteins that are modified by INH metabolites. Treating mice with INH leads to accumulation of isonicotinoyl-lysine residues on numerous proteins in the hepatic S9 fraction. Analysis of this fraction by SDS-PAGE followed by tryptic digestion of bands and LC-MS/MS revealed a single adducted peptide derived from d-dopachrome decarboxylase. When a tryptic digest of whole S9 was applied to anti-INH antibody immobilized on beads, only 12 peptides were retained, 5 of which clearly contained isonicotinoyl-lysine adducts and could be confidently assigned to 5 liver proteins. In another experiment, undigested S9 fractions from INA-treated and untreated (UT) mice were adsorbed in parallel on anti-INA beads and the retained proteins were digested and analyzed by LC-MS/MS. The INA-S9 digest showed 1 adducted peptide that was associated with a unique protein whose identity was corroborated by numerous nonadducted peptides in the digest and 13 other proteins identified only by multiple nonadducted peptides. None of these 14 proteins was associated with any peptides present in the UT-S9 fraction. Overall, we identified 7 mouse liver proteins that became adducted by INH metabolites in vivo. Of these 7 INH target proteins, only 2 have been previously reported as targets of any reactive metabolite in vivo.
MeSH term(s)	Animals ; Antitubercular Agents/chemistry ; Antitubercular Agents/metabolism ; Antitubercular Agents/toxicity ; Female ; Isoniazid/chemistry ; Isoniazid/metabolism ; Isoniazid/toxicity ; Liver/drug effects ; Liver/metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Structure ; Proteins/chemistry ; Proteins/metabolism
Chemical Substances	Antitubercular Agents ; Proteins ; Isoniazid (V83O1VOZ8L)
Language	English
Publishing date	2016--20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639353-6
ISSN	1520-5010 ; 0893-228X
ISSN (online)	1520-5010
ISSN	0893-228X
DOI	10.1021/acs.chemrestox.6b00098
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Article: Cytochrome P450-catalyzed oxidation of N-benzyl-N-cyclopropylamine generates both cyclopropanone hydrate and 3-hydroxypropionaldehyde via hydrogen abstraction, not single electron transfer.

Cerny, Matthew A / Hanzlik, Robert P

Journal of the American Chemical Society

2006 Volume 128, Issue 10, Page(s) 3346–3354

Abstract: The suicide substrate activity of N-benzyl-N-cyclopropylamine (1) and N-benzyl-N-(1'-methylcyclopropyl)amine (2) toward cytochrome P450 and other enzymes has been explained by a mechanism involving single electron transfer (SET) oxidation, followed by ... ...

Abstract	The suicide substrate activity of N-benzyl-N-cyclopropylamine (1) and N-benzyl-N-(1'-methylcyclopropyl)amine (2) toward cytochrome P450 and other enzymes has been explained by a mechanism involving single electron transfer (SET) oxidation, followed by ring-opening of the aminium radical cation (protonated aminyl radical) and reaction with the P450 active site. Although the SET oxidation of N-cyclopropyl-N-methylaniline (3) by horseradish peroxidase leads exclusively to ring-opened (non-cyclopropyl) products, P450 oxidation of 3 leads to formation of cyclopropanone hydrate and no ring-opened products, and 3 does not inactivate P450. To help reconcile these discrepant behaviors we have determined the complete metabolic fate of 1 with P450 in vitro. 3-Hydroxypropionaldehyde (3HP), the presumptive "signature metabolite" for SET oxidation of a cyclopropylamine, was observed for the first time in 57% yield, along with cyclopropanone hydrate (34%), cyclopropylamine (9%), benzaldehyde (6%), benzyl alcohol (12%), and benzaldoxime (19%). Unexpectedly, N-benzyl-N-cyclopropyl-N-methylamine (4) was found not to inactivate P450 and not to give rise to 3HP as a metabolite without first undergoing oxidative N-demethylation to 1. These and other observations argue against a role for SET mechanisms in the P450 oxidation of cyclopropylamines. We suggest that a conventional hydrogen abstraction/hydroxyl recombination mechanism (or its equivalent as a one-step "insertion" mechanism) at C-H bonds in 1-4 leads to nonrearranged carbinolamine intermediates and thereby to "ordinary" N-dealkylation products including cyclopropanone hydrate. Alternatively, hydrogen abstraction at the N-H bond of secondary cyclopropylamines 1 gives a neutral aminyl radical which could undergo rapid ring-opening leading either to enzyme inactivation or 3HP formation.
MeSH term(s)	Aldehydes/chemistry ; Aldehydes/metabolism ; Catalysis ; Cyclopropanes/chemistry ; Cyclopropanes/metabolism ; Cytochrome P-450 Enzyme System/chemistry ; Cytochrome P-450 Enzyme System/metabolism ; Glyceraldehyde/analogs & derivatives ; Glyceraldehyde/chemistry ; Glyceraldehyde/metabolism ; Horseradish Peroxidase/chemistry ; Horseradish Peroxidase/metabolism ; Hydrogen/chemistry ; Hydrogen/metabolism ; Kinetics ; Oxidation-Reduction ; Propane/chemistry ; Propane/metabolism
Chemical Substances	Aldehydes ; Cyclopropanes ; 3-hydroxypropionaldehyde (2134-29-4) ; 1-benzylcyclopropylamine (27067-03-4) ; Glyceraldehyde (367-47-5) ; Hydrogen (7YNJ3PO35Z) ; Cytochrome P-450 Enzyme System (9035-51-2) ; Horseradish Peroxidase (EC 1.11.1.-) ; Propane (T75W9911L6)
Language	English
Publishing date	2006-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/ja054938+
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Article ; Online: Eulogy to Mathias P. Mertes, 1932-1989.

Bowman-James, Kristin / Grunewald, Gary L / Hanzlik, Robert P

Medicinal research reviews

2009 Volume 29, Issue 1, Page(s) 1–2

MeSH term(s)	Chemistry, Pharmaceutical/history ; History, 20th Century ; Magnetic Resonance Spectroscopy/history ; United States
Language	English
Publishing date	2009-01
Publishing country	United States
Document type	Biography ; Historical Article ; Journal Article ; Portraits
ZDB-ID	603210-2
ISSN	1098-1128 ; 0198-6325
ISSN (online)	1098-1128
ISSN	0198-6325
DOI	10.1002/med.20147
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Article ; Online: Crystal and solution structures of human oncoprotein Musashi-2 N-terminal RNA recognition motif 1.

Lan, Lan / Xing, Minli / Kashipathy, Maithri / Douglas, Justin / Gao, Philip / Battaile, Kevin / Hanzlik, Robert / Lovell, Scott / Xu, Liang

Proteins

2019 Volume 88, Issue 4, Page(s) 573–583

Abstract: Musashi-2 (MSI2) belongs to Musashi family of RNA binding proteins (RBP). Like Musashi-1 (MSI1), it is overexpressed in a variety of cancers and is a promising therapeutic target. Both MSI proteins contain two N-terminal RNA recognition motifs and play ... ...

Abstract	Musashi-2 (MSI2) belongs to Musashi family of RNA binding proteins (RBP). Like Musashi-1 (MSI1), it is overexpressed in a variety of cancers and is a promising therapeutic target. Both MSI proteins contain two N-terminal RNA recognition motifs and play roles in posttranscriptional regulation of target mRNAs. Previously, we have identified several inhibitors of MSI1, all of which bind to MSI2 as well. In order to design MSI2-specific inhibitors and compare the differences of binding mode of the inhibitors, we set out to solve the structure of MSI2-RRM1, the key motif that is responsible for the binding. Here, we report the crystal structure and the first NMR solution structure of MSI2-RRM1, and compare these to the structures of MSI1-RBD1 and other RBPs. A high degree of structural similarity was observed between the crystal and solution NMR structures. MSI2-RRM1 shows a highly similar overall folding topology to MSI1-RBD1 and other RBPs. The structural information of MSI2-RRM1 will be helpful for understanding MSI2-RNA interaction and for guiding rational drug design of MSI2-specific inhibitors.
MeSH term(s)	Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Oncogene Proteins/chemistry ; Oncogene Proteins/genetics ; Oncogene Proteins/metabolism ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Folding ; Protein Interaction Domains and Motifs ; RNA Recognition Motif ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Thermodynamics
Chemical Substances	MSI1 protein, human ; MSI2 protein, human ; Nerve Tissue Proteins ; Oncogene Proteins ; RNA, Messenger ; RNA-Binding Proteins
Language	English
Publishing date	2019-10-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	806683-8
ISSN	1097-0134 ; 0887-3585
ISSN (online)	1097-0134
ISSN	0887-3585
DOI	10.1002/prot.25836
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Article: Cyclopropylamine inactivation of cytochromes P450: role of metabolic intermediate complexes.

Cerny, Matthew A / Hanzlik, Robert P

Archives of biochemistry and biophysics

2005 Volume 436, Issue 2, Page(s) 265–275

Abstract: The inactivation of cytochrome P450 enzymes by cyclopropylamines has been attributed to a mechanism involving initial one-electron oxidation at nitrogen followed by scission of the cyclopropane ring leading to covalent modification of the enzyme. Herein, ...

Abstract	The inactivation of cytochrome P450 enzymes by cyclopropylamines has been attributed to a mechanism involving initial one-electron oxidation at nitrogen followed by scission of the cyclopropane ring leading to covalent modification of the enzyme. Herein, we report that in liver microsomes N-cyclopropylbenzylamine (1) and related compounds inactivate P450 to a large extent via formation of metabolic intermediate complexes (MICs) in which a nitroso metabolite coordinates tightly to the heme iron, thereby preventing turnover. MIC formation from 1 does not occur in reconstituted P450 systems with CYP2B1/2, 2C11 or 2E1, or in microsomes exposed to gentle heating to inactivate the flavin-containing monooxygenase (FMO). In contrast, N-hydroxy-N-cyclopropylbenzylamine (3) and N-benzylhydroxylamine (4) generate MICs much faster than 1 in both reconstituted and microsomal systems. MIC formation from nitrone 5 (PhCH = N(O)cPr) is somewhat faster than from 1, but very much faster than the hydrolysis of 5 to a primary hydroxylamine. Thus the major overall route from 1 to a P450 MIC complex would appear to involve FMO oxidation to 3, further oxidation by P450 and/or FMO to nitrone 5' (C2H4C = N(O)CH2Ph), hydrolysis to 4, and P450 oxidation to alpha-nitrosotoluene as the precursor to oxime 2 and the major MIC from 1.
MeSH term(s)	Animals ; Aryl Hydrocarbon Hydroxylases/metabolism ; Cyclopropanes/chemistry ; Cyclopropanes/pharmacology ; Cytochrome P-450 CYP2B1/metabolism ; Cytochrome P-450 CYP2E1/metabolism ; Cytochrome P-450 Enzyme System/chemistry ; Cytochrome P450 Family 2 ; Electrons ; Flavins/chemistry ; Formamides/chemistry ; Heme/chemistry ; Hot Temperature ; Hydrolysis ; Hydroxylamine/chemistry ; Ions ; Kinetics ; Male ; Microsomes/metabolism ; Microsomes, Liver/metabolism ; Models, Chemical ; Nitroso Compounds/chemistry ; Oxygen/metabolism ; Oxygenases/chemistry ; Rats ; Rats, Sprague-Dawley ; Spectrophotometry ; Steroid 16-alpha-Hydroxylase/metabolism ; Steroid Hydroxylases/metabolism ; Temperature ; Time Factors
Chemical Substances	Cyclopropanes ; Flavins ; Formamides ; Ions ; Nitroso Compounds ; Hydroxylamine (2FP81O2L9Z) ; Heme (42VZT0U6YR) ; formamide (4781T907ZS) ; cyclopropylamine (8PR8XTH1X1) ; Cytochrome P-450 Enzyme System (9035-51-2) ; Oxygenases (EC 1.13.-) ; Steroid Hydroxylases (EC 1.14.-) ; Cytochrome P-450 CYP2E1 (EC 1.14.13.-) ; dimethylaniline monooxygenase (N-oxide forming) (EC 1.14.13.8) ; Aryl Hydrocarbon Hydroxylases (EC 1.14.14.1) ; CYP2C11 protein, rat (EC 1.14.14.1) ; Cytochrome P-450 CYP2B1 (EC 1.14.14.1) ; Cytochrome P450 Family 2 (EC 1.14.14.1) ; Steroid 16-alpha-Hydroxylase (EC 1.14.14.1) ; steroid 16-beta-hydroxylase (EC 1.14.14.1) ; 2-nitrosotoluene (H2P2O30ZSS) ; Oxygen (S88TT14065)
Language	English
Publishing date	2005-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2005.02.020
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Article ; Online: Filling and mining the reactive metabolite target protein database.

Hanzlik, Robert P / Fang, Jianwen / Koen, Yakov M

Chemico-biological interactions

2009 Volume 179, Issue 1, Page(s) 38–44

Abstract: The post-translational modification of proteins is a well-known endogenous mechanism for regulating protein function and activity. Cellular proteins are also susceptible to post-translational modification by xenobiotic agents that possess, or whose ... ...

Abstract	The post-translational modification of proteins is a well-known endogenous mechanism for regulating protein function and activity. Cellular proteins are also susceptible to post-translational modification by xenobiotic agents that possess, or whose metabolites possess, significant electrophilic character. Such non-physiological modifications to endogenous proteins are sometimes benign, but in other cases they are strongly associated with, and are presumed to cause, lethal cytotoxic consequences via necrosis and/or apoptosis. The Reactive Metabolite Target Protein Database (TPDB) is a searchable, freely web-accessible (http://tpdb.medchem.ku.edu:8080/protein_database/) resource that attempts to provide a comprehensive, up-to-date listing of known reactive metabolite target proteins. In this report we characterize the TPDB by reviewing briefly how the information it contains came to be known. We also compare its information to that provided by other types of "-omics" studies relevant to toxicology, and we illustrate how bioinformatic analysis of target proteins may help to elucidate mechanisms of cytotoxic responses to reactive metabolites.
MeSH term(s)	Databases, Protein ; Information Storage and Retrieval ; Protein Binding
Language	English
Publishing date	2009-04-15
Publishing country	Ireland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	218799-1
ISSN	1872-7786 ; 0009-2797
ISSN (online)	1872-7786
ISSN	0009-2797
DOI	10.1016/j.cbi.2008.08.016
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