Monoamine Oxidase: Methods and Protocols (Methods in Molecular Biology, 2558)

259 Pages·2022·7.285 MB·English

by  Claudia Binda (editor)

Methods in
Molecular Biology 2558
Claudia Binda Editor
Monoamine
Oxidase
Methods and Protocols
M M B
ETHODS IN OLECULAR IO LO GY
SeriesEditor
JohnM.Walker
School of Lifeand MedicalSciences
University ofHertfordshire
Hatfield, Hertfordshire, UK
Forfurther volumes:
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For over 35 years, biological scientists have come to rely on the research protocols and
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Monoamine Oxidase
Methods and Protocols
Edited by
Claudia Binda
Department of Biology and Biotechnology, University of Pavia, Pavia, Italy
Editor
ClaudiaBinda
DepartmentofBiologyandBiotechnology
UniversityofPavia
Pavia,Italy
ISSN1064-3745 ISSN1940-6029 (electronic)
MethodsinMolecularBiology
ISBN978-1-0716-2642-9 ISBN978-1-0716-2643-6 (eBook)
https://doi.org/10.1007/978-1-0716-2643-6
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Preface
This volume of the Methods in Molecular Biology series is specifically dedicated to mono-
amine oxidases (MAOs). Among the different enzymes that catalyse the oxidation of a
carbon-nitrogen bond in bioactive substrates, MAOs play a key role in the central nervous
systembydeaminatingaromaticneurotransmitterssuchasdopamine,serotonin,andadren-
aline. Moreover, xenobiotic compounds containing primary, secondary, or even tertiary
amino groups that may be introduced pharmacologically or with one’s diet may be sub-
strates for MAOs. Two isozymes, MAO A and MAO B, are expressed in mammals, which
share 70% sequence identity and are both FAD-dependent enzymes anchored to the outer
mitochondrialmembranethroughaC-terminalα-helix.
MAOs have been known for almost a century, given that the identification of an
oxidative deamination activity on tyramine was published in 1928. Since then, a huge
number of studies on MAOs have been reported yielding more than 24,000 results by
searching PubMed with the keyword “monoamine oxidase”. Other eukaryotic MAO
enzymes were discovered such as fungal MAO N that is about 25% identical to MAO
A/MAO B and is devoid of the membrane-binding domain, which makes this enzyme
idealforbiocatalyticindustrialapplicationsthatinvolveanamineoxidationstep.Thisbook
willfocusonmethodsusedtostudymammalian(mainlyhuman)MAOAandMAOBthat,
for their central rolein neurotransmitter metabolism, are validateddrug targets for neuro-
pathologies such as Parkinson’s and Alzheimer’s diseases and depression. In addition, the
clinical context involving MAO A and MAO B is expanding as these enzymes are widely
expressed not only in the brain but also in other organs such as heart, liver, placenta, and
platelets. Their enzymatic activity, which generates high levels of hydrogen peroxide as
secondary product, is supposed to contribute to the onset of ageing-related cardiovascular
diseasesandcertaintypesofsolidtumoursbyincreasingcellularoxidativestress.
MammalianMAOshavebeenextensivelystudied,bothbiochemicallywithinthespecific
contextofflavoenzymes(coveringalsopurelymechanisticaspects)andpharmacologicallyin
theframeworkoftheirinvolvementinneurologicaldiseases.Thisbookaimsatprovidinga
picture of the main methods to study mammalian MAOs, ranging from cell biology to
computationalchemistry.Acollectionof17chaptershavebeenwrittenbyscientistsactively
involved in this field who contributed to developing most of the described methods. The
first two chapters are focused on methods used to obtain pure samples of MAO A and
MAO B, either from natural tissues (Chap. 1) or as recombinant proteins (Chap. 2). The
former was routinely used before the advent of molecular biology techniques and may be
stillusefulwhennativetissue-specificenzymesarerequired,thelatterentailedthedevelop-
ment of a eukaryotic expression system in Pichia pastoris which was then extensively used
also for other membrane proteins. Chapters 3, 4, 5, 6, 7, and 8 concern assays and
techniques used to measure MAO enzymatic activity and perform inhibition studies.
Chapter 9 is focused on protocol to crystallize human MAO B, which so far has been the
most characterized form from a structural point of view. Chapters 10, 11, 12, 13, and 14
describedifferentmethodstoaddresscellularlocalizationandfunctionofMAOs,eitherin
cell lines or in animal models. The last chapters (Chaps. 15, 16, and 17) are dedicated to
computationalmethodsappliedtorationaldrugdesignapproachesthatareusedtodevelop
newMAOinhibitors.
v
vi Preface
Some of the methods described in this book were elaborated many years ago and they
arestillused,insomecasesoptimizedwithtechnologicalimprovements.For thisreason,it
may be difficult to learn and reproducibly apply these MAO-specific methods simply
following the experimental section of articles. I hope this book may be useful for scientists
interestedinstudyingMAOsandothersimilaramineoxidaseenzymes.
Pavia,Italy ClaudiaBinda
Contents
Preface ..................................................................... v
Contributors................................................................. ix
1 PurificationofMAOAandMAOBfromMammalianTissueSources......... 1
DaleE.Edmondson
2 PurificationofRecombinantEukaryoticMAOAandMAOB
UtilizingthePichiapastorisExpressionSystem ...... ........ ....... ........ 11
DaleE.Edmondson
3 ThePeroxidase-CoupledAssaytoMeasureMAOEnzymaticActivity.......... 23
JoanaReisandClaudiaBinda
4 MeasurementofMAOEnzymaticActivitybySpectrophotometric
DirectAssays ....... ....... ........ ....... ....... ........ ....... ........ 35
JoanaReisandClaudiaBinda
5 RadiochemicalAssayofMonoamineOxidaseActivity ... ..... ...... ....... .. 45
AndrewHolt
6 MAOVisibleSpectroscopyforLigandInteractions,RedoxChemistry,
andKineticsofIrreversibleInhibition ....... ....... ........ ....... ........ 63
RonaR.Ramsay
7 ConventionalReceptorRadioligandBindingTechniquesApplied
totheStudyofMonoamineOxidase ........ ....... ........ ....... ........ 75
AndrewHolt
8 AssayofMAOInhibitionbyChromatographicTechniques
(HPLC/HPLC-MS) ....... ........ ...... ....... ....... .. ....... ........ 97
Toma´sHerraiz
9 CrystallizationofHumanMonoamineOxidaseB.... ........ ....... ........ 115
ClaudiaBinda,DaleE.Edmondson,andAndreaMattevi
10 DetectingMonoamineOxidaseAandBProteins:AWesternBlotting
ProtocolandSomePracticalConsiderations ........ ........ ....... ........ 123
JenniferN.K.Nyarko,RyanM.Heistad,PaulR.Pennington,
andDarrellD.Mousseau
11 An(Immuno)FluorescenceProtocolforMonitoringMonoamine
OxidaseA/BProteinDistributionWithintheCell........... ....... ........ 143
TylerJ.Wenzel,JenniferN.K.Nyarko,RyanM.Heistad,
PaulR.Pennington,ChrisP.Phenix,andDarrellD.Mousseau
12 ExpressionandFunctionofMAOAinCardiacCellsbyMeans
ofAdenovirus-MediatedGeneTransfer...... ....... ........ ....... ........ 163
YohanSantin,AngeloParini,andJeanneMialet-Perez
13 InVitroandInVivoAssaysCharacterizingMAOAFunctioninCancers...... 171
BoyangJasonWuandJeanC.Shih
vii
viii Contents
14 InVivoStudyofMonoamineOxidasesUsingMultisiteIntracerebral
Microdialysis ....... ....... ........ ....... ....... ........ ....... ........ 183
PhilippeDeDeurwaerde`re,NouhadSamb,HasnaElBoukhari,
Re´miCorne,AbdeslamChagraoui,andGiuseppeDiGiovanni
15 InformedUseof3D-QSARfor theRationalDesignofCoumarin
DerivativesasPotentandSelectiveMAOBInhibitors........ ....... ........ 197
NicolaGambacorta,MarcoCatto,LeonardoPisani,
AngeloCarotti,andOrazioNicolotti
16 Hansch-TypeQSARModelsfor theRationalDesignofMAO
Inhibitors:BasicPrinciplesandMethodology ....... ........ ....... ........ 207
LeonardoPisani,ModestodeCandia,MariagraziaRullo,
andCosimoD.Altomare
17 ComputationalChemistryandMolecularModelingofReversible
MAOInhibitors ... ........ ........ ....... ....... ........ ....... ........ 221
KemalYelekc¸iandSafiyeSag˘ Erdem
Index ...................................................................... 253
Contributors
COSIMOD.ALTOMARE • DepartmentofPharmacy-Pharmaceutical Sciences,Universityof
Bari“AldoMoro”,Bari,Italy
CLAUDIABINDA • DepartmentofBiologyandBiotechnology,UniversityofPavia,Pavia,Italy
ANGELOCAROTTI • DepartmentofPharmacy-PharmaceuticalSciences,UniversityofBari
“AldoMoro”,Bari,Italy
MARCOCATTO • DepartmentofPharmacy-Pharmaceutical Sciences,UniversityofBari
“AldoMoro”,Bari,Italy
ABDESLAMCHAGRAOUI • NormandieUniversity,UNIROUEN,INSERM,U1239,CHU
Rouen,NeuronalandNeuroendocrineDifferentiationandCommunicationLaboratory,
InstituteforResearchandInnovationinBiomedicineofNormandy(IRIB),Rouen,
France;DepartmentofMedicalBiochemistry,RouenUniversityHospital,Rouen,France
RE´MICORNE • CentreNationaldelaRechercheScientifique(Unite´MixtedeRecherche
5287),BordeauxCedex,France
MODESTODECANDIA • DepartmentofPharmacy-PharmaceuticalSciences,Universityof
Bari“AldoMoro”,Bari,Italy
PHILIPPEDEDEURWAERDE`RE • CentreNationaldelaRechercheScientifique(Unite´Mixtede
Recherche5287),BordeauxCedex,France
GIUSEPPE DIGIOVANNI • DepartmentofPhysiologyandBiochemistry,FacultyofMedicine
andSurgery,UniversityofMalta,Msida,Malta;SchoolofBiosciences,CardiffUniversity,
Cardiff,UK
DALEE.EDMONDSON • DepartmentofBiochemistry,EmoryUniversity,Atlanta,GA,USA
HASNAELBOUKHARI • CentreNationaldelaRechercheScientifique(Unite´Mixtede
Recherche5287),BordeauxCedex,France
SAFIYESAG˘ ERDEM • DepartmentofChemistry,FacultyofArtsandSciences,Marmara
University,Istanbul,Turkey
NICOLA GAMBACORTA • DepartmentofPharmacy-PharmaceuticalSciences,Universityof
Bari“AldoMoro”,Bari,Italy
RYANM.HEISTAD • DepartmentofPsychiatry,UniversityofSaskatchewan,Saskatoon,SK,
Canada
TOMA´SHERRAIZ • InstitutodeCienciayTecnologı´adeAlimentosyNutrici(cid:1)on(ICTAN),
SpanishNationalResearchCouncil(CSIC),Madrid,Spain
ANDREWHOLT • NeurochemicalResearchUnit,DepartmentofPsychiatry,Facultyof
MedicineandDentistry,UniversityofAlberta,Edmonton,AB,Canada
ANDREA MATTEVI • DepartmentofBiologyandBiotechnology,UniversityofPavia,Pavia,
Italy
JEANNEMIALET-PEREZ • InstituteofMetabolicandCardiovascularDiseases(I2MC),
INSERM,Universite´deToulouse,Toulouse,France
DARRELLD.MOUSSEAU • DepartmentofPsychiatry,UniversityofSaskatchewan,Saskatoon,
SK,Canada
ORAZIONICOLOTTI • DepartmentofPharmacy-PharmaceuticalSciences,UniversityofBari
“AldoMoro”,Bari,Italy
JENNIFERN.K.NYARKO • DepartmentofPsychiatry,UniversityofSaskatchewan,Saskatoon,
SK,Canada
ix