ACE activity is modulated by the enzyme [alpha]-galactosidase A
Fabry disease is a multisystem X-linked disorder resulting from α-galactosidase A (α-GalA) gene mutations leading to the accumulation of globotriaosylceramide mainly in endothelium compromising heart, kidney, and brain. In Fabry patients, progressive renal failure is frequently treated with angioten...
Saved in:
Published in | Journal of molecular medicine (Berlin, Germany) Vol. 89; no. 1; p. 65 |
---|---|
Main Authors | , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
New York
Springer Nature B.V
01.01.2011
|
Online Access | Get full text |
Cover
Loading…
Abstract | Fabry disease is a multisystem X-linked disorder resulting from α-galactosidase A (α-GalA) gene mutations leading to the accumulation of globotriaosylceramide mainly in endothelium compromising heart, kidney, and brain. In Fabry patients, progressive renal failure is frequently treated with angiotensin I-converting enzyme (ACE) inhibitors. We were interested in the possible interactions between ACE inhibitors therapy and the only causative therapy for Fabry disease, the enzyme replacement therapy (ERT) using recombinant human α-GalA (rhα-GalA). Our results suggest that ACE activity was significantly inhibited in plasma of Fabry patients and the blood pressure level decreased just after ERT (at the end of the rhα-GalA infusion). Interestingly, 2 weeks later, ACE activity was significantly upregulated and the plasma levels of angiotensin II increased in the patients treated with rhα-GalA following the elevations of ACE activity. The same inhibitory effect on ACE activity was also observed in rats after rhα-GalA infusion. Furthermore, ACE activity in CHO cells transfected with the human ACE was inhibited dose and time-dependently by rhα-GalA. In vitro, the incubation of plasma from healthy volunteers with rhα-GalA significantly reduced ACE activity. Finally, rhα-GalA also inhibited ACE activity and released galactose residues from purified rabbit lung ACE dose-dependently. In summary, our results suggest that rhα-GalA interacts with ACE and inhibits its activity, possibly by removing the galactose residues from the enzyme. This modulation might have profound impact on the clinical outcome of Fabry patients treated with rhα-GalA.[PUBLICATION ABSTRACT] |
---|---|
AbstractList | Fabry disease is a multisystem X-linked disorder resulting from α-galactosidase A (α-GalA) gene mutations leading to the accumulation of globotriaosylceramide mainly in endothelium compromising heart, kidney, and brain. In Fabry patients, progressive renal failure is frequently treated with angiotensin I-converting enzyme (ACE) inhibitors. We were interested in the possible interactions between ACE inhibitors therapy and the only causative therapy for Fabry disease, the enzyme replacement therapy (ERT) using recombinant human α-GalA (rhα-GalA). Our results suggest that ACE activity was significantly inhibited in plasma of Fabry patients and the blood pressure level decreased just after ERT (at the end of the rhα-GalA infusion). Interestingly, 2 weeks later, ACE activity was significantly upregulated and the plasma levels of angiotensin II increased in the patients treated with rhα-GalA following the elevations of ACE activity. The same inhibitory effect on ACE activity was also observed in rats after rhα-GalA infusion. Furthermore, ACE activity in CHO cells transfected with the human ACE was inhibited dose and time-dependently by rhα-GalA. In vitro, the incubation of plasma from healthy volunteers with rhα-GalA significantly reduced ACE activity. Finally, rhα-GalA also inhibited ACE activity and released galactose residues from purified rabbit lung ACE dose-dependently. In summary, our results suggest that rhα-GalA interacts with ACE and inhibits its activity, possibly by removing the galactose residues from the enzyme. This modulation might have profound impact on the clinical outcome of Fabry patients treated with rhα-GalA.[PUBLICATION ABSTRACT] |
Author | Bader, Michael Da Silva, Elton Dias Pesquero, João Bosco Rojas, Maria Verônica; Munoz Carvalho, Luiz Roberto Batista, Elice Carneiro Carmona, Adriana Karaoglanovic Dos Santos, Edson Lucas Martins, Ana Maria Casarini, Dulce Elena Dos Santos, Robson Augusto de Oliveira, Suzana Macedo de Picoly Souza, Kely D'almeida, Vânia Nakaie, Clovis Ryuichi |
Author_xml | – sequence: 1 givenname: Elice surname: Batista middlename: Carneiro fullname: Batista, Elice Carneiro – sequence: 2 givenname: Luiz surname: Carvalho middlename: Roberto fullname: Carvalho, Luiz Roberto – sequence: 3 givenname: Dulce surname: Casarini middlename: Elena fullname: Casarini, Dulce Elena – sequence: 4 givenname: Adriana surname: Carmona middlename: Karaoglanovic fullname: Carmona, Adriana Karaoglanovic – sequence: 5 givenname: Edson surname: Dos Santos middlename: Lucas fullname: Dos Santos, Edson Lucas – sequence: 6 givenname: Elton surname: Da Silva middlename: Dias fullname: Da Silva, Elton Dias – sequence: 7 givenname: Robson surname: Dos Santos middlename: Augusto fullname: Dos Santos, Robson Augusto – sequence: 8 givenname: Clovis surname: Nakaie middlename: Ryuichi fullname: Nakaie, Clovis Ryuichi – sequence: 9 givenname: Maria surname: Rojas middlename: Verônica; Munoz fullname: Rojas, Maria Verônica; Munoz – sequence: 10 givenname: Suzana surname: de Oliveira middlename: Macedo fullname: de Oliveira, Suzana Macedo – sequence: 11 givenname: Michael surname: Bader fullname: Bader, Michael – sequence: 12 givenname: Vânia surname: D'almeida fullname: D'almeida, Vânia – sequence: 13 givenname: Ana surname: Martins middlename: Maria fullname: Martins, Ana Maria – sequence: 14 givenname: Kely surname: de Picoly Souza fullname: de Picoly Souza, Kely – sequence: 15 givenname: João surname: Pesquero middlename: Bosco fullname: Pesquero, João Bosco |
BookMark | eNqNyk0KwjAUBOCHVLBVD-AuuI--1PRvJSKKB3AnUqKNWolJNalQT28WHsDNDMx8EQTaaAkwYThjiNncIjIsqA-KaZ7SuAch44uYMs4xgBAL7seMpQOIrL17nSUFD2G5Wm-IOLv6XbuO1JY8TNUq4WRFTh1xN0mk_nQPSQ5CNTdxpFehPDe2roSVZDWC_kUoK8e_HsJ0u9mvd7R5mWcrrSvvpn1pf5V5zDKeJJgs_kJf2cA_2Q |
ContentType | Journal Article |
Copyright | Springer-Verlag 2011 |
Copyright_xml | – notice: Springer-Verlag 2011 |
DBID | 3V. 7TK 7X7 7XB 88E 8AO 8FI 8FJ 8FK ABUWG AFKRA BENPR CCPQU FYUFA GHDGH K9. M0S M1P PQEST PQQKQ PQUKI PRINS |
DOI | 10.1007/s00109-010-0686-2 |
DatabaseName | ProQuest Central (Corporate) Neurosciences Abstracts ProQuest - Health & Medical Complete保健、医学与药学数据库 ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) ProQuest Pharma Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest Central UK/Ireland AUTh Library subscriptions: ProQuest Central ProQuest One Community College Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Health & Medical Complete (Alumni) Health & Medical Collection (Alumni Edition) PML(ProQuest Medical Library) ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China |
DatabaseTitle | ProQuest One Academic Eastern Edition ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest Hospital Collection Health Research Premium Collection (Alumni) ProQuest Pharma Collection Neurosciences Abstracts ProQuest Central China ProQuest Hospital Collection (Alumni) ProQuest Central ProQuest Health & Medical Complete Health Research Premium Collection ProQuest Medical Library ProQuest One Academic UKI Edition Health and Medicine Complete (Alumni Edition) ProQuest One Academic ProQuest Medical Library (Alumni) ProQuest Central (Alumni) |
DatabaseTitleList | ProQuest One Academic Eastern Edition |
Database_xml | – sequence: 1 dbid: 7X7 name: ProQuest Health & Medical Collection url: https://search.proquest.com/healthcomplete sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Medicine |
EISSN | 1432-1440 |
ExternalDocumentID | 2225959391 |
GroupedDBID | --- -4W -56 -5G -BR -EM -~C .86 .VR 06C 06D 0R~ 0VY 199 1N0 203 29L 29~ 2J2 2JN 2JY 2KG 2KM 2LR 2VQ 2~H 30V 36B 3V. 4.4 406 408 409 40D 40E 5GY 5RE 5VS 67N 67Z 6NX 78A 7TK 7X7 7XB 88E 8AO 8FI 8FJ 8FK 8TC 8UJ 95- 95. 95~ 96X AAAVM AABHQ AACDK AAHNG AAIAL AAJBT AAJKR AANXM AANZL AARHV AARTL AASML AATNV AATVU AAUYE AAWCG AAYIU AAYQN AAYTO ABAKF ABBBX ABBXA ABDZT ABECU ABFTV ABHLI ABHQN ABJOX ABKCH ABKTR ABLJU ABMNI ABMQK ABNWP ABOCM ABPLI ABQBU ABSXP ABTEG ABTHY ABTKH ABTMW ABULA ABUWG ABWNU ABXPI ACAOD ACBXY ACDTI ACGFS ACHSB ACHXU ACIPQ ACIWK ACKNC ACMDZ ACMLO ACOKC ACOMO ACPRK ACZOJ ADBBV ADHIR ADIMF ADINQ ADKNI ADKPE ADRFC ADTPH ADURQ ADYFF ADZKW AEBTG AEFQL AEGAL AEGNC AEJHL AEJRE AEKMD AEMSY AEOHA AEPYU AESKC AETLH AEVLU AEXYK AFGCZ AFKRA AFLOW AFQWF AFRAH AFWTZ AFZKB AGAYW AGDGC AGJBK AGMZJ AGQEE AGQMX AGRTI AGWIL AGWZB AGYKE AHBYD AHKAY AHMBA AHSBF AHYZX AIAKS AIGIU AIIXL AILAN AITGF AJBLW AJRNO AJZVZ AKMHD ALIPV ALMA_UNASSIGNED_HOLDINGS ALWAN AMKLP AMXSW AMYLF AOCGG ARMRJ ASPBG AXYYD AZFZN B-. BA0 BDATZ BENPR BGNMA BPHCQ BVXVI CAG CCPQU COF CS3 CSCUP DDRTE DL5 DNIVK DPUIP EBD EBLON EBS EIOEI EJD EMB EMOBN EN4 EPAXT ESBYG F5P FEDTE FERAY FFXSO FIGPU FINBP FNLPD FRRFC FSGXE FWDCC FYUFA G-Y G-Z GGCAI GGRSB GJIRD GNWQR GQ6 GQ7 GQ8 GXS H13 HF~ HG5 HG6 HMCUK HMJXF HQYDN HRMNR HVGLF HZ~ I09 IHE IJ- IKXTQ ITM IWAJR IXC IZIGR IZQ I~X I~Z J-C J0Z JBSCW JCJTX JZLTJ K9. KDC KOV KPH LAS LLZTM M1P M4Y MA- N2Q N9A NB0 NPVJJ NQJWS NU0 O9- O93 O9G O9I O9J OAM P19 PF0 PQEST PQQKQ PQUKI PRINS PROAC PSQYO PT4 PT5 Q2X QOK QOR QOS R89 R9I RHV RIG RNS ROL RPX RRX RSV S16 S27 S3A S3B SAP SBL SDH SDM SHX SISQX SJYHP SNE SNPRN SNX SOHCF SOJ SPISZ SRMVM SSLCW SSXJD STPWE SV3 SZN T13 TSG TSK TSV TUC U2A U9L UG4 UKHRP UOJIU UTJUX UZXMN VC2 VFIZW W23 W48 WJK WK8 YLTOR Z45 Z7R Z7U Z7W Z7Z Z82 Z83 Z87 Z8M Z8O Z8Q Z8T Z8V Z8W Z91 ZMTXR ZOVNA ~EX |
ID | FETCH-proquest_journals_8217455053 |
IEDL.DBID | BENPR |
ISSN | 0946-2716 |
IngestDate | Thu Oct 10 17:44:57 EDT 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 1 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-proquest_journals_8217455053 |
PQID | 821745505 |
PQPubID | 48876 |
ParticipantIDs | proquest_journals_821745505 |
PublicationCentury | 2000 |
PublicationDate | 20110101 |
PublicationDateYYYYMMDD | 2011-01-01 |
PublicationDate_xml | – month: 01 year: 2011 text: 20110101 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | New York |
PublicationPlace_xml | – name: New York |
PublicationTitle | Journal of molecular medicine (Berlin, Germany) |
PublicationYear | 2011 |
Publisher | Springer Nature B.V |
Publisher_xml | – name: Springer Nature B.V |
SSID | ssj0017594 |
Score | 4.000864 |
Snippet | Fabry disease is a multisystem X-linked disorder resulting from α-galactosidase A (α-GalA) gene mutations leading to the accumulation of globotriaosylceramide... |
SourceID | proquest |
SourceType | Aggregation Database |
StartPage | 65 |
Title | ACE activity is modulated by the enzyme [alpha]-galactosidase A |
URI | https://www.proquest.com/docview/821745505 |
Volume | 89 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1NS8NAEB1sC-Kl-Im2WhbxuthNs9ntqcSSUoQWEYWASCHZLXhooqYe6q93ZrvpRSjkNpBkP5h5s29mH8CdRUw77C8115YkzLQZ8EzKnGMmIZc6EEZE1OA8m0fT1_Axlamvzal8WWXtE52jNmVOZ-T3mrAzwenR5xcn0SgiV72CRgNagQiJpW09JPOn5x2NoKRTQsQPRzzAzKCmNfvuFlHhSoWc7gqa_zljF2Emx9D20JDF27U8gQNbnMLhzJPfZzCKxwmjPgSSe2AfFVuVhsS3rGHZhiGQY7b43awse3MNtO8cnT-p6eB-w1DF4nO4nSQv4ymvf2DhN1K12A17cAHNoizsJTDMOawyTvpRhTkGF8zirBiGOtPS5EZeQXfPizp7rV042p6a0nMNzfX3j73BsLvOetBQqer5Kf4DRLSFRA |
link.rule.ids | 315,786,790,12083,21416,27955,27956,31752,33777,43343,43838,74100,74657 |
linkProvider | ProQuest |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1NS8NAEB20gnoRP1HrxyJeF5tmN9meSigtUZueKgREAsluwUOTauqh_npntptehEJuC_kc5r23M5MH8GiQ0_Y6M8WVIQszpX2eS1lwVBJyprqe9gIacE4mQfwmXlKZut6c2rVVNjnRJmpdFbRH_qSIOxOd7i--OJlGUXHVOWjswp7wfUFhHqYbvYXAaH0Q8bIB76IuaIqaHfsPUc82ClnXFVz-l4otvoyO4cgRQxatv-QJ7JjyFPYTV_o-g340GDKaQiCzB_ZZs3mlyXrLaJavGNI4Zsrf1dywdzs--8Ex9ZOXDkYbAhWLzuFhNJwOYt7cQObCqM42D-1fQKusSnMJDBWHCbU1fgxFgdCCGs54PaFyJXWh5RW0t5zoeuvqPRzE02ScjZ8nr204XO-f0nEDreX3j7lFAF7md_Y1_wEwg4Xk |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1La8MwDBZbB2WX0b3Y1j3M2NU0aePEPZXQNnSPlh02CIwRSOzADk3Wpjt0v36S6_QyKPhmMEY2-vRZkj-AB40xbd_JJZeaJMyk6vFUiIwjkxC57LrK9anBeTrzJ-_eUyxi-6VQZcsqa59oHLUqM3oj70iKnSmc7uS2KuJ1FA2-F5wEpCjRatU09uEAQdIhFYcg3nIvBEmjiYhb8HkXOUKd4HTMf6KuKRoyCiw4_c8tG6yJWnBkg0QWbk71GPZ0cQLNqU2Dn8IgHI4ZdSSQ8AP7qti8VCTDpRVL1wxDOqaL3_Vcsw_TSvvJEQZIVwdvHoIWC8_gPhq_DSe83kBir1SVbA3QO4dGURb6AhiyDx0oIwIZeBnCDPI57fY9mUqhMiUuob1joauds3fQRAsnL4-z5zYcbp5SaVxDY7X80TeIxav01lj5D_H-ihA |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=ACE+activity+is+modulated+by+the+enzyme+%5Balpha%5D-galactosidase+A&rft.jtitle=Journal+of+molecular+medicine+%28Berlin%2C+Germany%29&rft.au=Batista%2C+Elice+Carneiro&rft.au=Carvalho%2C+Luiz+Roberto&rft.au=Casarini%2C+Dulce+Elena&rft.au=Carmona%2C+Adriana+Karaoglanovic&rft.date=2011-01-01&rft.pub=Springer+Nature+B.V&rft.issn=0946-2716&rft.eissn=1432-1440&rft.volume=89&rft.issue=1&rft.spage=65&rft_id=info:doi/10.1007%2Fs00109-010-0686-2&rft.externalDBID=HAS_PDF_LINK&rft.externalDocID=2225959391 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0946-2716&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0946-2716&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0946-2716&client=summon |