Immunohistochemical Localization of the Acylases that Catalyze the Deacetylation of N-Acetyl-l-cysteine and Haloalkene-Derived Mercapturates
Acylases catalyze the hydrolysis of a range of S -substituted N -acetyl- l -cysteines. The hydrolysis of N -acetyl- l -cysteine is catalyzed by cytosolic acylase I, and activity is present in human endothelial cells and rat lung, intestinal, and liver homogenates. Many haloalkenes are metabolized to...
Saved in:
Published in | Drug metabolism and disposition Vol. 28; no. 6; pp. 625 - 632 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Pharmacology and Experimental Therapeutics
01.06.2000
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Acylases catalyze the hydrolysis of a range of S -substituted N -acetyl- l -cysteines. The hydrolysis of N -acetyl- l -cysteine is catalyzed by cytosolic acylase I, and activity is present in human endothelial cells and rat lung, intestinal,
and liver homogenates. Many haloalkenes are metabolized to mercapturates, which also undergo acylase-catalyzed hydrolysis.
The acylases that catalyze the deacetylation of N -acetyl- l -cysteine and several haloalkene-derived mercapturates have been recently identified: acylase I catalyzes the deacetylation
of N -acetyl- l -cysteine and some haloalkene-derived mercapturates whereas an acylase purified from rat kidney cytosol catalyzes the deacetylation
of a distinct set of substrates, including several haloalkene-derived mercapturates. The objective of these studies was to
examine the tissue and subcellular localization of acylase I and purified rat kidney acylase. Immunoblotting showed the presence
of immunoreactive acylase I and purified rat kidney acylase in rat kidney, liver, lung, and brain. Both acylases were identified
by immunohistochemistry in several rat organs, including kidney, liver, lung, brain, stomach, intestines, adrenals, pancreas,
and testis, indicating that acylase activity is widespread in rat tissues. |
---|---|
AbstractList | Acylases catalyze the hydrolysis of a range of S -substituted N -acetyl- l -cysteines. The hydrolysis of N -acetyl- l -cysteine is catalyzed by cytosolic acylase I, and activity is present in human endothelial cells and rat lung, intestinal,
and liver homogenates. Many haloalkenes are metabolized to mercapturates, which also undergo acylase-catalyzed hydrolysis.
The acylases that catalyze the deacetylation of N -acetyl- l -cysteine and several haloalkene-derived mercapturates have been recently identified: acylase I catalyzes the deacetylation
of N -acetyl- l -cysteine and some haloalkene-derived mercapturates whereas an acylase purified from rat kidney cytosol catalyzes the deacetylation
of a distinct set of substrates, including several haloalkene-derived mercapturates. The objective of these studies was to
examine the tissue and subcellular localization of acylase I and purified rat kidney acylase. Immunoblotting showed the presence
of immunoreactive acylase I and purified rat kidney acylase in rat kidney, liver, lung, and brain. Both acylases were identified
by immunohistochemistry in several rat organs, including kidney, liver, lung, brain, stomach, intestines, adrenals, pancreas,
and testis, indicating that acylase activity is widespread in rat tissues. Acylases catalyze the hydrolysis of a range of S-substituted N-acetyl-L-cysteines. The hydrolysis of N-acetyl-L-cysteine is catalyzed by cytosolic acylase I, and activity is present in human endothelial cells and rat lung, intestinal, and liver homogenates. Many haloalkenes are metabolized to mercapturates, which also undergo acylase-catalyzed hydrolysis. The acylases that catalyze the deacetylation of N-acetyl-L-cysteine and several haloalkene-derived mercapturates have been recently identified: acylase I catalyzes the deacetylation of N-acetyl-L-cysteine and some haloalkene-derived mercapturates whereas an acylase purified from rat kidney cytosol catalyzes the deacetylation of a distinct set of substrates, including several haloalkene-derived mercapturates. The objective of these studies was to examine the tissue and subcellular localization of acylase I and purified rat kidney acylase. Immunoblotting showed the presence of immunoreactive acylase I and purified rat kidney acylase in rat kidney, liver, lung, and brain. Both acylases were identified by immunohistochemistry in several rat organs, including kidney, liver, lung, brain, stomach, intestines, adrenals, pancreas, and testis, indicating that acylase activity is widespread in rat tissues. |
Author | Daria M. Krenitsky Raymond B. Baggs Vinita Uttamsingh M. W. Anders |
Author_xml | – sequence: 1 givenname: V surname: Uttamsingh fullname: Uttamsingh, V organization: Department of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, New York, USA – sequence: 2 givenname: R B surname: Baggs fullname: Baggs, R B – sequence: 3 givenname: D M surname: Krenitsky fullname: Krenitsky, D M – sequence: 4 givenname: M W surname: Anders fullname: Anders, M W |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10820133$$D View this record in MEDLINE/PubMed |
BookMark | eNo1kM1OwzAQhC1URMvPK6Bc4GbJdmInPlYtUKQCF5C4RVtnSwxOXGIHFJ6BhyaCcpnR7HzawxyTSetbPCAzLgWnjOnnCZmNxqiWUk3JcQivjPEsS_URmXJWCMbTdEa-b5umb31tQ_SmxsYacMnaj2q_IFrfJn6bxBqTuRkcBAxjgJgsIIIbvvC3WiIYjGP9z9_T-e-BOmqGENG2mEBbJStwHtwbtkiX2NkPrJI77AzsYt9BxHBKDrfgAp7t_YQ8XV89LlZ0_XBzu5ivaS3SPNK8UIVhSqHOUALLZJXqbVbkOVSFzjOlFZcKpJaVkULkmyJPgbONKDATQkmTnpDLv7-7zr_3GGLZ2GDQOWjR96HMORc603wEz_dgv2mwKnedbaAbyv_9RuDiD6jtS_1pOyx3NXQNGO_8y1CKolSlEjL9AVS5fXo |
ContentType | Journal Article |
DBID | CGR CUY CVF ECM EIF NPM 7X8 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
DatabaseTitleList | MEDLINE - Academic MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Pharmacy, Therapeutics, & Pharmacology |
EISSN | 1521-009X |
EndPage | 632 |
ExternalDocumentID | 10820133 28_6_625 |
Genre | Research Support, U.S. Gov't, P.H.S Journal Article |
GrantInformation_xml | – fundername: NIEHS NIH HHS grantid: ES01247 – fundername: NIEHS NIH HHS grantid: ES03127 |
GroupedDBID | - 08R 0R 2WC 53G 5GY 5RE 5VS AAPBV AAWZA ABFLS ABSGY ACGFS ACIWK ACPRK ADACO AENEX AFFNX AFRAH ALMA_UNASSIGNED_HOLDINGS CS3 DIK DU5 E3Z EBS EJD F5P FH7 FRP GJ GX1 H13 HZ IH2 INIJC KM KQ8 LSO O0- O9- OK1 P2P R0Z RHF RHI RPT SJN VH1 W2D WH7 WOQ ZGI ZXP --- .GJ 0R~ 18M 4.4 ABJNI ABSQV ACGFO ADBBV AERNN AFOSN AI. BAWUL BTFSW CGR CUY CVF ECM EIF F9R HZ~ NPM TR2 W8F YCJ YHG ~KM 7X8 |
ID | FETCH-LOGICAL-h237t-7868c066e94e5a045d39f4877ad8974696156a595dc5227b873a10b28e42265c3 |
ISSN | 0090-9556 |
IngestDate | Fri Aug 16 00:42:57 EDT 2024 Sat Sep 28 07:35:24 EDT 2024 Tue Jan 05 21:16:59 EST 2021 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 6 |
Language | English |
LinkModel | OpenURL |
MergedId | FETCHMERGED-LOGICAL-h237t-7868c066e94e5a045d39f4877ad8974696156a595dc5227b873a10b28e42265c3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 10820133 |
PQID | 71129491 |
PQPubID | 23479 |
PageCount | 8 |
ParticipantIDs | proquest_miscellaneous_71129491 pubmed_primary_10820133 highwire_pharmacology_28_6_625 |
ProviderPackageCode | RHF RHI |
PublicationCentury | 2000 |
PublicationDate | 2000-Jun |
PublicationDateYYYYMMDD | 2000-06-01 |
PublicationDate_xml | – month: 06 year: 2000 text: 2000-Jun |
PublicationDecade | 2000 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Drug metabolism and disposition |
PublicationTitleAlternate | Drug Metab Dispos |
PublicationYear | 2000 |
Publisher | American Society for Pharmacology and Experimental Therapeutics |
Publisher_xml | – name: American Society for Pharmacology and Experimental Therapeutics |
SSID | ssj0014439 |
Score | 1.8334041 |
Snippet | Acylases catalyze the hydrolysis of a range of S -substituted N -acetyl- l -cysteines. The hydrolysis of N -acetyl- l -cysteine is catalyzed by cytosolic... Acylases catalyze the hydrolysis of a range of S-substituted N-acetyl-L-cysteines. The hydrolysis of N-acetyl-L-cysteine is catalyzed by cytosolic acylase I,... |
SourceID | proquest pubmed highwire |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 625 |
SubjectTerms | Acetylation Acetylcysteine - chemistry Acetylcysteine - metabolism Alkenes - chemistry Alkenes - metabolism Amidohydrolases - analysis Amidohydrolases - metabolism Animals Humans Immunohistochemistry Kidney - chemistry Kidney - enzymology Kidney - metabolism Male Rats Rats, Inbred F344 Sulfonium Compounds - metabolism Tissue Distribution |
Title | Immunohistochemical Localization of the Acylases that Catalyze the Deacetylation of N-Acetyl-l-cysteine and Haloalkene-Derived Mercapturates |
URI | http://dmd.aspetjournals.org/content/28/6/625.abstract https://www.ncbi.nlm.nih.gov/pubmed/10820133 https://search.proquest.com/docview/71129491 |
Volume | 28 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1db9MwFLW6PfGC2PgqjOEHtBdm1Hw5zuPGQIPBNFAr7S1ybGdFtE3VuUjZb9iP3rUdNyl0EvASVbFVNTmn1_de33uM0JssAR9ahZQIJVMSR4ySAtYJAlaSKV7EoVJmR_frOT0dxZ8vk8ter-xULS118U7cbOwr-R9U4R7garpk_wHZ1ZfCDfgM-MIVEIbrX2H8yTR3VFYyWPjGf7s4Nc2VvgCAixqcZCPmMOb6rc3Y1DfKDkkwiUrXk9X8c-JukC9EGJVn44Wa5PqYTyo--QmmkUh4tl_gqE7VQvC5Ee7QTSVi4-WeLJZX5mxqINjEH8Ihf6wKxDzII6351OQqxmvVtse8ydd_b4-EPjNFgbpJ9J60Kdwj25tjs7quVHCVwRi0lVbeKmcDkiVOYNxb5ZB12Nc1sdQ1SnfgnU8tvoH1Zpysxm8a2n5oC21FgSn8PPvW7jXFceSCpOZXGB3ZZn5HNfr-CMR6IsNH6GETQuAjx4cd1FOzXXRw4TTI60M8bFvqrg_xAb5o1cnrx-h2A2lwlzS4KjEwA3vSYEMa7Eljh9ZIY-ZvIA0G0PGfpMFrpHmCRh8_DN-fkuZIDjIOo1STlFEmwEtVWawSDuGAjLISYt6USwaRKc3AQaY8yRIpwLFPC5ZGPBgU8L83HduJiJ6i7Vk1U88RLmVJQ8mkokURq5RyFgZSwIJTBiUrC9pH-_7d5_POi8pDltMcWNBHrz0iOdhEs9HFZ6paXuepCSLiLOijZw6ofO6kW3IP7It7R16iBy1H99C2XizVK_A7dbFvaXMHgLGN-Q |
link.rule.ids | 315,786,790 |
linkProvider | Colorado Alliance of Research Libraries |
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=Immunohistochemical+localization+of+the+acylases+that+catalyze+the+deacetylation+of+N-acetyl-L-cysteine+and+haloalkene-derived+mercapturates&rft.jtitle=Drug+metabolism+and+disposition&rft.au=Uttamsingh%2C+V&rft.au=Baggs%2C+R+B&rft.au=Krenitsky%2C+D+M&rft.au=Anders%2C+M+W&rft.date=2000-06-01&rft.issn=0090-9556&rft.volume=28&rft.issue=6&rft.spage=625&rft_id=info%3Apmid%2F10820133&rft.externalDocID=10820133 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0090-9556&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0090-9556&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0090-9556&client=summon |