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Titolo:
COMPARATIVE CHARACTERIZATION OF A WILD-TYPE AND TRANSMEMBRANE DOMAIN-DELETED FATTY-ACID AMIDE HYDROLASE - IDENTIFICATION OF THE TRANSMEMBRANE DOMAIN AS A SITE FOR OLIGOMERIZATION
Autore:
PATRICELLI MP; LASHUEL HA; GIANG DK; KELLY JW; CRAVATT BF;
Indirizzi:
SCRIPPS RES INST,SKAGGS INST CHEM BIOL,DEPT CELL BIOL,10550 N TORREY PINES RD LA JOLLA CA 92037 SCRIPPS RES INST,SKAGGS INST CHEM BIOL,DEPT CELL BIOL LA JOLLA CA 92037 SCRIPPS RES INST,DEPT CHEM LA JOLLA CA 92037
Titolo Testata:
Biochemistry (Easton)
fascicolo: 43, volume: 37, anno: 1998,
pagine: 15177 - 15187
SICI:
0006-2960(1998)37:43<15177:CCOAWA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
SEDIMENTATION-VELOCITY EXPERIMENTS; ASPERGILLUS-NIDULANS; MOLECULAR CHARACTERIZATION; BOUNDARY ANALYSIS; ANANDAMIDE AMIDOHYDROLASE; CANNABINOID RECEPTOR; NUCLEOTIDE-SEQUENCE; NITRILE HYDRATASE; AMDS GENE; SLEEP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
M.P. Patricelli et al., "COMPARATIVE CHARACTERIZATION OF A WILD-TYPE AND TRANSMEMBRANE DOMAIN-DELETED FATTY-ACID AMIDE HYDROLASE - IDENTIFICATION OF THE TRANSMEMBRANE DOMAIN AS A SITE FOR OLIGOMERIZATION", Biochemistry (Easton), 37(43), 1998, pp. 15177-15187

Abstract

Fatty acid amide hydrolase (FAAH) is an integral membrane protein responsible for the hydrolysis of a number of primary and secondary fattyacid amides, including the neuromodulatory compounds anandamide and oleamide. Analysis of FAAH's primary sequence reveals the presence of asingle predicted transmembrane domain at the extreme N-terminus of the enzyme. A mutant form of the rat FAAH protein lacking this N-terminal transmembrane domain (Delta TM-FAAH) was generated and, like wild type FAAH (WT-FAAH), was found to be tightly associated with membranes when expressed in COS-7 cells. Recombinant forms of WT- and Delta TM-FAAH expressed and purified from Escherichia coli exhibited essentially identical enzymatic properties which were also similar to those of thenative enzyme from rat liver. Analysis of the oligomerization states of WT- and Delta TM-FAAH by chemical cross-linking, sedimentation velocity analytical ultracentrifugation, and size exclusion chromatographyindicated that both enzymes were oligomeric when membrane-bound and after solubilization. However, WT-FAAH consistently behaved as a largeroligomer than Delta TM-FAAH. Additionally, SDS-PAGE analysis of the recombinant proteins identified the presence of SDS-resistant oligomersfor WT-FAAH, but not for Delta TM-FAAH. Self-association through FAAH's transmembrane domain was further demonstrated by a FAAH transmembrane domain-GST fusion protein which formed SDS-resistant dimers and large oligomeric assemblies in solution.

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Documento generato il 08/04/20 alle ore 23:51:24