Document Detail


Induction of peptidylglycine alpha-amidating monooxygenase in N(18)TG(2) cells: a model for studying oleamide biosynthesis.
MedLine Citation:
PMID:  10631094     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The fatty-acid primary amide, oleamide, is a novel signaling molecule whose mechanism of biosynthesis is unknown. Recently, the N(18)TG(2) cell line was shown to synthesize oleamide from oleic acid, thereby demonstrating that these cells contain the necessary catalytic activities for generating the fatty-acid primary amide. The ability of peptide alpha-amidating enzyme, peptidylglycine-alpha-amidating monooxygenase (PAM; EC 1.14.17.3), to catalyze the formation of oleamide from oleoylglycine in vitro suggests this as a function for the enzyme in vivo. This investigation shows that N(18)TG(2) cells, in fact, express PAM and that cellular differentiation dramatically increases this expression. PAM expression was confirmed by the detection of PAM mRNA, PAM protein, and enzymatic activity that exhibits the functional characteristics of PAM isolated from mammalian neuroendocrine tissues. The regulated expression of PAM in N(18)TG(2) cells is consistent with the proposed role of PAM in the biosynthesis of fatty-acid primary amides and further establishes this cell line as a model for studying the pathway.
Authors:
K J Ritenour-Rodgers; W J Driscoll; K A Merkler; D J Merkler; G P Mueller
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  267     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2000 Jan 
Date Detail:
Created Date:  2000-02-23     Completed Date:  2000-02-23     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  521-6     Citation Subset:  IM    
Copyright Information:
Copyright 2000 Academic Press.
Affiliation:
Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Base Sequence
Cell Differentiation
DNA Primers / genetics
Enzyme Induction
Mice
Mixed Function Oxygenases / biosynthesis*,  genetics
Models, Biological
Multienzyme Complexes*
Neuroblastoma / enzymology,  genetics,  pathology
Oleic Acids / biosynthesis*
RNA, Messenger / genetics,  metabolism
RNA, Neoplasm / genetics,  metabolism
Tumor Cells, Cultured
Grant Support
ID/Acronym/Agency:
NS34173/NS/NINDS NIH HHS; R15-GM59050/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Multienzyme Complexes; 0/Oleic Acids; 0/RNA, Messenger; 0/RNA, Neoplasm; 301-02-0/oleylamide; EC 1.-/Mixed Function Oxygenases; EC 1.14.17.3/peptidylglycine monooxygenase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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