Regulation of prostaglandin synthesis and cell adhesion by a tryptophan catabolizing enzyme.

Hdl Handle:
http://hdl.handle.net/10675.2/53
Title:
Regulation of prostaglandin synthesis and cell adhesion by a tryptophan catabolizing enzyme.
Authors:
Marshall, Brendan; Keskin, Derin B.; Mellor, Andrew L.
Abstract:
BACKGROUND: The tryptophan catabolizing enzyme, indoleamine 2,3, dioxygenase (IDO) is one of two mammalian enzymes, which can catabolize the rarest essential amino acid, tryptophan. IDO is inducible by cytokines such as interferon-gamma and plays a role in inflammation and maternal tolerance of fetal allografts, although its exact mode of action is unclear. Therefore, we investigated the circumstances under which IDO is expressed in vitro together with the effects of overexpression of IDO on the growth and morphology of cells. RESULTS: Overexpression of IDO in the murine macrophage cell line RAW 264.7 and the murine fibrosarcoma cell line MC57, resulted in the growth of macroscopic cell foci, with altered cell adhesion properties. The expression of IDO was also detected during adhesion of wild type, nontransfected cells in tissue culture to standard cell growth substrates. Inhibition of this expression, likewise resulted in alterations in cell adhesion. Overexpression of IDO or inhibition of endogenous IDO expression was accompanied by changes in metalloproteinase expression and also in the expression and activity of the cyclooxygenase enzymes. In the case of RAW cells, IDO effects on cell growth could be reversed by adding back prostaglandins. CONCLUSIONS: These results suggest that catabolism of the rarest essential amino acid may regulate processes such as cell adhesion and prostaglandin synthesis.
Citation:
BMC Biochem. 2001 May 17; 2:5
Issue Date:
19-Nov-2002
URI:
http://hdl.handle.net/10675.2/53
PubMed ID:
11375052
PubMed Central ID:
PMC31925
Type:
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
ISSN:
1471-2091
Appears in Collections:
Institute of Molecular Medicine and Genetics: Faculty Research and Publications

Full metadata record

DC FieldValue Language
dc.contributor.authorMarshall, Brendanen_US
dc.contributor.authorKeskin, Derin B.en_US
dc.contributor.authorMellor, Andrew L.en_US
dc.date.accessioned2010-09-24T21:26:48Z-
dc.date.available2010-09-24T21:26:48Z-
dc.date.issued2002-11-19en_US
dc.identifier.citationBMC Biochem. 2001 May 17; 2:5en_US
dc.identifier.issn1471-2091en_US
dc.identifier.pmid11375052en_US
dc.identifier.urihttp://hdl.handle.net/10675.2/53-
dc.description.abstractBACKGROUND: The tryptophan catabolizing enzyme, indoleamine 2,3, dioxygenase (IDO) is one of two mammalian enzymes, which can catabolize the rarest essential amino acid, tryptophan. IDO is inducible by cytokines such as interferon-gamma and plays a role in inflammation and maternal tolerance of fetal allografts, although its exact mode of action is unclear. Therefore, we investigated the circumstances under which IDO is expressed in vitro together with the effects of overexpression of IDO on the growth and morphology of cells. RESULTS: Overexpression of IDO in the murine macrophage cell line RAW 264.7 and the murine fibrosarcoma cell line MC57, resulted in the growth of macroscopic cell foci, with altered cell adhesion properties. The expression of IDO was also detected during adhesion of wild type, nontransfected cells in tissue culture to standard cell growth substrates. Inhibition of this expression, likewise resulted in alterations in cell adhesion. Overexpression of IDO or inhibition of endogenous IDO expression was accompanied by changes in metalloproteinase expression and also in the expression and activity of the cyclooxygenase enzymes. In the case of RAW cells, IDO effects on cell growth could be reversed by adding back prostaglandins. CONCLUSIONS: These results suggest that catabolism of the rarest essential amino acid may regulate processes such as cell adhesion and prostaglandin synthesis.en_US
dc.rightsThe PMC Open Access Subset is a relatively small part of the total collection of articles in PMC. Articles in the PMC Open Access Subset are still protected by copyright, but are made available under a Creative Commons or similar license that generally allows more liberal redistribution and reuse than a traditional copyrighted work. Please refer to the license statement in each article for specific terms of use. The license terms are not identical for all articles in this subset.en_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Adhesionen_US
dc.subject.meshCell Division / drug effectsen_US
dc.subject.meshCell Lineen_US
dc.subject.meshIndoleamine-Pyrrole 2,3,-Dioxygenaseen_US
dc.subject.meshMetalloendopeptidases / metabolismen_US
dc.subject.meshMiceen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshProstaglandin-Endoperoxide Synthases / metabolismen_US
dc.subject.meshProstaglandins / biosynthesis / pharmacologyen_US
dc.subject.meshRNA, Antisense / pharmacologyen_US
dc.subject.meshTransfectionen_US
dc.subject.meshTryptophan / metabolismen_US
dc.subject.meshTryptophan Oxygenase / antagonists & inhibitors / genetics / physiologyen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.titleRegulation of prostaglandin synthesis and cell adhesion by a tryptophan catabolizing enzyme.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
dc.typeResearch Support, U.S. Gov't, P.H.S.en_US
dc.identifier.pmcidPMC31925en_US
dc.contributor.corporatenameInstitute of Molecular Medicine and Geneticsen_US

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