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Cloning and functional studies of a splice variant of CYP26B1: a cellular storage protein for all-trans retinoic acid
Örebro universitet, Hälsoakademin.
Örebro universitet, Hälsoakademin.ORCID-id: 0000-0002-2244-9816
Örebro universitet, Akademin för naturvetenskap och teknik. (Biofysikalisk kemi)
Örebro universitet, Hälsoakademin.
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2010 (Engelska)Ingår i: In Vivo, ISSN 0258-851X, E-ISSN 1791-7549, Vol. 24, nr 3, s. 345-346Artikel i tidskrift, Meeting abstract (Refereegranskat) Published
Abstract [en]

Background

All-trans retinoic acid (atRA) plays an essential role in the regulation of gene expression, cell growth and differentiation and is also important for normal cardiovascular development but may in turn be involved in cardiovascular diseases, i.e. atherosclerosis and restenosis. The cellular atRA levels are under strict control involving several cytochromes P450 isoforms (CYPs). CYP26 may be the most important regulator of atRA catabolism in vascular cells. The present study describes the molecular cloning, characterization and function of atRA-induced expression of a spliced variant of the CYP26B1 gene.

Methodology/Principal Findings

The coding region of the spliced CYP26B1 lacking exon 2 was amplified from cDNA synthesized from atRA-treated human aortic smooth muscle cells and sequenced. Both the spliced variant and full length CYP26B1 was found to be expressed in cultured human endothelial and smooth muscle cells, and in normal and atherosclerotic vessel. atRA induced both variants of CYP26B1 in cultured vascular cells. Furthermore, the levels of spliced mRNA transcript were 4.5 times higher in the atherosclerotic lesion compared to normal arteries and the expression in the lesions was increased 20-fold upon atRA treatment. The spliced CYP26B1 still has the capability to degrade atRA, but at an initial rate one-third that of the corresponding full length enzyme. Transfection of COS-1 and THP-1 cells with the CYP26B1 spliced variant indicated either an increase or a decrease in the catabolism of atRA, probably depending on the expression of other atRA catabolizing enzymes in the cells.

Conclusions/Significance

Vascular cells express the spliced variant of CYP26B1 lacking exon 2 and it is also increased in atherosclerotic lesions. The spliced variant displays a slower and reduced degradation of atRA as compared to the full-length enzyme. Further studies are needed, however, to clarify the substrate specificity and role of the CYP26B1 splice variant in health and disease.

Ort, förlag, år, upplaga, sidor
2010. Vol. 24, nr 3, s. 345-346
Nationell ämneskategori
Medicin och hälsovetenskap Kemi
Forskningsämne
Biomedicin; Biokemi
Identifikatorer
URN: urn:nbn:se:oru:diva-14227OAI: oai:DiVA.org:oru-14227DiVA, id: diva2:391646
Anmärkning

Abstracts of the 3rd Swedish-Hellenic life sciences research conference

Tillgänglig från: 2012-08-06 Skapad: 2011-01-25 Senast uppdaterad: 2019-03-26Bibliografiskt granskad

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Elmabsout, AliKumawat, Ashok K.Karlsson, MagnusKrivospitskaya, OlesyaSävenstrand, HelenaStrid, ÅkeEriksson, Leif ASirsjö, Allan

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Av författaren/redaktören
Elmabsout, AliKumawat, Ashok K.Karlsson, MagnusKrivospitskaya, OlesyaSävenstrand, HelenaStrid, ÅkeEriksson, Leif ASirsjö, Allan
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HälsoakademinAkademin för naturvetenskap och teknik
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In Vivo
Medicin och hälsovetenskapKemi

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