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Translation of the human angiotensin II type 1 receptor mRNA is mediated by a highly efficient internal ribosome entry site.

Abstract：

:Activation of the angiotensin II type 1 receptor (AT1R) is closely involved in the pathogenesis of cardiovascular disease. The human AT1R (hAT1R) mRNA splice variants have long 5'-untranslated regions (5'-UTRs) ranging from 272 to 414 bp that have the potential to form stable secondary structures. In this study, we show that the 5'-UTR of hAT(1)R mRNAs contains an internal ribosome entry site (IRES) located within the first 40 bp of the proximal end of exon 1. Experiments utilizing the hAT1R 5'-UTR as a molecular decoy demonstrate a reduction in IRES activity of approximately 50%. This inhibition is most efficient for the hAT1R IRES suggesting that a defined set of trans-factors are required to initiate translation through this cis-element. Translation initiation from the hAT1R IRES appears to be physiologically relevant since IRES activity was maintained during serum starvation, a cellular stress known to inhibit cap-dependent translation. These results suggest that cap-independent translation initiation by internal ribosome entry may represent an important mechanism for the regulation of hAT1R expression.

journal_name

Mol Cell Endocrinol

journal_title

Molecular and cellular endocrinology

authors

Martin MM,Garcia JA,McFarland JD,Duffy AA,Gregson JP,Elton TS

doi

10.1016/j.mce.2003.09.017

keywords:

subject

Has Abstract

pub_date

2003-12-30 00:00:00

pages

51-61

issue

1-2

eissn

0303-7207

issn

1872-8057

pii

S0303720703003320

journal_volume

212

pub_type

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