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The role of alternative splicing and C-terminal amino acids in thromboxane receptor stabilization.

Abstract：

:The thromboxane receptor has two alternatively spliced isoforms, alpha and beta, which differ only in sequences within the cytoplasmic C-terminal domain. Oxidative stress induced by H(2)O(2) in a COS-7 cell model results in stabilization of the thromboxane receptor beta isoform by translocation from the endoplasmic reticulum to the Golgi complex, which in turn results in protection of the receptor from degradation. We now report that both the alpha and beta thromboxane receptor isoforms respond identically to oxidative stress. Further, mutagenesis studies indicate that replacing the normal C-terminus with a nonsense sequence also does not alter stabilization behaviour ruling out a role for the distinct C-termini in this process. Further mutagenesis implicates a cluster of arginine residues within the C-terminal domain as involved in oxidative stress-induced stabilization. These data identify a region of the thromboxane receptor that is responsible for responding to oxidative challenge and open the possibility of identification of the molecular machinery underpinning this response.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Valentin F,Tippins JR,Field MC

doi

10.1016/j.bbrc.2005.02.058

subject

Has Abstract

pub_date

2005-04-15 00:00:00

pages

898-904

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)00299-8

journal_volume

329

pub_type

杂志文章

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