Agonist-Mediated Down-Regulation of Rat β<sub>1</sub>-Adrenergic Receptor Transcripts: Role of Potential Post-Transcriptional Degradation Factors

Kirigiti, Philbert; Bai, Ying; Ys, Yang; Li, Xiaorong; Li, Biao; Brewer, Gary; Machida, Curtis A.

doi:10.1124/mol.60.6.1308

Cited by 23 publications

(23 citation statements)

References 37 publications

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“…ET B receptors, which mediate relaxation in gastric fundus strips [20], were unchanged. The ET A and ET B receptors are G protein-coupled receptors, which have been shown to have a half-life of approximately 40 min [23]. Therefore, our findings of increased mRNA levels of both endothelin receptors appear plausible.…”

Section: Discussionmentioning

confidence: 56%

Vasopressin Aggravates Cardiopulmonary Bypass-Induced Gastric Mucosal Ischemia

Bomberg

Bierbach²,

Flache³

et al. 2014

Eur Surg Res

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Background/Aim: Upper gastrointestinal bleeding (UGIB) is one of the most frequent gastrointestinal complications after cardiac surgery with cardiopulmonary bypass (CPB). Endothelin expression and microcirculatory dysfunction have been shown to be involved in UGIB. The aim of this study was to analyze the effect of vasopressin during CPB on the gastric mucosal microcirculation and the involvement of the endothelin system. Methods: Eighteen pigs were randomized into three groups (n = 6 each): group I = sham, group II = CPB (1-hour CPB) and group III = CPB + vasopressin (1-hour CPB and vasopressin administration during CPB to maintain baseline arterial pressure). All animals were observed for a further 90 min after termination of CPB. Systemic hemodynamics as well as blood flow and oxygen saturation of the gastric mucosa were measured continuously. At the end of the experiment, the gastric mucosal expressions of endothelin-1 (ET-1) and its receptor subtypes A (ET_A) and B (ET_B) were determined by polymerase chain reaction. Gastric mucosal injury, apoptotic cell death and leukocytic infiltration were determined by histology and immunohistochemical analyses of cleaved caspase-3 and myeloperoxidase. Results: CPB decreased gastric microvascular perfusion, which was associated with an increased expression of ET-1 and ET_A. Vasopressin aggravated the CPB-associated malperfusion, whereas it completely abrogated the upregulation of ET-1 and ET_A. Interestingly, vasopressin did not induce gastric mucosal morphologic injury, leukocytic infiltration or apoptotic cell death. Conclusion: Vasopressin aggravates CPB-associated microvascular malperfusion of the gastric mucosa but does not induce gastric mucosal injury.

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Section: Discussionmentioning

confidence: 56%

Vasopressin Aggravates Cardiopulmonary Bypass-Induced Gastric Mucosal Ischemia

Bomberg

Bierbach²,

Flache³

et al. 2014

Eur Surg Res

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“…Upon exposure of rat C6 glioma cells to a β 1 ‐adrenergic receptor agonist, an up‐regulation of the constitutively expressed RNA binding protein, HuR, is observed. Up‐regulation of HuR results in a concomitant decrease in the β 1 ‐adrenergic receptor mRNA half‐life, indicating that HuR plays a role in both agonist‐independent and agonist‐dependent post‐transcriptional regulation of the β 1 ‐adrenergic receptor mRNA (Kirigiti et al ., 2001).…”

Section: Discussionmentioning

confidence: 99%

A novel RNA binding protein that interacts with NMDA R1 mRNA: regulation by ethanol

Anji

2006

Eur J of Neuroscience

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Excitatory NMDA receptors are an important target of ethanol. Chronic ethanol exposure, in vivo and in vitro, increases polypeptide levels of NR1 subunit, the key subunit of functional NMDA receptors. In vitro, chronic ethanol treatment increases the half-life of NR1 mRNA and this observation is dependent on new protein synthesis. The present study was undertaken to locate cis-acting region(s) within the NR1 3'-untranslated region (UTR) and identify NR1 3'-UTR binding trans-acting proteins expressed in mouse fetal cortical neurons. Utilizing RNA gel shift assays we identified a 156-nt cis-acting region that binds to polysomal trans-acting proteins. This binding was highly specific as inclusion of cyclophilin RNA or tRNA did not interfere with cis-trans interactions. Importantly, the 3'-UTR binding activity was significantly up-regulated in the presence of ethanol. UV cross-link analysis detected three NR1 3'-UTR binding proteins and their molecular mass calculated by Northwestern analysis was approximately 88, 60 and 47 kDa, respectively. Northwestern analysis showed a significant up-regulation of the 88-kDa protein after chronic ethanol treatment. The 88-kDa protein was purified and identified by tandem mass spectrometry as the beta subunit of alpha glucosidase II (GIIbeta). That GIIbeta is indeed a trans-acting protein and binds specifically to 3'-UTR of NR1 mRNA was confirmed by RNA gel mobility supershift assays and immuno RT-PCR. Western blotting data established a significant increase of GIIbeta polypeptide in chronic ethanol-exposed fetal cortical neurons. We hypothesize that the identified cis-acting region and the associated RNA-binding proteins are important regulators of NR1 subunit gene expression.

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“…HuR has been reported to selectively stabilize ARE-containing mRNAs (55,56). Although HuR has been reported to bind ␤ 1 and ␤ 2 -AR mRNAs (57,58), its role in receptor mRNA regulation is not understood. From the present data, it is not possible to conclude whether the translational suppression and stabilization is achieved by the same protein or by different proteins that bind to different regions in the 3Ј-UTR of the receptor mRNA.…”

Section: Discussionmentioning

confidence: 99%

Translational Control of β2-Adrenergic Receptor mRNA by T-cell-restricted Intracellular Antigen-related Protein

Kandasamy

Joseph

Subramaniam

et al. 2005

Journal of Biological Chemistry

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Cellular expression of the ␤ 2 -adrenergic receptor (␤ 2 -AR) is suppressed at the translational level by 3-untranslated region (UTR) sequences. To test the possible role of 3-UTR-binding proteins in translational suppression of ␤ 2 -AR mRNA, we expressed the full-length 3-UTR or the adenylate/uridylate-rich (A؉U-rich element (ARE)) RNA from the 3-UTR sequences of ␤ 2 -AR in cell lines that endogenously express this receptor. Reversal of ␤ 2 -adrenergic receptor translational repression by retroviral expression of 3-UTR sequences suggested that ARE RNA-binding proteins are involved in translational suppression of ␤ 2 -adrenergic receptor expression. Using a 20-nucleotide ARE RNA from the receptor 3-UTR as an affinity ligand, we purified the proteins that bind to these sequences. T-cell-restricted intracellular antigen-related protein (TIAR) was one of the strongly bound proteins identified by this method. UV-catalyzed cross-linking experiments using in vitro transcribed 3-UTR RNA and glutathione S-transferase-TIAR demonstrated multiple binding sites for this protein on ␤ 2 -AR 3-UTR sequences. The distal 340-nucleotide region of the 3-UTR was identified as a target RNA motif for TIAR binding by both RNA gel shift analysis and immunoprecipitation experiments. Overexpression of TIAR resulted in suppression of receptor protein synthesis and a significant shift in endogenously expressed ␤ 2 -AR mRNA toward low molecular weight fractions in sucrose gradient polysome fractionation. Taken together, our results provide the first evidence for translational control of ␤ 2 -AR mRNA by TIAR.1 are low abundance membrane-integrated G-protein-coupled receptors that are activated by catecholamines at the cell surface. ␤ 2 -AR mRNA is transcribed from a single intronless gene (1-3), and both transcriptional (4) and post-transcriptional mechanisms (5-10) are known to regulate receptor expression. Post-transcriptional mechanisms include regulation at the level of receptor mRNA translation (5-7) as well as regulation of mRNA stability (8, 9). A highly conserved 5Ј-leader cistron present in the 5Ј-untranslated region (UTR) of this receptor inhibits the translation of receptor mRNA (5, 6). ␤ 2 -Adrenergic receptors from several mammalian species have a highly conserved 3Ј-untranslated region (10) with multiple adenine/uridine-rich (ARE) regions (11-13). The 3Ј-untranslated region of the ␤ 2 -adrenergic receptor contains regulatory elements that can alter stability of the receptor transcript in response to agonist challenge (11-13). Recently, we demonstrated that the 3Ј-UTR sequences negatively regulate the translation of the receptor mRNA (7).The modulation of translational efficiency is an important post-transcriptional control mechanism for eukaryotic gene expression. In most cases, translational control results from interaction of RNA-binding proteins with the 5Ј-and/or 3Ј-UTR sequences (14 -28). Many sequence-specific RNA-binding proteins that bind to 3Ј-UTR of mRNAs have also been identified (29 -33). These interacting proteins ...

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Agonist-Mediated Down-Regulation of Rat β₁-Adrenergic Receptor Transcripts: Role of Potential Post-Transcriptional Degradation Factors

Cited by 23 publications

References 37 publications

Vasopressin Aggravates Cardiopulmonary Bypass-Induced Gastric Mucosal Ischemia

Vasopressin Aggravates Cardiopulmonary Bypass-Induced Gastric Mucosal Ischemia

A novel RNA binding protein that interacts with NMDA R1 mRNA: regulation by ethanol

Translational Control of β2-Adrenergic Receptor mRNA by T-cell-restricted Intracellular Antigen-related Protein

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Agonist-Mediated Down-Regulation of Rat β1-Adrenergic Receptor Transcripts: Role of Potential Post-Transcriptional Degradation Factors

Cited by 23 publications

References 37 publications

Vasopressin Aggravates Cardiopulmonary Bypass-Induced Gastric Mucosal Ischemia

Vasopressin Aggravates Cardiopulmonary Bypass-Induced Gastric Mucosal Ischemia

A novel RNA binding protein that interacts with NMDA R1 mRNA: regulation by ethanol

Translational Control of β2-Adrenergic Receptor mRNA by T-cell-restricted Intracellular Antigen-related Protein

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Agonist-Mediated Down-Regulation of Rat β₁-Adrenergic Receptor Transcripts: Role of Potential Post-Transcriptional Degradation Factors