scholarly journals MicroRNA-155 Promotes Myocardial Infarction-Induced Apoptosis by Targeting RNA-Binding Protein QKI

2019 ◽  
Vol 2019 ◽  
pp. 1-14 ◽  
Author(s):  
Jing Guo ◽  
Hui-Bin Liu ◽  
Chuan Sun ◽  
Xiu-Qing Yan ◽  
Juan Hu ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Cell Apoptosis ◽  
Caspase 3 ◽  
Rna Binding ◽  
Apoptotic Cell ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Cell Number ◽  
Neonatal Rat

Acute myocardial infarction (AMI) is the leading cause of sudden death worldwide. MicroRNA-155 (miR-155) has been reported to target antiapoptotic genes in various diseases models, but the functional role of miR-155 in response to MI injury needs further investigations. This study investigated the role of miR-155 in myocardial ischemia injury. TUNEL and flow cytometry were performed to measure cell apoptosis. Western blot analysis was employed to detect protein expressions of Bcl-2, XIAP, Bax, and caspase-3. qRT-PCR was used to quantify miRNA levels. We showed that miR-155 was dynamically elevated in murine hearts subjected to MI and in neonatal rat ventricular cardiomyocyte (NRVM) injury induced by hydrogen peroxide (H2O2). In response to H2O2, the silencing of miR-155 using AMO-155 (antisense inhibitor oligodeoxyribonucleotides) significantly increased cell viability and reduced cell apoptosis. Moreover, AMO-155 reversed the H2O2-induced downregulation of Bcl-2 and XIAP and upregulation of Bax and cleaved-caspase-3. Further study revealed that AMO-155 resulted in a decrease of H2O2-induced JC-1-labelled monomeric cell number. In addition, AMO-155 markedly decreased infarct size, ameliorated impaired cardiac function, and significantly reduced apoptotic cell percentages in MI mice heart. The RNA-binding protein Quaking (QKI) was predicted as a target gene of miR-155 through bioinformatic analysis, and AMO-155 attenuated the downregulation of QKI in H2O2-treated cardiomyocytes and MI mice heart. Knockdown of QKI by siRNA abolished the antiapoptotic effects of AMO-155. Taken together, miR-155 is upregulated in the MI heart and NRVMs in response to H2O2 stress, and downregulating of miR-155 protects cardiomyocytes against apoptosis. Mechanistically, it is probably due to the repression of QKI signaling pathway.

scholarly journals Critical role of tristetraprolin and AU‐rich element RNA‐binding protein 1 in the suppression of cancer cell growth by globular adiponectin

FEBS Open Bio ◽  
2018 ◽  
Vol 8 (12) ◽  
pp. 1964-1976 ◽  
Author(s):  
Nirmala Tilija Pun ◽  
Amrita Khakurel ◽  
Aastha Shrestha ◽  
Sang‐Hyun Kim ◽  
Pil‐Hoon Park
Keyword(s):  
Cell Growth ◽  
Cancer Cell ◽  
Rna Binding ◽  
Binding Protein ◽  
Critical Role ◽  
Rna Binding Protein ◽  
Cancer Cell Growth ◽  
Globular Adiponectin

scholarly journals The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases

2016 ◽  
Vol 44 (5) ◽  
pp. 1321-1337 ◽  
Author(s):  
Andrew R. Clark ◽  
Jonathan L.E. Dean
Keyword(s):  
Inflammatory Mediators ◽  
Knockout Mouse ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Human Orthologue ◽  
And Function ◽  
Detailed Picture ◽  
Lines Of Evidence

Twenty years ago, the first description of a tristetraprolin (TTP) knockout mouse highlighted the fundamental role of TTP in the restraint of inflammation. Since then, work from several groups has generated a detailed picture of the expression and function of TTP. It is a sequence-specific RNA-binding protein that orchestrates the deadenylation and degradation of several mRNAs encoding inflammatory mediators. It is very extensively post-translationally modified, with more than 30 phosphorylations that are supported by at least two independent lines of evidence. The phosphorylation of two particular residues, serines 52 and 178 of mouse TTP (serines 60 and 186 of the human orthologue), has profound effects on the expression, function and localisation of TTP. Here, we discuss the control of TTP biology via its phosphorylation and dephosphorylation, with a particular focus on recent advances and on questions that remain unanswered.

scholarly journals Role of RNA‐binding protein HuR and CUGBP1 in LPS‐induced Interleukin‐6 Expression in Macrophages

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Weibin Zha ◽  
Guangji Wang ◽  
Beth S. Pecora ◽  
Elaine Studer ◽  
Phillip B Hylemon ◽  
...  
Keyword(s):  
Interleukin 6 ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals The role of the RNA-binding protein Sam68 in mammary tumourigenesis

2010 ◽  
Vol 222 (3) ◽  
pp. 223-226 ◽  
Author(s):  
David J Elliott ◽  
Prabhakar Rajan
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

Chitin binding protein as a possible RNA binding protein in Leishmania parasites

2020 ◽  
Vol 78 (1) ◽  
Author(s):  
Sajad Rashidi ◽  
Kurosh Kalantar ◽  
Celia Fernandez-Rubio ◽  
Enayat Anvari ◽  
Paul Nguewa ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Novel Proteins ◽  
Transcriptional Gene Regulation ◽  
Chitin Binding Protein ◽  
Effective Drugs ◽  
Genus Leishmania ◽  
Leishmania Parasites

ABSTRACT Leishmaniasis includes a broad spectrum of pathological outcomes in humans caused by protozoan parasites from the genus Leishmania. In recent years, proteomic techniques have introduced novel proteins with critical functions in Leishmania parasites. Based on our report of a Chitin binding protein (CBP) in our previous immunoproteomic study, this article suggests that CBP might be an RNA binding protein (RBP) in Leishmania parasites. RBPs, as key regulatory factors, have a role in post-transcriptional gene regulation. The presence of RBPs in Leishmania parasites has not been considered so far; however, this study aims to open a new venue regarding RBPs in Leishmania parasites. Confirming CBP as an RBP in Leishmania parasites, exploring other RBPs and their functions might lead to interesting issues in leishmaniasis. In fact, due to the regulatory role of RBPs in different diseases including cancers and their further classification as therapeutic targets, the emerging evaluation of CBP and RBPs from Leishmania parasites may allow the discovery of novel and effective drugs against leishmaniasis.

scholarly journals The RNA-Binding Protein Hfq of Listeria monocytogenes: Role in Stress Tolerance and Virulence

2004 ◽  
Vol 186 (11) ◽  
pp. 3355-3362 ◽  
Author(s):  
Janne K. Christiansen ◽  
Marianne H. Larsen ◽  
Hanne Ingmer ◽  
Lotte Søgaard-Andersen ◽  
Birgitte H. Kallipolitis
Keyword(s):  
Listeria Monocytogenes ◽  
Stress Tolerance ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stationary Growth Phase ◽  
Ethanol Stress ◽  
Gram Positive ◽  
Term Survival

ABSTRACT In gram-negative bacteria, the RNA-binding protein Hfq has emerged as an important regulatory factor in a variety of physiological processes, including stress resistance and virulence. In Escherichia coli, Hfq modulates the stability or the translation of mRNAs and interacts with numerous small regulatory RNAs. Here, we studied the role of Hfq in the stress tolerance and virulence of the gram-positive food-borne human pathogen Listeria monocytogenes. We present evidence that Hfq is involved in the ability of L. monocytogenes to tolerate osmotic and ethanol stress and contributes to long-term survival under amino acid-limiting conditions. However, Hfq is not required for resistance to acid and oxidative stress. Transcription of hfq is induced under various stress conditions, including osmotic and ethanol stress and at the entry into the stationary growth phase, thus supporting the view that Hfq is important for the growth and survival of L. monocytogenes in harsh environments. The stress-inducible transcription of hfq depends on the alternative sigma factor σB, which controls the expression of numerous stress- and virulence-associated genes in L. monocytogenes. Infection studies showed that Hfq contributes to pathogenesis in mice, yet plays no role in the infection of cultured cell lines. This study provides, for the first time, information on the role of Hfq in the stress tolerance and virulence of a gram-positive pathogen.

The role of thymidylate synthase as an RNA binding protein

BioEssays ◽  
1996 ◽  
Vol 18 (3) ◽  
pp. 191-198 ◽  
Author(s):  
Edward Chu ◽  
Carmen J. Allegra
Keyword(s):  
Thymidylate Synthase ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein
Sign in / Sign up

Export Citation Format

Share Document