Receptor for Activated C Kinase-1 protein from Penaeus monodon (Pm-RACK1) participates in the shrimp antioxidant response

Saelee, Netnapa; Tonganunt-Srithaworn, Moltira; Wanna, Warapond; Phongdara, Amornrat

doi:10.1016/j.ijbiomac.2011.03.012

Cited by 12 publications

(10 citation statements)

References 39 publications

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“…This kinase receptor interacts with the VP9 viral protein of WSSV and involves in the response against viral infection in P. monodon[30]. It can also participate in the shrimp antioxidant response induced by the formation of ROS[31]. This postulates the rVP28P binding mediated signal transduction activation of the kinase receptor and its role in vaccination mediated protective immunity in shrimps.Rab7 is a VP28 binding protein that aids the recognition and entry of WSSV into shrimp cells.…”

mentioning

confidence: 99%

Expression profile of key immune-related genes in Penaeus monodon juveniles after oral administration of recombinant envelope protein VP28 of white spot syndrome virus

Thomas

Sudheer

Kiron

et al. 2016

Microbial Pathogenesis

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mentioning

confidence: 99%

Expression profile of key immune-related genes in Penaeus monodon juveniles after oral administration of recombinant envelope protein VP28 of white spot syndrome virus

Thomas

Sudheer

Kiron

et al. 2016

Microbial Pathogenesis

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“…WB detection of Aeal RACK1 in C6/36 HT showed that untreated cells have low protein level; in previous studies in invertebrates ( Penaeus monodon, Pinctada martensii Choristoneura fumiferana and Crassostrea angulate ) it was documented that RACK1 expression levels vary in tissues according to environmental, metabolic and developmental conditions of the cells [9,25,53,54]. Recent studies also showed that RACK1 expression in Drosophila L3 larva cells is negligible [27].…”

Section: Discussionmentioning

confidence: 99%

“…The expression of both, protein and mRNA Aeal RACK1 increments in C6/36 HT cells under serum deprivation and dexamethasone treatment similarly to those reported in Drosophila larva fat body during starvation, where deletion of RACK1 impaired both basal and starvation-induced autophagy. Under the effect of other stress inductors, RACK1 also increase, in P. monodon RACK1 expression levels rose when animals were treated with hydrogen peroxide and a non-enzymatic antioxidant function has been suggested [9]. Similarly, RACK1 was upregulated in A. thaliana under salt stress [59].…”

Section: Discussionmentioning

confidence: 99%

“…The receptor for activated C kinase 1 (RACK1) is a highly conserved protein [1–5] that contains seven tryptophan-aspartate repeats (WD40). RACK1 is the best characterized member of the WD multidomain scaffold protein family and coordinates a variety of important cell activities such as signal transduction, adhesion, migration, development and immune and stress response among others [6–9]. RACK1 binds specifically to other proteins as the active form of protein kinase C (PKCβ) [10,11], tyrosine kinase Src [12], integrin β subunit [13], β isoform of the thromboxane A2 receptor (TPβ) a G protein-coupled receptor (GPCR) [14], and the Gβγ subunits of heterotrimeric G proteins [15].…”

Section: Introductionmentioning

confidence: 99%

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AealRACK1 expression and localization in response to stress in C6/36 HT mosquito cells

González‐Calixto

Cázares-Raga

Cortés-Martínez

et al. 2015

Journal of Proteomics

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Insect cells adapt to numerous environmental stressors, including chemicals and invasion of pathogenic microorganisms among others, coordinating cellular and organismal responses. Individual cells sense the environment using receptors that trigger signaling pathways that regulate expression of specific effector proteins and/or cellular responses as movement or secretion. In the coordination of responses to stress, scaffold proteins are pivotal molecules that recruit other proteins forming active complexes. The Receptor for Activated C Kinase 1 (RACK1) is the best studied member of the conserved tryptophan-aspartate (WD) repeat family. RACK1 folds in a seven-bladed β-propeller structure and it could be activated during stress, participating in different signaling pathways. The presence and activities of RACK1 in mosquitoes had not been documented before, in this work the molecule is demonstrated in an Aedes albopictus-derived cell line and its reaction to stress is observed under the effect of serum deprivation and the presence of glucocorticoid analog dexamethasone, a chemical used to cause stress in vitro.

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“…RACK1 was originally identified to bind and activate protein kinase C and is now recognized as a multi-functional scaffold protein (11,12). Evidence has indicated that RACK1 protects from oxidative stress-induced cell death in various types of cells, including fission yeasts (13), shrimp cells (14), neurons (15), HeLa cells (16) and HL60 cells (17). However, such a role for RACK1 has not been reported in HCC cells to the best of our knowledge.…”

Section: Introductionmentioning

confidence: 99%

RACK1 promotes hepatocellular carcinoma cell survival via CBR1 by suppressing TNF-α-induced ROS generation

Zhou¹,

Cao²,

Zhao³

et al. 2016

Oncology Letters

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Abstract. It has been reported that intracellular accumulation of reactive oxygen species (ROS) has a significant role in tumor necrosis factor (TNF)-α-induced cell apoptosis and necrosis; however, the key molecules regulating ROS generation remain to be elucidated. The present study reports that knockdown of endogenous receptor for activated C kinase 1 (RACK1) increases the intracellular ROS level following TNF-α or H 2 O 2 stimulation in human hepatocellular carcinoma (HCC) cells, leading to promotion of cell death. Carbonyl reductase 1 (CBR1), a ubiquitous nicotinamide adenine dinucleotide phosphate-dependent enzyme, is reported to protect cells from ROS-induced cell damage. The present study reports that RACK1 is a regulator of CBR1 that interacts with and sustains the protein stability of CBR1. Overexpression of CBR1 reverses the enhanced cell death due to RACK1 knockdown. Taken together, the results of the present study suggest that RACK1 protects HCC cells from TNF-α-induced cell death by suppressing ROS generation through interacting with and regulating CBR1. IntroductionEscape from tumor necrosis factor (TNF)-α-induced cell apoptosis and necrosis is of importance in tumor development (1-3).This process is regulated by a number of intracellular signaling pathways, including c-jun N-terminal kinase (JNK) and IκB kinase (IKK), as well as reactive oxygen species (ROS) (4,5). Extensive studies have indicated that reduced levels of oxidant stress and ROS promote malignant transformation and oncogenic growth in hepatocellular carcinoma (HCC) cells (6-9). However, the key molecules regulating ROS in HCC remain to be elucidated. It has been reported that scaffolding protein receptor for activated C kinase 1 (RACK1) enhances JNK activation in HCC, leading to promotion of the malignant growth of HCC (10). Therefore, it may be assumed that RACK1 affects other aspects of HCC. RACK1 was originally identified to bind and activate protein kinase C and is now recognized as a multi-functional scaffold protein (11,12). Evidence has indicated that RACK1 protects from oxidative stress-induced cell death in various types of cells, including fission yeasts (13), shrimp cells (14), neurons (15), HeLa cells (16) and HL60 cells (17). However, such a role for RACK1 has not been reported in HCC cells to the best of our knowledge. In the present study, it was demonstrated that RACK1 knockdown leads to increased cell death in TNF-α-treated HCC cells in the presence of cycloheximide (CHX), a protein synthesis inhibitor. Subsequently, it was observed that RACK1 knockdown promotes intracellular ROS accumulation upon TNF-α or H 2 O 2 stimulation. A combination of co-immunoprecipitation (co-IP) and mass spectrometry analysis indicated that carbonyl reductase 1 (CBR1), a ubiquitous nicotinamide adenine dinucleotide phosphate-dependent enzyme, acts as a RACK1-interacting partner in HCC cells. CBR1 has been reported to provide protection from ROS-induced cellular damage in HCC and leukemia (4,18), which suggests that CBR1 serves a role in c...

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Receptor for Activated C Kinase-1 protein from Penaeus monodon (Pm-RACK1) participates in the shrimp antioxidant response

Cited by 12 publications

References 39 publications

Expression profile of key immune-related genes in Penaeus monodon juveniles after oral administration of recombinant envelope protein VP28 of white spot syndrome virus

Expression profile of key immune-related genes in Penaeus monodon juveniles after oral administration of recombinant envelope protein VP28 of white spot syndrome virus

AealRACK1 expression and localization in response to stress in C6/36 HT mosquito cells

RACK1 promotes hepatocellular carcinoma cell survival via CBR1 by suppressing TNF-α-induced ROS generation

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