Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinoma

Veremieva, M. V.; Хоруженко, А. И.; Zaicev, Sergej; Negrutskii, B. S.; El’skaya, A. V.

doi:10.1111/j.1365-2362.2010.02404.x

Cited by 27 publications

(32 citation statements)

References 37 publications

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“…The cancer-related role of the Bα subunit is poorly documented. Recent data indicate that the individual subunits can exist separately from the EF-1B complex in cancer tissues and that disintegration of EF-1B could be an important sign of cancer development (Veremieva et al 2011).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of NME1/NDPK A null mouse liver: evidence for a post-translational regulation of annexin IV and EF-1Bα

Bruneel

Wendum

Labas

et al. 2011

Naunyn-Schmiedeberg's Arch Pharmacol

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NME/NDPK family proteins are involved in the control of intracellular nucleotide homeostasis as well as in both physiological and pathological cellular processes, such as proliferation, differentiation, development, apoptosis, and metastasis dissemination, through mechanisms still largely unknown. One family member, NME1/NDPK-A, is a metastasis suppressor, yet the primary physiological functions of this protein are still missing. The purpose of this study was to identify new NME1/NDPK-A-dependent biological functions and pathways regulated by this gene in the liver. We analyzed the proteomes of wild-type and transgenic NME1-null mouse livers by combining two-dimensional gel electrophoresis and mass spectrometry (matrix-assisted laser desorption/ionization time of flight and liquid chromatography-tandem mass spectrometry). We found that the levels of three proteins, namely, phenylalanine hydroxylase, annexin IV, and elongation factor 1 Bα (EF-1Bα), were strongly reduced in the cytosolic fraction of NME1(-/-) mouse livers when compared to the wild type. This was confirmed by immunoblotting analysis. No concomitant reduction in the corresponding messenger RNAs or of total protein level was observed, however, suggesting that NME1 controls annexin IV and EF-1Bα amounts by post-translational mechanisms. NME1 deletion induced a change in the subcellular location of annexin IV in hepatocytes resulting in enrichment of this protein at the plasma membrane. We also observed a redistribution of EF-1Bα in NME1(-/-) hepatocytes to an intracytoplasmic compartment that colocalized with a marker of the reticulum endoplasmic. Finally, we found reduced expression of annexin IV coincident with decreased NME1 expression in a panel of different carcinoma cell lines. Taken together, our data suggest for the first time that NME1 might regulate the subcellular trafficking of annexin IV and EF-1Bα. The potential role of these proteins in metastatic dissemination is discussed.

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Section: Discussionmentioning

confidence: 99%

Proteomic analysis of NME1/NDPK A null mouse liver: evidence for a post-translational regulation of annexin IV and EF-1Bα

Bruneel

Wendum

Labas

et al. 2011

Naunyn-Schmiedeberg's Arch Pharmacol

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“…Immunohistochemical study of tissue samples was carried out according to the protocol described previously [28]; the mandatory control staining of tissue sections was performed via using only secondary antibodies («Control»). Working dilution of the anti-peptide antibody preparation against eEF1A2 is specified in the figure legends.…”

Section: Methodsmentioning

confidence: 99%

“…Immunoblotting of proteins was performed as described in [28]. The secondary antibodies (1:5000 dilution) against goat IgGs conjugated to horseradish peroxidase («Imtek», Russian Federation) were used for detection of primary anti-peptide antibodies.…”

Section: Methodsmentioning

confidence: 99%

Characterization of novel peptide-specific antibodies against the translation elongation factor eEF1A2 and their application for cancer research

et al. 2014

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Aim.We intend to characterize the new peptide-specific antibodies against the isoform 2 of translation elongation factor 1A (eEF1A2) and determine its presence in the postoperative samples of human breast, lung and stomach tumor tissues. Methods. The analysis of antibody specificity was performed by enzyme-linked immunosorbent assay, immunoblotting and immunohistochemistry. Immunoblotting and immunohistochemistry were used for the determination of the eEF1A2 in the human tumor samples, as well as in the samples of normal tissues surrounding tumors. Results. The antibodies obtained against the eEF1A2 specifically recognized this protein in the cell extracts and histological sections and did not cross-react with the elongation factor 1A isoform 1. eEF1A2 was revealed in the postoperative samples of breast, lung and stomach tumors as well as in the putative normal tissues surrounding tumors. Conclusions. The antibodies obtained against eEF1A2 are highly specific for the antigen and can be used for the immunological studies of tumors.

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“…However, the existence of free eEF1Bγ was detected in human cancer tissues. Moreover, cancer cells showed a sign of nuclear localization of eEF1Bγ [7,8]. As there is a general belief that protein synthesis occurs exclusively in cytoplasm [9], the cyto-nucleo transfer of eEF1Bγ implies some non-translational role of the subunit.…”

Section: Introductionmentioning

confidence: 99%

Analysis of eEF1Bγ interactome in the nuclear fraction of A549 human lung adenocarcinoma cells

et al. 2019

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Aim.To study the translation elongation factor eEF1B gamma (eEF1Bγ) in the nucleus of lung carcinoma cells. Methods. The protein partners of eEF1Bγin the nuclear fraction of A549 cells were identified by co-immunoprecipitation (co-IP) and liquid chromatography-tandem mass spectrometry (LC-MS/MS). The protein interaction network for nuclear eEF1Bγ was determined by Cytoscape 3.2.0 program using the MCODE plugin. Additional analysis of the eEF1Bγ partners was conducted by Map of the cell database. Results. 234 proteins interacting with eEF1Bγ in the nuclear fraction of A549 cells were identified. Possible functional networks involving these contacts were analyzed by two bioinformatic approaches. Conclusions. Splicing of pre-mRNA and regulation of mRNA stability are assumed to be the main processes in which nuclear eEF1Bγ can be involved. We hypothesize that a portion of eEF1Bγ leaves the cytoplasmlocalizede EF1B complex during carcinogenesis and enters the nucleus to regulate certain mRNAs by affecting the splicing of their pre-mRNA and/or stability of mRNA. K e y w o r d s: eEF1Bγ, protein-protein interactions, nucleus, A549 cell Structure and Function of Biopolymers

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Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinoma

Cited by 27 publications

References 37 publications

Proteomic analysis of NME1/NDPK A null mouse liver: evidence for a post-translational regulation of annexin IV and EF-1Bα

Proteomic analysis of NME1/NDPK A null mouse liver: evidence for a post-translational regulation of annexin IV and EF-1Bα

Characterization of novel peptide-specific antibodies against the translation elongation factor eEF1A2 and their application for cancer research

Analysis of eEF1Bγ interactome in the nuclear fraction of A549 human lung adenocarcinoma cells

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Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinoma

Cited by 27 publications

References 37 publications

Proteomic analysis of NME1/NDPK A null mouse liver: evidence for a post-translational regulation of annexin IV and EF-1Bα

Proteomic analysis of NME1/NDPK A null mouse liver: evidence for a post-translational regulation of annexin IV and EF-1Bα

Characterization of novel peptide-specific antibodies against the translation elongation factor eEF1A2 and their application for cancer research

Analysis of eEF1B&gamma; interactome in the nuclear fraction of A549 human lung adenocarcinoma cells

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Analysis of eEF1Bγ interactome in the nuclear fraction of A549 human lung adenocarcinoma cells