Proteomic analysis of lung biopsies: Differential protein expression profile between peritumoral and tumoral tissue

Alfonso, Patricia; Catalá, Myriam; Rico-Morales, María Luisa; Durante‐Rodríguez, Gonzalo; Moro-Rodríguez, Ernesto; Fernández-García, Héctor; Escribano, José M.; Álvarez-Fernández, Emilio; García-Poblete, Eduardo

doi:10.1002/pmic.200300647

Cited by 32 publications

(21 citation statements)

References 23 publications

(15 reference statements)

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“…At the protein level, consistent with mRNA expression, MG132 , Immenschuh et al 2002, Wijayanti et al 2008, indicating the expression of PRDX1 is inducible by various stimuli. PRDX1 expression is also elevated in most cancers, although the physiological mechanism is still unclear (Yanagawa et al 1999, Chang et al 2001, Kim et al 2003, Alfonso et al 2004, Lehtonen et al 2004, Xin et al 2005. Previous studies have reported that an increased level of PRDX1 might be involved in the protection of cancer cells against various therapeutic challenges ( Butzke et al 2004, Song et al 2009).…”

Section: Discussionmentioning

confidence: 99%

“…Analysis of cells and mice lacking PRDX1 suggest that it not only regulates H 2 O 2 levels, but also possesses the properties of a tumor suppressor (Neumann et al 2003), which was further supported by the finding that PRDX1 interacts with c-Myc, thereby selectively inhibiting c-Myc transcriptional activity (Egler et al 2005). However, many studies indicated that aberrant increased expression of PRDX1 is found in various kinds of cancers including thyroid, lung, and breast (Yanagawa et al 1999, Chang et al 2001, Kim et al 2003, Alfonso et al 2004, Lehtonen et al 2004, Xin et al 2005, which obscures its actual role in tumorigenesis. As the hypoxic and unstable oxygenation microenvironment of a tumor is one of the key factors influencing tumor growth and progression, this increase in PRDX1 expression might be an adaptive response.…”

Section: Introductionmentioning

confidence: 96%

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Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Du¹,

Yan²,

Zhang³

et al. 2010

Endocrine-Related Cancer

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Proteasome inhibitors represent a novel class of antitumor agents with pre-clinical and clinical evidence of activity against hematologic malignancies and solid tumors. However, emerging evidence indicates that antiapoptotic factors may also accumulate as a consequence of exposure to these drugs, thus it seems plausible that the activation of survival signaling cascades might compromise their antitumoral effects. Peroxiredoxins (PRDXs) are a family of thiol-containing peroxidases identified primarily by their ability to remove cellular hydroperoxides. The function of PRDX1 in particular has been implicated in regulating cell proliferation, differentiation, and apoptosis. Another important finding is that aberrant upregulation of PRDX1 has been discovered in various cancers. Apoptosis signal-regulating kinase 1 (ASK1) is a mitogen-activated protein kinase (MAPK) kinase kinase that is regulated under conditions of cellular stress. ASK1 phosphorylates c-Jun N-terminal kinase and p38 MAPK, and elicits an apoptotic response. ASK1 activity is regulated at multiple levels, one of which is through interaction with PRDX1. In this study, for the first time we report that upregulation of PRDX1 expression was found in thyroid cancer cells treated with proteasome inhibitors, and PRDX1 knockdown resulted in accelerated proteasome inhibitor-induced cell death. In addition, we demonstrated that ASK1 activity was implicated in the PRDX1-dependent response of thyroid cancer cells to proteasome inhibitormediated cell death.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Du¹,

Yan²,

Zhang³

et al. 2010

Endocrine-Related Cancer

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“…The disulfide bond is reduced back to the active thiol form (Cys-SH) by various mechanisms (2)(3)(4). We and others previously reported that Prx1 is frequently elevated in human lung cancer cells and tissues (5)(6)(7)(8)(9). Based on the observations in cultured cells and animals, a survival enhancing function of Prx1 has been proposed.…”

Section: Introductionmentioning

confidence: 99%

Prx1 Suppresses Radiation-Induced c-Jun NH2-Terminal Kinase Signaling in Lung Cancer Cells through Interaction with the Glutathione S-Transferase Pi/c-Jun NH2-Terminal Kinase Complex

Kim¹,

Lee²,

et al. 2006

Cancer Research

127

119

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Radiotherapy is one of the major treatment modalities for lung cancer. Cell killing by ionizing radiation is mediated primarily through the reactive oxygen species (ROS) and ROSdriven oxidative stress. Prx1, a peroxiredoxin family member, was shown to be frequently elevated in lung cancer cells and tissues. Although the antioxidant function of Prx1 is expected to affect the radiotherapy response of lung cancer, the physiologic significance of its peroxidase activity in irradiated cells is unclear because the catalytic Cys 52 is easily inactivated by ROS due to its overoxidation to sulfinic or sulfonic acid. In this study, we investigated the role of Prx1 in radiation sensitivity of human lung cancer cells, with special emphasis on the redox status of the catalytic Cys 52 . We found that overexpression of Prx1 enhances the clonogenic survival of irradiated cells and suppresses ionizing radiation-induced c-Jun NH 2 -terminal kinase (JNK) activation and apoptosis. The peroxidase activity of Prx1, however, is not essential for inhibiting JNK activation. The latter effect is mediated through its association with the glutathione S-transferase pi (GSTpi)-JNK complex, thereby preventing JNK release from the complex. Reduced JNK activation is observed when the peroxidase activity of Prx1 is compromised by Cys 52 overoxidation or in the presence of the Cys 52 to Ser 52 mutant (Prx1C52S) lacking peroxidase activity. We show that both Prx1 and Prx1C52S interact with the GSTpi-JNK complex and suppress the release of JNK from the complex. Our study provides new insight into the antiapoptotic function of Prx1 in modulating radiosensitivity and provides the impetus to monitor the influence of Prx1 levels in the management of lung cancer. (Cancer Res 2006; 66(14): 7136-42)

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“…Proteomic analysis, therefore, can play an important, non-redundant role in the identification and characterization of potential biomarkers and targets of cancer intervention. 19 Several studies have used advanced proteomics methods and statistical analyses to attempt to distinguish normal and cancer specimens for lung, 20 ovarian, 21 and breast cancer. 22 Based on our transcriptome results, we framed a similar hypothesis: nonmalignant proliferating B cells and malignant proliferating B cells will share the induction of important proliferation-associated proteins in comparison with non-proliferating controls; however, malignant cells will show additional changes in protein expression, including posttranslational modification, that are unique to their malignant state, over and above those changes associated with normal, mitogen-stimulated proliferation alone.…”

mentioning

confidence: 99%

Development of a Malignancy-Associated Proteomic Signature for Diffuse Large B-Cell Lymphoma

Romesser

Perlman

Faller

et al. 2009

The American Journal of Pathology

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The extreme pathological diversity of non-Hodgkin's lymphomas has made their accurate histological assessment difficult. New diagnostics and treatment modalities are urgently needed for these lymphomas, particularly in drug development for cancer-specific targets. Previously, we showed that a subset of B cell lymphoma, diffuse large B cell lymphoma, may be characterized by two major, orthogonal axes of gene expression: one set of transcripts that is differentially expressed between resting and proliferating, nonmalignant cells (ie, a "proliferative signature") and another set that is expressed only in proliferating malignant cells (ie, a "cancer signature"). A differential proteomic analysis of B cell proliferative states, similar to previous transcriptional profiling analyses, holds great promise either to reveal novel factors that participate in lymphomagenesis or to define biomarkers of onset or progression. Here, we use a murine model of diffuse large B cell lymphoma to conduct unbiased two-dimensional gel electrophoresis and mass spectrometry-based comparative proteomic analyses of malignant proliferating B cells and tissue-matched, normal resting, or normal proliferating cells. We show that the expression patterns of particular proteins or isoforms across these states fall into eight specific trends that provide a framework to identify malignancy-associated biomarkers and potential drug targets , a signature proteome. Our results support the central hypothesis that clusters of proteins of known function represent a panel of expression markers uniquely associated with malignancy and not normal proliferation.

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Proteomic analysis of lung biopsies: Differential protein expression profile between peritumoral and tumoral tissue

Cited by 32 publications

References 23 publications

Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Prx1 Suppresses Radiation-Induced c-Jun NH2-Terminal Kinase Signaling in Lung Cancer Cells through Interaction with the Glutathione S-Transferase Pi/c-Jun NH2-Terminal Kinase Complex

Development of a Malignancy-Associated Proteomic Signature for Diffuse Large B-Cell Lymphoma

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