Comprehensive identification of proteins in Hodgkin lymphoma-derived Reed–Sternberg cells by LC-MS/MS

Wallentine, Jeremy C.; Kim, Ki Kwon; Seiler, Charles E.; Vaughn, Cecily P.; Crockett, David K.; Tripp, Sheryl R.; Elenitoba-Johnson, Kojo S.J.; Lim, Megan S.

doi:10.1038/labinvest.3700672

Cited by 22 publications

(19 citation statements)

References 44 publications

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“…PANC-1 cells were maintained in Dulbecco’s modified Eagle’s medium (D-MEM) supplemented with 10% fetal calf serum (FCS), 2 mM glutamine, 100 U/ml penicillin and 100 mg/ml streptomycin. For secretome preparation, cells were cultured at 1.5×10 6 cell/ml in D-MEM until of 70–80% confluence (4). …”

Section: Methodsmentioning

confidence: 99%

Characterization of proteins secreted by pancreatic cancer cells with anticancer drug treatment in vitro

et al. 2012

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Pancreatic cancer is one of the most lethal cancers, with an incidence equaling mortality. It is a heterogeneous group of neoplasms in which pancreatic ductal adenocarcinoma is most common. Pancreatic cancer cannot be cured even if detected early. When treatment is initiated, a suitable method of administration of anticancer drugs must be chosen. Anticancer drugs kill tumor cells. However, side effects including initiation are problematic in anticancer drug therapy. Improved methods for the diagnosis of side effects of pancreatic cancer by using sensitive and specific tumor markers are highly desirable. Therefore, efficient strategies for biomarker discovery are urgently needed. Here, we present an approach based on direct experimental access to proteins released by PANC-1 human pancreatic cancer cells in vitro. A two-dimensional (2-D) map and catalog of this subproteome, herein termed the secretome, were established comprising more than 1,000 proteins observed by ‘2-D difference in-gel electrophoresis analysis using cyanine dye’. We investigated 22 spots that were 1.20-fold upregulated and 31 spots that were 0.66-fold downregulated by gemcitabine chloride treatment. Proteins in these spots were identified by nano-high-performance liquid chromatography electrospray ionization time of flight mass spectrometry/mass spectrometry. Most secretome constituents were nominally cellular proteins. By mass spectrometry screening, 14-3-3 protein sigma (14-3-3 σ), protein S100-A8, protein S100-A9, galectin-7, lactotransferrin (lactoferrin, LF) precursor, serotransferrin (transferrin) precursor, and vitamin D binding protein precursor were identified. Western blotting confirmed the presence of 14-3-3 σ and LF. We found that upregulation of 14-3-3 σ was associated with apoptosis, and downregulation of LF was found to suppress tumorigenesis.

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Section: Methodsmentioning

confidence: 99%

Characterization of proteins secreted by pancreatic cancer cells with anticancer drug treatment in vitro

et al. 2012

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“…The induction of lymphomas in PIM-containing mice is markedly enhanced by treatment of these animals with chemical carcinogens (9) or γ-irradiation (10). The PIM protein kinases are over-expressed in many human cancers, including prostate cancer (11, 12), lymphoma (13, 14), leukemia (15), head and neck squamous cell carcinomas (16, 17), and pancreatic and colon cancers (18, 19). In human prostate, expression of PIM1 is low in benign prostatic hypertrophy, moderate in high grant intraepithelial neoplasia, and increased in frank cancer (11, 20).…”

Section: Introductionmentioning

confidence: 99%

p53-Dependent Induction of Prostate Cancer Cell Senescence by the PIM1 Protein Kinase

Zemskova

Lilly

Lin

et al. 2010

Molecular Cancer Research

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The PIM family of serine threonine protein kinases plays an important role in regulating both the growth and transformation of malignant cells. However, in a cell line–dependent manner, overexpression of PIM1 can inhibit cell and tumor growth. In 22Rv1 human prostate cells, but not in Du145 or RWPE-2, PIM1 over-expression was associated with marked increases in cellular senescence, as shown by changes in the levels of β-galactosidase (SA-β-Gal), p21, interleukin (IL)-6 and IL-8 mRNA and protein. During early cell passages, PIM1 induced cellular polyploidy. As the passage number increased, markers of DNA damage, including the level of γH2AX and CHK2 phosphorylation, were seen. Coincident with these DNA damage markers, the level of p53 protein and genes transcriptionally activated by p53, such as p21, TP53INP1, and DDIT4, increased. In these 22Rv1 cells, the induction of p53 protein was associated not only with senescence but also with a significant level of apoptosis. The importance of the p53 pathway to PIM1-driven cellular senescence was further shown by the observation that expression of dominant-negative p53 or shRNA targeting p21 blocked the PIM1-induced changes in the DNA damage response and increases in SA-β-Gal activity. Likewise, in a subcutaneous tumor model, PIM1-induced senescence was rescued when the p53-p21 pathways are inactivated. Based on these results, PIM1 will have its most profound effects on tumorigenesis in situations where the senescence response is inactivated.

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“…6 Therefore, proteomics-based approaches have recently been used in HL to identify protein patterns that may provide pathogenetic and prognostic clues. 7,8 However, these studies were only performed in cell lines and still await confirmation in an in vivo setting.…”

Section: Introductionmentioning

confidence: 99%

Proteomic analysis identifies galectin-1 as a predictive biomarker for relapsed/refractory disease in classical Hodgkin lymphoma

Kamper

Ludvigsen

Bendix

et al. 2011

Blood

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Considerable effort has been spent identifying prognostic biomarkers in classic Hodgkin lymphoma (cHL). The aim of our study was to search for possible prognostic parameters in advanced-stage cHL using a proteomics-based strategy. A total of 14 cHL pretreatment tissue samples from younger, advanced-stage patients were included. Patients were grouped according to treatment response. Proteins that were differentially expressed between the groups were analyzed using 2D-PAGE and identified by liquid chromatography mass spectrometry. Selected proteins were validated using Western blot analysis. One of the differentially expressed proteins, the carbohydrate-binding protein galectin-1 (Gal-1), was further analyzed using immunohistochemistry HC and its expression was correlated with clinicopathologic and outcome parameters in 143 advanced-stage cHL cases. At the univariate level, high Gal-1 expression in the tumor microenvironment was correlated with poor event-free survival (P ‫؍‬ .02). Among younger (< 61 years) patients, high Gal-1 was correlated with poorer overall and event-free survival (both P ‫؍‬ .007). In this patient group and at the multivariate level, high Gal-1 expression retained a significant predictive impact on event-free survival. Therefore, in addition to its functional role in cHL-induced immunosuppression, Gal-1 is also associated with an adverse clinical outcome in this disease. (Blood. 2011;117(24):6638-6649)

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Comprehensive identification of proteins in Hodgkin lymphoma-derived Reed–Sternberg cells by LC-MS/MS

Cited by 22 publications

References 44 publications

Characterization of proteins secreted by pancreatic cancer cells with anticancer drug treatment in vitro

Characterization of proteins secreted by pancreatic cancer cells with anticancer drug treatment in vitro

p53-Dependent Induction of Prostate Cancer Cell Senescence by the PIM1 Protein Kinase

Proteomic analysis identifies galectin-1 as a predictive biomarker for relapsed/refractory disease in classical Hodgkin lymphoma

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