Comparative Proteomic Analysis of Matched Primary and Metastatic Melanoma Cell Lines

2008 ◽  
Vol 7 (9) ◽  
pp. 4107-4118 ◽  
Author(s):  
Mohammad Al-Ghoul ◽  
Thomas B. Brück ◽  
Janelle L. Lauer-Fields ◽  
Victor S. Asirvatham ◽  
Claudia Zapata ◽  
...  
Keyword(s):  
Metastatic Melanoma ◽  
Cell Lines ◽  
Melanoma Cell ◽  
Proteomic Analysis ◽  
Metastatic Melanoma Cell ◽  
Comparative Proteomic Analysis ◽  
Melanoma Cell Lines

PAX3 knockdown in metastatic melanoma cell lines does not reduce MITF expression

2011 ◽  
Vol 21 (1) ◽  
pp. 24-34 ◽  
Author(s):  
Shujie He ◽  
Caiyun G. Li ◽  
Lynn Slobbe ◽  
Amy Glover ◽  
Elaine Marshall ◽  
...  
Keyword(s):  
Metastatic Melanoma ◽  
Cell Lines ◽  
Melanoma Cell ◽  
Metastatic Melanoma Cell ◽  
Mitf Expression ◽  
Melanoma Cell Lines

Inhibition of glucose metabolism through treatment of BRAF mutated metastatic melanoma with vemurafenib.

2019 ◽  
Vol 37 (15_suppl) ◽  
pp. e21005-e21005 ◽  
Author(s):  
Govind Warrier ◽  
Lilibeth Lanceta ◽  
Yoannis Imbert-Fernandez ◽  
Jason Alan Chesney
Keyword(s):  
Glucose Metabolism ◽  
Protein Expression ◽  
Metastatic Melanoma ◽  
Cell Lines ◽  
Melanoma Cell ◽  
Control Point ◽  
Braf Inhibitor ◽  
Growth And Survival ◽  
Metastatic Melanoma Cell ◽  
Melanoma Cell Lines

e21005 Background: Increased glucose metabolism is a hallmark of neoplastic cells that allows self-promotion of growth and survival. The enzyme 6-phosphofructo-2-kinase (PFKFB3) is an integral controller of glycolysis by promoting the synthesis of fructose 2,6-bisphosphonate (F2,6BP) which activates 6-phoshofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in the glycolytic pathway. Additionally, mitogen-activated protein kinase (MAPK) is a key signaling pathway in a number of cancers with mutations of the BRAF component, described most commonly in melanoma, resulting in constitutive activation of the MAPK pathway. We aim to demonstrate that vemurafenib, a BRAF inhibitor, has antiglycolytic activity in sensitive melanoma cell lines which may help guide development of future therapies with specific attention to PFKFB3 as a potential enzymatic target to decrease glycolytic flux thereby inhibiting tumor growth and survival. Methods: Vemurafenib sensitive and resistant variants of two separate human metastatic melanoma cell lines (451Lu and WM983) were treated with 3 mM Vemurafenib for 24 and 48 hours. Additionally, cells from aforementioned lines were probed for PFKFB3 after 24 hours of treatment with vemurafenib. Glycolysis was measured by incubating cells in complete media containing 1 mCi [5-3H]glucose for 60 minutes. [3H]H2O produced by glycolysis through enolase was measured. Results: A decrease in PFKFB3 protein expression was found in vemurafenib sensitive cells compared to controls but not in resistant cells after 24h treatment with 3 mM vemurafenib in both 451Lu and WM983 metastatic melanoma cell lines (n = 2). Treatment with vemurafenib led to decrease in glycolysis compared to untreated controls in both vemurafenib sensitive metastatic melanoma cell lines but not in resistant cell lines (n = 5). Additionally, there was a significant reduction in glycolysis in vemurafenib resistant WM983 at 48 hours compared to resistant untreated control. Conclusions: BRAF mutated metastatic melanoma cells showed decrease in PFKFB3 protein expression and decreased glycolysis after treatment with BRAF inhibitor vemurafenib. Future studies will focus on assessing metastatic melanoma cell viability and glycolytic activity after treatment with combination BRAF inhibition and PFKFB3 specific inhibition.

scholarly journals Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential

2021 ◽  
Author(s):  
Martina Paumann-Page ◽  
Nikolaus Ferdinand Kienzl ◽  
Jyoti Motwani ◽  
Boushra Boushra Bathish ◽  
Louise N Paton ◽  
...  
Keyword(s):  
Metastatic Melanoma ◽  
Cell Lines ◽  
Melanoma Cell ◽  
Collagen Iv ◽  
Metastatic Melanoma Cell ◽  
Protein Levels ◽  
Non Invasive ◽  
Hypobromous Acid ◽  
Invasive Cell ◽  
Melanoma Cell Lines

Peroxidasin, a heme peroxidase, has been shown to play a role in cancer progression. mRNA expression has been reported to be upregulated in metastatic melanoma cell lines and connected to the invasive phenotype, but little is known about how peroxidasin acts in cancer cells. We have analyzed peroxidasin protein expression and activity in eight metastatic melanoma cell lines using an ELISA developed with an in-house peroxidasin binding protein. RNAseq data analysis confirmed high peroxidasin mRNA expression in the five cell lines classified as invasive and low expression in the three non-invasive cell lines. Protein levels of peroxidasin were higher in the cell lines with an invasive phenotype. Active peroxidasin was secreted to the cell culture medium, where it accumulated over time, and peroxidasin protein levels in the medium were also much higher in invasive than non-invasive cell lines. The only well-established physiological role of peroxidasin is in the formation of a sulfilimine bond, which cross-links collagen IV in basement membranes via catalyzed oxidation of bromide to hypobromous acid. We found that peroxidasin secreted from melanoma cells formed sulfilimine bonds in uncross-linked collagen IV, confirming peroxidasin activity and hypobromous acid formation. Moreover, 3-bromotyrosine, a stable product of hypobromous acid reacting with tyrosine residues, was detected in invasive melanoma cells, substantiating that their expression of peroxidasin generates hypobromous acid, and showing that it does not exclusively react with collagen IV, but also with other biomolecules.

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