Expression of constructs of the neuronal isoform of myosin-Va interferes with the distribution of melanosomes and other vesicles in melanoma cells

2002 ◽  
Vol 51 (2) ◽  
pp. 57-75 ◽  
Author(s):  
Jo�o Carlos da Silva Bizario ◽  
Alexandra Aparecida da Cunha Nascimento ◽  
Luciana Casaletti ◽  
Eliana Val�ria Patussi ◽  
Maria Fernanda Chociay ◽  
...  
Keyword(s):  
Melanoma Cells ◽  
Myosin Va

scholarly journals A myosin-Va tail fragment sequesters dynein light chains leading to apoptosis in melanoma cells

2013 ◽  
Vol 4 (3) ◽  
pp. e547-e547 ◽  
Author(s):  
T C Izidoro-Toledo ◽  
A C Borges ◽  
D D Araújo ◽  
D P S Leitão Mazzi ◽  
F O Nascimento ◽  
...  
Keyword(s):  
Melanoma Cells ◽  
Light Chains ◽  
Myosin Va ◽  
Dynein Light Chains

scholarly journals Myosin-Va Contributes to Manifestation of Malignant-Related Properties in Melanoma Cells

2013 ◽  
Vol 133 (12) ◽  
pp. 2809-2812 ◽  
Author(s):  
Cleidson P. Alves ◽  
Milene H. Moraes ◽  
Josane F. Sousa ◽  
Carmen Lucia S. Pontes ◽  
Anelisa Ramão ◽  
...  
Keyword(s):  
Melanoma Cells ◽  
Myosin Va

Abstract 3167: Myosin-Va involvement in malignant properties of melanoma cells

2014 ◽  
Author(s):  
Anelisa Ramao ◽  
Carmen Lucia S. Pontes ◽  
Enilza M. Espreafico
Keyword(s):  
Melanoma Cells ◽  
Myosin Va

scholarly journals A novel role for Myosin-Va in mitochondrial fission

2019 ◽  
Author(s):  
Jackeline S Araujo ◽  
Rui M P Silva-Junior ◽  
Tong Zhang ◽  
Cara R Schiavon ◽  
Qian Chu ◽  
...  
Keyword(s):  
Molecular Motors ◽  
Molecular Motor ◽  
Mitochondrial Fission ◽  
Regulatory Protein ◽  
Melanoma Cells ◽  
Cellular Respiration ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Morphology ◽  
Myosin Va ◽  
The Warburg Effect

ABSTRACTIn cancer cells metabolic changes and mitochondrial morphology are coupled. It is known that the cytoskeleton and molecular motors are directly involved in regulating mitochondrial morphology. Here we show that myosin-Va, an actin-based molecular motor, is required for the malignant properties of melanoma cells and localizes to mitochondria in these cells. Knockdown of myosin-Va increases cellular respiration rates and ROS production and decreases glucose uptake and lactate secretion. In addition, knockdown of myosin-Va results in reduced mitochondrial fission and correspondingly elongated mitochondria. We show that myosin-Va interacts with the mitochondrial outer membrane protein Spire1C, an actin-regulatory protein implicated in mitochondrial fission, and that Spire1C recruits myosin-Va to mitochondria. Finally, we show that during mitochondrial fission myosin-Va localization to mitochondria increases, and that myosin-Va localizes to mitochondrial fission sites immediately adjacent to Drp1 punctae. We conclude that myosin-Va facilitates mitochondrial fission. These data implicate myosin-Va as a target for the Warburg effect in melanoma cells.

Sequential detection of mRNA for the chemokine IL-8 and macrophages (F4/80) in human melanoma

1995 ◽  
Vol 53 ◽  
pp. 1008-1009
Author(s):  
C.D. Bucana ◽  
R. Sanchez ◽  
R. Singh ◽  
I.J. Fidler
Keyword(s):  
Tumor Cells ◽  
Nude Mice ◽  
Constitutive Expression ◽  
Metastatic Potential ◽  
Melanoma Cells ◽  
Human Melanoma ◽  
Angiogenic Factor ◽  
Infiltrating Cells ◽  
Immunoperoxidase Assay ◽  
Multifunctional Cytokine

The purpose of this study was to demonstrate by ISH the presence of IL-8 mRNA, and by immunohistochemistry (IHC) the presence of the chemokine IL-8 and the distribution of infiltrating macrophages in subcutaneous melanomas in the same tumor. IL-8 is a multifunctional cytokine produced by melanoma cells, activated macrophages and monocytes and it has been shown to be a growth and angiogenic factor for tumor cells. More recently it was shown that constitutive expression of IL-8 correlated directly with metastatic potential of human melanoma cells in nude mice. IL-8 content of a solid tumor as determined by Western blot analysis does not take into account the contribution of macrophages. Previous studies showed that murine tumors contain many infiltrating cells interspersed among tumor cells whereas human tumors growing in nude mice exhibit macrophages at the periphery or between tumor islands. In this study we demonstrate the expression of IL-8 and the distribution of macrophages by immunoperoxidase assay and IL-8 mRNA by ISH.

Oleanolic acid rich solubilized triterpene extracts from mistletoe induce apoptotic and necrotic cell death of murine B16. F10 melanoma cells

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
CM Strüh ◽  
S Jäger ◽  
CM Schempp ◽  
T Jakob ◽  
A Scheffler ◽  
...  
Keyword(s):  
Cell Death ◽  
Oleanolic Acid ◽  
Melanoma Cells ◽  
Necrotic Cell Death ◽  
Necrotic Cell

Comparative gene expression study in WM164 melanoma cells treated with dimethylacrylshikonin.

2017 ◽  
Author(s):  
N Kretschmer ◽  
A Deutsch ◽  
B Rinner ◽  
M Scheideler ◽  
R Bauer
Keyword(s):  
Gene Expression ◽  
Melanoma Cells ◽  
Gene Expression Study ◽  
Expression Study

Ancylostoma caninum Anticoagulant Peptide Blocks Metastasis In Vivo and Inhibits Factor Xa Binding to Melanoma Cells In Vitro

1998 ◽  
Vol 79 (05) ◽  
pp. 1041-1047 ◽  
Author(s):  
Kathleen M. Donnelly ◽  
Michael E. Bromberg ◽  
Aaron Milstone ◽  
Jennifer Madison McNiff ◽  
Gordon Terwilliger ◽  
...  
Keyword(s):  
Active Site ◽  
Thrombin Generation ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Melanoma Cells ◽  
Factor V ◽  
Ancylostoma Caninum ◽  
Metastatic Activity

SummaryWe evaluated the in vivo anti-metastatic activity of recombinant Ancylostoma caninum Anticoagulant Peptide (rAcAP), a potent (Ki = 265 pM) and specific active site inhibitor of human coagulation factor Xa originally isolated from bloodfeeding hookworms. Subcutaneous injection of SCID mice with rAcAP (0.01-0.2 mg/mouse) prior to tail vein injection of LOX human melanoma cells resulted in a dose dependent reduction in pulmonary metastases. In order to elucidate potential mechanisms of rAcAP’s anti-metastatic activity, experiments were carried out to identify specific interactions between factor Xa and LOX. Binding of biotinylated factor Xa to LOX monolayers was both specific and saturable (Kd = 15 nM). Competition experiments using antibodies to previously identified factor Xa binding proteins, including factor V/Va, effector cell protease receptor-1, and tissue factor pathway inhibitor failed to implicate any of these molecules as significant binding sites for Factor Xa. Functional prothrombinase activity was also supported by LOX, with a half maximal rate of thrombin generation detected at a factor Xa concentration of 2.4 nM. Additional competition experiments using an excess of either rAcAP or active site blocked factor Xa (EGR-Xa) revealed that most of the total factor Xa binding to LOX is mediated via interaction with the enzyme’s active site, predicting that the vast majority of cell-associated factor Xa does not participate directly in thrombin generation. In addition to establishing two distinct mechanisms of factor Xa binding to melanoma, these data raise the possibility that rAcAP’s antimetastatic effect in vivo might involve novel non-coagulant pathways, perhaps via inhibition of active-site mediated interactions between factor Xa and tumor cells.

Re-expression of Dipeptidylpeptidase 4 (DPP4) in melanoma cells – insights into molecular consequences

2004 ◽  
Vol 30 (08/09) ◽  
Author(s):  
B Becker ◽  
A Roesch ◽  
C Hafner ◽  
W Stolz ◽  
M Landthaler ◽  
...  
Keyword(s):  
Melanoma Cells ◽  
Dipeptidylpeptidase 4
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