Platelet Interaction with Tumor Cells

1975 ◽  
Author(s):  
G. Gasic ◽  
T. Gasic ◽  
B. Hsu ◽  
P. Koch ◽  
S. Niewiarowski
Keyword(s):  
Tumor Cells ◽  
Gamma Globulin ◽  
Wilms Tumor ◽  
Preliminary Evidence ◽  
Human Tumors ◽  
Research Support ◽  
Mouse Tumors ◽  
Adp Release ◽  
Colonic Adenocarcinomas ◽  
Mammary Adenocarcinomas

Previous investigations demonstrated that mouse tumors cause platelet aggregation (PA) and increase platelet turnover. Depletion of platelets by neuraminidase and inhibition of PA by aspirin reduced the munber of metastases (Gasic et al., Int. J. Cancer 11, 704, 1973). The purpose of this investigation was to study further interaction of cells from various mouse and human tumors with platelets. Cells of 7 mouse tumors (1 mammary adenocarcinomas, 5 sarcomas, I melanoma) and 14 human tumors (8 breast, 3 colonic adenocarcinomas, 1 cancer of the ureter, 1 Wilms tumor, and 1 neuroblastoma) aggregated homologous platelets suspended in heparinized plasma. Three mouse tumors (2 mammary and 1 sarcoma) and 5 human tumors (2 breast, 1 sarcoma, 1 Wilms, and 1 neuroblastoma) did not. PA was accompanied by the release of radio-activity from 14C-serotonin labeled platelets (range 15–90%). PA activity was not correlated with fibrinolytic or procoagulant activity. The contribution of plasminogen activators, thrombin, and tumor immune complexes has been excluded. However, gamma globulin of tumor bearing mice contained a “blocking factor” which delayed PA. Since enzymatic removal of ADP reduced PA it is possible that the ADP release either by tumors or by platelets played a contributory role. The pattern of PA by tumor cells rossembled that induced by collagen. Indeed preliminary evidence suggests that collagen-like material associated with tumor cells might be involved in platelet adherence to these cells and subsequent aggregation.(Supported by NIH Grants CA-15728, HL 14217. HL 15226, and by a Univ. of Penna.’s General Research Support Grant.)

566: Comparative Genomic Hybridization of Chemotherapy Survived Wilms' Tumor Cells

2004 ◽  
Vol 171 (4S) ◽  
pp. 150-151
Author(s):  
Thorsten Schlomm ◽  
Bastian Gunawan ◽  
Hans J. Schulten ◽  
Norbert Graf ◽  
Ivo Leuschner ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Comparative Genomic Hybridization ◽  
Wilms Tumor ◽  
Comparative Genomic ◽  
Genomic Hybridization

scholarly journals TAMI-23. NEUTROPHIL-TRIGGERED FERROPTOSIS PROMOTES TUMOR NECROSIS IN GLIOBLASTOMA PROGRESSION

2020 ◽  
Vol 22 (Supplement_2) ◽  
pp. ii218-ii218
Author(s):  
Patricia Yee ◽  
Yiju Wei ◽  
Soo Yeon Kim ◽  
Tong Lu ◽  
Cynthia Lawson ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Tumor Necrosis ◽  
Treatment Resistance ◽  
Binding Motif ◽  
Lipid Hydroperoxides ◽  
Orthotopic Mouse Model ◽  
Mouse Tumors ◽  
Downstream Effector ◽  
Human Gbm ◽  
Early Tumor

Abstract Tumor necrosis indicates poor prognoses in many cancers, including glioblastomas (GBMs). Although thought to result from chronic ischemia, the underlying nature and mechanisms driving the involved cell death remain obscured by lack of animal models recapitulating the extent of necrosis in human GBMs. The molecular and clinical heterogeneity of GBMs adds further complexity. Not all GBMs contain necrosis. Mesenchymal (MES)-GBM, the subtype correlated with worst prognosis and highest treatment resistance, is most closely associated with necrosis. MES-GBM exhibits hyperactivity of transcriptional coactivator with PDZ-binding motif (TAZ), a Hippo tumor suppressive pathway effector whose expression in human GBMs predicts short survival. To elucidate mechanisms driving GBM necrosis, we devised a novel orthotopic mouse model recapitulating human MES-GBM phenotypically and histopathologically by expressing a constitutively-active TAZ mutant (TAZ4SA) in three human GBM cell lines (LN229, U87, and LN18) lacking MES signatures (GBM4SA). GBM4SA mice lived significantly shorter than mice implanted with GBMvector or mutant TAZ unable to bind its downstream effector, TEAD (GBM4SA-S51A). Extensive (≥30% of tumor volume) necrosis was present in GBM4SA mice but not GBMvector or GBM4SA-S51A. In GBM4SA tumors, neutrophils coincide with necrosis temporally and spatially. Neutrophil depletion dampens necrosis. Neutrophils isolated from mouse tumors killed co-cultured tumor cells. Neutrophils induce iron-dependent accumulation of lipid hydroperoxides within tumor cells by transferring myeloperoxidase-containing granules into tumor cells. Inhibiting myeloperoxidase suppresses neutrophil-induced tumor cytotoxicity. Intratumoral glutathione peroxidase 4 (GPX4) overexpression or acyl-CoA synthetase 4 (ACSL4) depletion diminishes necrosis and aggressiveness of tumors. Human GBM analysis indicates neutrophils and ferroptosis are associated with necrosis and predict poor survival. Together, we propose that certain tumor damage(s) during early tumor progression (i.e. ischemia) recruits neutrophils to damaged tissue and results in a positive feedback loop, amplifying GBM necrosis development. We show GBM necrosis involves neutrophil-triggered ferroptosis and reveal an unprecedented pro-tumorigenic role of ferroptosis.

scholarly journals Loss of allelic heterozygosity at a second locus on chromosome 11 in sporadic Wilms' tumor cells.

1989 ◽  
Vol 9 (4) ◽  
pp. 1799-1803 ◽  
Author(s):  
A E Reeve ◽  
S A Sih ◽  
A M Raizis ◽  
A P Feinberg
Keyword(s):  
Mental Retardation ◽  
Tumor Cells ◽  
Germ Line ◽  
Wilms Tumor ◽  
Globin Gene ◽  
Allelic Loss ◽  
Chromosomal Band ◽  
Chromosome 11 ◽  
Gamma Globin ◽  
Wagr Syndrome

Children with associated Wilms' tumor, aniridia, genitourinary malformations, and mental retardation (WAGR syndrome) frequently have a cytogenetically visible germ line deletion of chromosomal band 11p13. In accordance with the Knudson hypothesis of two-hit carcinogenesis, the absence of this chromosomal band suggests that loss of both alleles of a gene at 11p13 causes Wilms' tumor. Consistent with this model, chromosomes from sporadically occurring Wilms' tumor cells frequently show loss of allelic heterozygosity at polymorphic 11p15 loci, and therefore it has been assumed that allelic loss extends proximally to include 11p13. We report here that in samples from five sporadic Wilms' tumors, allelic loss occurred distal to the WAGR locus on 11p13. In cells from one tumor, mitotic recombination occurred distal to the gamma-globin gene on 11p15.5. Thus, allelic loss in sporadic Wilms' tumor cells may involve a second locus on 11p.

KDM6B Inhibition Has Anti-Tumor Activity in Anaplastic Wilms Tumor Cells Associated with WT1 And MYCN Pathway Silencing

2021 ◽  
Author(s):  
Hyea Jin Gil ◽  
Emilia M. Pinto ◽  
Andrew M. Davidoff ◽  
Gerard P. Zambetti ◽  
Jun Yang ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Wilms Tumor ◽  
Anti Tumor Activity

scholarly journals Focal Adhesion Kinase Suppresses Apoptosis by Binding to the Death Domain of Receptor-Interacting Protein

2004 ◽  
Vol 24 (10) ◽  
pp. 4361-4371 ◽  
Author(s):  
Elena Kurenova ◽  
Li-Hui Xu ◽  
Xihui Yang ◽  
Albert S. Baldwin ◽  
Rolf J. Craven ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Tumor Cells ◽  
Focal Adhesion ◽  
Death Receptor ◽  
Human Tumors ◽  
Receptor Complex ◽  
Death Domain ◽  
Functional Link ◽  
Interacting Protein ◽  
Survival Signals

ABSTRACT Tumor cells resist the apoptotic stimuli associated with invasion and metastasis by activating survival signals that suppress apoptosis. Focal adhesion kinase (FAK), a tyrosine kinase that is overexpressed in a variety of human tumors, mediates one of these survival signals. Attenuation of FAK expression in tumor cells results in apoptosis that is mediated by caspase 8- and FADD-dependent pathways, suggesting that death receptor pathways are involved in the process. Here, we report a functional link between FAK and death receptors. We have demonstrated that FAK binds to the death domain kinase receptor-interacting protein (RIP). RIP is a major component of the death receptor complex and has been shown to interact with Fas and tumor necrosis factor receptor 1 through its binding to adapter proteins. We have shown that RIP provides proapoptotic signals that are suppressed by its binding to FAK. We thus propose that FAK overexpression in human tumors provides a survival signal function by binding to RIP and inhibiting its interaction with the death receptor complex.

scholarly journals MicroRNA-27a-5p inhibits proliferation, migration and invasion and promotes apoptosis of Wilms tumor cell by targeting PBOV1

2021 ◽  
Author(s):  
zhengtuan guo ◽  
qiang yv ◽  
chunlin miao ◽  
wenan ge ◽  
peng li
Keyword(s):  
Tumor Cells ◽  
Wilms Tumor ◽  
Suppressive Effect ◽  
Luciferase Reporter ◽  
Migration And Invasion ◽  
Tumor Tissues ◽  
And Function ◽  
Tumor Suppressive Effect

Wilms tumor is the most common type of renal tumor in children. MicroRNAs (miRNA) are small non-coding RNAs that play crucial regulatory roles in tumorigenesis. We aimed to study the expression profile and function of miR-27a-5p in Wilms tumor. MiR-27a-5p expression was downregulated in human Wilms tumor tissues. Functionally, overexpression of miR-27a-5p promoted cell apoptosis of Wilms tumor cells. Furthermore, upregulated miR-27a-5p delayed xenograft Wilms tumor tumorigenesis in vivo. Bioinformatics analysis predicted miR-27-5p directly targeted to the 3’-untranslated region (UTR) of PBOV1 and luciferase reporter assay confirmed the interaction between miR-27a-5p and PBOV1. The function of PBOV1 in Wilms tumor was evaluated in vitro and knockdown of PBOV1 dampened cell migration. In addition, overexpression of PBOV1 antagonized the tumor-suppressive effect of miR-27a-5p in Wilms tumor cells. Collectively, our findings reveal the regulatory axis of miR-27-5p/PBOV1 in Wilms tumor and miR-27a-5p might serve as a novel therapeutic target in Wilms tumor.

Wilms tumor-suppressing peptide inhibits proliferation and induces apoptosis of Wilms tumor cells in vitro and in vivo

2019 ◽  
Vol 145 (10) ◽  
pp. 2457-2468 ◽  
Author(s):  
Wei Zhao ◽  
Juan Li ◽  
Ping Li ◽  
Fei Guo ◽  
Pengfei Gao ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Wilms Tumor

scholarly journals Inhibitory effect of Par-4 combined with cisplatin on human Wilms’ tumor cells

Tumor Biology ◽  
2017 ◽  
Vol 39 (7) ◽  
pp. 101042831771668 ◽  
Author(s):  
Jun Wang ◽  
Yunjie Li ◽  
Fangfang Ma ◽  
Huifeng Zhou ◽  
Rong Ding ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Wilms Tumor ◽  
Inhibitory Effect

Salmonella engineered to express CD20-targeting antibodies and a drug-converting enzyme can eradicate human lymphomas

Blood ◽  
2013 ◽  
Vol 122 (5) ◽  
pp. 705-714 ◽  
Author(s):  
Paul E. Massa ◽  
Aida Paniccia ◽  
Ana Monegal ◽  
Ario de Marco ◽  
Maria Rescigno
Keyword(s):  
Immune Response ◽  
Tumor Cells ◽  
Tumor Antigen ◽  
Adaptive Immune Response ◽  
Human Tumors ◽  
Converting Enzyme ◽  
Adaptive Immune ◽  
Key Points

Key PointsSalmonella is engineered to specifically infect tumor cells based on recognition of a tumor antigen by a bacterial-expressed antibody. Once inside, Salmonella can transfer cytotoxic cargos to destroy human tumors even in the absence of an adaptive immune response.

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