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Dysregulation of c-terminal ezrin phosphorylation prevents tumor progression and metastasis and alters cellular metabolism in osteosarcoma

ABSTRACT: This dataset contains Affymetrix Mouse Genome 430 2.0 Array data obtained from K7M2 cells over-expressing ezrinT567A and the wild-type

ORGANISM(S): Mus musculus

PROVIDER: GSE33897 | GEO | 2012/03/14

SECONDARY ACCESSION(S): PRJNA148255

REPOSITORIES: GEO

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Dysregulation of c-terminal ezrin phosphorylation prevents tumor progression and metastasis and alters cellular metabolism in osteosarcoma

Project description:This dataset contains Affymetrix Mouse Genome 430 2.0 Array data obtained from K7M2 cells over-expressing ezrinT567A and the wild-type Gene expression analysis of K7M2 cells over-expressing ezrinT567A compared to the wild-type

2012-03-14 | E-GEOD-33897 | biostudies-arrayexpress

Dysregulation of ezrin phosphorylation prevents metastasis and alters cellular metabolism in osteosarcoma.

Project description:Ezrin links the plasma membrane to the actin cytoskeleton where it plays a pivotal role in the metastatic progression of several human cancers; however, the precise mechanistic basis for its role remains unknown. Here, we define transitions between active (phosphorylated open) and inactive (dephosphorylated closed) forms of Ezrin that occur during metastatic progression in osteosarcoma. In our evaluation of these conformations we expressed C-terminal mutant forms of Ezrin that are open (phosphomimetic T567D) or closed (phosphodeficient T567A) and compared their biologic characteristics to full-length wild-type Ezrin in osteosarcoma cells. Unexpectedly, cells expressing open, active Ezrin could form neither primary orthotopic tumors nor lung metastases. In contrast, cells expressing closed, inactive Ezrin were also deficient in metastasis but were unaffected in their capacity for primary tumor growth. By imaging single metastatic cells in the lung, we found that cells expressing either open or closed Ezrin displayed increased levels of apoptosis early after their arrival in the lung. Gene expression analysis suggested dysregulation of genes that are functionally linked to carbohydrate and amino acid metabolism. In particular, cells expressing closed, inactive Ezrin exhibited reduced lactate production and basal or ATP-dependent oxygen consumption. Collectively, our results suggest that dynamic regulation of Ezrin phosphorylation at amino acid T567 that controls structural transitions of this protein plays a pivotal role in tumor progression and metastasis, possibly in part by altering cellular metabolism.

| S-EPMC3867810 | biostudies-literature

RNA sequencing of murine osteosarcoma tumors

Project description:We utilized murine osteosarcoma cell lines F420 and K7M2. F420 was originally derived from a female C57BL/6 mouse transgenic for a mutant p53 under control of a bone-selective promoter (PMID: 25579177). K7M2 was derived from a spontaneous metastatic lesion in a female Balb/C background (PMID: 16837208). F420 osteosarcoma tumors were established by subcutaneously injecting 5 x 10^6 osteosarcoma cells into the flanks of 6-week-old C57BL/6 mice (Envigo, Frederick, MD). K7M2 tumors were established by transplanting small pieces of sectioned tumor (~2mm3) into the flanks of 6-week-old Balb/C mice (Envigo). We found K7M2 to be more immunogenic than F420 as it demonstrated higher immune cell infiltrates, higher expression of immune-related genes, and slower growth in syngeneic versus nude models.

2021-06-29 | GSE166282 | GEO

Poly (ADP-ribose) polymerase 1 (PARP1) inhibition promotes pulmonary metastasis of osteosarcoma by boosting ezrin phosphorylation.

Project description:Due to the large proportion of BRCA deficiency and chromosomal instability in OS patients, poly (ADP-ribose) polymerase inhibitors (PARPi) could be an effective strategy for anti-OS therapy. In two orthotopic OS mouse models, we discovered that although PARPi had inhibitory effect on the growth of the orthotopic OS tumors regardless of BRCA deficiency, the treatment of PARPi essentially aggravated the pulmonary metastasis of OS in both models. A protein playing a crucial role in OS metastasis, ezrin, was identified as an interactive protein for PARP1. The phosphorylation of ezrin was significantly promoted during PARP inhibition. Besides the traditional function of phosphorylated ezrin at plasma membrane, we newly identified its nuclear speckle localization and its function with mRNA export. Ezrin knockdown or phosphorylation inhibition could partially rescue PARPi induced metastasis. Collectively, we unveiled a new mechanism for PARP-involved OS metastasis, which proposed a novel combinational therapy strategy using PARP and ezrin inhibitors for future OS treatment.

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Mus musculus

Project description:Mouse brain region gene expression (430 2.0 Array)

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LC-MS/MS of extracellular vesicles from murine osteosarcoma cell line K7 and K7M2

Project description:Extracellular vesicles have been shown to be highly enriched in proteins with various functions, including organotropic metastasis. To identify possible protein cargos involved in regulating mestastatic potential of osteosarcoma cell line, we performed quantitative mass spectrometry analysis of EVs from highly metastatic K7M2 cells and poorly metastatic parental K7 cells.

2024-01-15 | PXD035216 | Pride

Role of Ezrin Phosphorylation in HIV-1 Replication.

Project description:Host-cell expression of the ezrin protein is required for CXCR4 (X4)-tropic HIV-1 infection. Ezrin function is regulated by phosphorylation at threonine-567. This study investigates the role of ezrin phosphorylation in HIV-1 infection and virion release. We analyzed the effects of ezrin mutations involving substitution of threonine-567 by alanine (EZ-TA), a constitutively inactive mutant, or by aspartic acid (EZ-TD), which mimics phosphorylated threonine. We also investigated the effects of ezrin silencing on HIV-1 virion release using a specific siRNA. We observed that X4-tropic HIV-1 vector infection was inhibited by expression of the EZ-TA mutant but increased by expression of the EZ-TD mutant, suggesting that ezrin phosphorylation in target cells is required for efficient HIV-1 entry. Expression of a dominant-negative mutant of ezrin (EZ-N) and ezrin silencing in HIV-1 vector-producing cells significantly reduced the infectivity of released virions without affecting virion production. This result indicates that endogenous ezrin expression is required for virion infectivity. The EZ-TD but not the EZ-TA inhibited virion release from HIV-1 vector-producing cells. Taken together, these findings suggest that ezrin phosphorylation in target cells is required for efficient HIV-1 entry but inhibits virion release from HIV-1 vector-producing cells.

| S-EPMC6119696 | biostudies-literature

RenalMSCvsJGcells_MouseMicroarray

Project description:Microarray data comparison of renal mesenchymal stromal cells (MSC) vs Juxtaglomerular cells using Affimetric Mouse 430 2.0

2021-05-24 | GSE114903 | GEO

Gene expression profiling of HhAntag-treated pancreatic xenografts

Project description:Four vehicle-treated and four HhAntag-treated pancreatic xenograft tumors were profiled for gene expression changes using Affymetrix U133 Plus 2.0 and Affymetrix Mouse Genome 430 2.0 arrays. Keywords: comparative gene expression, hedgehog, hh

2008-09-12 | GSE11981 | GEO

Design, synthesis and biological evaluation of ezrin inhibitors targeting metastatic osteosarcoma.

Project description:Respiratory failure due to pulmonary metastasis is the major cause of death for patients with osteosarcoma. However, the molecular basis for metastasis of osteosarcoma is poorly understood. Recently, ezrin, a member of the ERM family of proteins, has been associated with osteosarcoma metastasis to the lungs. The small molecule NSC 668394 was identified to bind to ezrin, inhibit in vitro and in vivo cell migration, invasion, and metastatic colony survival. Reported herein are the design and synthesis of analogues of NSC 668394, and subsequent functional ezrin inhibition studies. The binding affinity was characterized by surface plasmon resonance technique. Cell migration and invasion activity was determined by electrical cell impedance methodology. Optimization of a series of heterocyclic-dione analogues led to the discovery of compounds 21k and 21m as potential novel antimetastatic agents.

| S-EPMC4349528 | biostudies-literature

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