PI-3-kinase and MAPK regulate mesangial cell proliferation and migration in response to PDGF

1997 ◽  
Vol 273 (6) ◽  
pp. F931-F938 ◽  
Author(s):  
Goutam Ghosh Choudhury ◽  
C. Karamitsos ◽  
James Hernandez ◽  
Alessandra Gentilini ◽  
John Bardgette ◽  
...  
Keyword(s):  
Kinase Activity ◽  
Mesangial Cell ◽  
Mesangial Cells ◽  
Kinase Assay ◽  
Dependent Manner ◽  
Mapk Activity ◽  
And Migration ◽  
Dose Dependent ◽  
Proliferation And Migration

Proliferation and migration are important biological responses of mesangial cells to injury. Platelet-derived growth factor (PDGF) is a prime candidate to mediate these responses in glomerular disease. PDGF and its receptor (PDGFR) are upregulated in the mesangium during glomerular injury. We have recently shown that PDGF activates phosphatidylinositol 3-kinase (PI-3-kinase) in cultured mesangial cells. The role of this enzyme and other more distal signaling pathways in regulating migration and proliferation of mesangial cells has not yet been addressed. In this study, we used two inhibitors of PI-3-kinase, wortmannin (WMN) and LY-294002, to investigate the role of this enzyme in these processes. Pretreatment of mesangial cells with WMN and LY-294002 dose-dependently inhibited PDGF-induced PI-3-kinase activity assayed in antiphosphotyrosine immunoprecipitates. WMN pretreatment also inhibited the PI-3-kinase activity associated with anti-PDGFRβ immunoprecipitates prepared from mesangial cells treated with PDGF. Pretreatment of the cells with different concentrations of WMN resulted in a dose-dependent inhibition of PDGF-induced DNA synthesis. Both WMN and LY-294002 inhibited PDGF-stimulated migration of mesangial cells in a dose-dependent manner. It has recently been shown that PI-3-kinase physically interacts with Ras protein. Because Ras is an upstream regulator of the kinase cascade leading to the activation of mitogen-activated protein kinase (MAPK), we determined whether activation of PI-3-kinase is necessary for activation of MAPK. Pretreatment of mesangial cells with WMN and LY-294002 significantly inhibited PDGF-induced MAPK activity as measured by immune complex kinase assay of MAPK immunoprecipitates. Furthermore, PD-098059, an inhibitor of MAPK-activating kinase inhibited PDGF-induced MAPK activity and resulted in significant reduction of mesangial cell migration in response to PDGF. These data indicate that MAPK is a downstream target of PI-3-kinase and that both these enzymes are involved in regulating proliferation and migration of mesangial cells.

The role of CXCL16 and its processing metalloproteinases ADAM10 and ADAM17 in the proliferation and migration of human mesangial cells

2008 ◽  
Vol 370 (2) ◽  
pp. 311-316 ◽  
Author(s):  
Anja Schramme ◽  
Mohamed Sadek Abdel-Bakky ◽  
Nicole Kämpfer-Kolb ◽  
Josef Pfeilschifter ◽  
Paul Gutwein
Keyword(s):  
Mesangial Cells ◽  
Human Mesangial Cells ◽  
And Migration ◽  
Proliferation And Migration

scholarly journals Proteolytic Cleavage of Cyclin E Leads to Inactivation of Associated Kinase Activity and Amplification of Apoptosis in Hematopoietic Cells

2002 ◽  
Vol 22 (7) ◽  
pp. 2398-2409 ◽  
Author(s):  
Suparna Mazumder ◽  
Bendi Gong ◽  
Quan Chen ◽  
Judith A. Drazba ◽  
Jeffrey C. Buchsbaum ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Cell Cycle Progression ◽  
Kinase Activity ◽  
Cyclin E ◽  
Genotoxic Stress ◽  
Dependent Manner ◽  
Amino Acid Residues ◽  
Dose Dependent

ABSTRACT Cyclin E/Cdk2 is a critical regulator of cell cycle progression from G1 to S in mammalian cells and has an established role in oncogenesis. Here we examined the role of deregulated cyclin E expression in apoptosis. The levels of p50-cyclin E initially increased, and this was followed by a decrease starting at 8 h after treatment with genotoxic stress agents, such as ionizing radiation. This pattern was mirrored by the cyclin E-Cdk2-associated kinase activity and a time-dependent expression of a novel p18-cyclin E. p18-cyclin E was induced during apoptosis triggered by multiple genotoxic stress agents in all hematopoietic tumor cell lines we have examined. The p18-cyclin E expression was prevented by Bcl-2 overexpression and by the general caspase and specific caspase 3 pharmacologic inhibitors zVAD-fluoromethyl ketone (zVAD-fmk) and N-acetyl-Asp-Glu-Val-Asp-aldehyde (DEVD-CHO), indicating that it was linked to apoptosis. A p18-cyclin E276-395 (where cyclin E276-395 is the cyclin E fragment containing residues 276 to 395) was reconstituted in vitro, with mutagenesis experiments, indicating that the caspase-dependent cleavage was at amino acid residues 272 to 275. Immunoprecipitation analyses of the ectopically expressed cyclin E1-275, cyclin E276-395 deletion mutants, and native p50-cyclin E demonstrated that caspase-mediated cyclin E cleavage eliminated interaction with Cdk2 and therefore inactivated the associated kinase activity. Overexpression of cyclin E276-395, but not of several other cyclin E mutants, specifically induced phosphatidylserine exposure and caspase activation in a dose-dependent manner, which were inhibited in Bcl-2-overexpressing cells or in the presence of zVAD-fmk. Apoptosis and generation of p18-cyclin E were significantly inhibited by overexpressing the cleavage-resistant cyclin E mutant, indicating a functional role for caspase-dependent proteolysis of cyclin E for apoptosis of hematopoietic tumor cells.

scholarly journals High Glucose Induces Sumoylation of Smad4 via SUMO2/3 in Mesangial Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Xueqin Zhou ◽  
Chenlin Gao ◽  
Wei Huang ◽  
Maojun Yang ◽  
Guo Chen ◽  
...  
Keyword(s):  
High Glucose ◽  
Laser Scanning ◽  
Transforming Growth Factor ◽  
Mesangial Cells ◽  
Critical Role ◽  
Confocal Laser ◽  
Dependent Manner ◽  
High Glucose Condition ◽  
Dose Dependent

Recent studies have shown that sumoylation is a posttranslational modification involved in regulation of the transforming growth factor-β(TGF-β) signaling pathway, which plays a critical role in renal fibrosis in diabetic nephropathy (DN). However, the role of sumoylation in the regulation of TGF-βsignaling in DN is still unclear. In the present study, we investigated the expression of SUMO (SUMO1 and SUMO2/3) and Smad4 and the interaction between SUMO and Smad4 in cultured rat mesangial cells induced by high glucose. We found that SUMO1 and SUMO2/3 expression was significantly increased in the high glucose groups compared to the normal groupP<0.05. Smad4 and fibronectin (FN) levels were also increased in the high glucose groups in a dose-dependent manner. Coimmunoprecipitation and confocal laser scanning revealed that Smad4 interacted and colocalized with SUMO2/3, but not with SUMO1 in mesangial cells. Sumoylation (SUMO2/3) of Smad4 under high glucose condition was strongly enhanced compared to normal controlP<0.05. These results suggest that high glucose may activate TGF-β/Smad signaling through sumoylation of Samd4 by SUMO2/3 in mesangial cells.

scholarly journals Involvement of F-Actin in Chaperonin-Containing t-Complex 1 Beta Regulating Mouse Mesangial Cell Functions in a Glucose-Induction Cell Model

2011 ◽  
Vol 2011 ◽  
pp. 1-10 ◽  
Author(s):  
Jin-Shuen Chen ◽  
Li-Chien Chang ◽  
Chia-Chao Wu ◽  
Lai-King Yeung ◽  
Yuh-Feng Lin
Keyword(s):  
Mesangial Cell ◽  
Cell Model ◽  
Cell Contraction ◽  
Small Interference Rna ◽  
Cell Functions ◽  
T Complex ◽  
Glucose Induction ◽  
And Migration ◽  
Proliferation And Migration

The aim of this study is to investigate the role of chaperonin-containing t-complex polypeptide 1 beta (CCT2) in the regulation of mouse mesangial cell (mMC) contraction, proliferation, and migration with filamentous/globular-(F/G-) actin ratio under high glucose induction. A low CCT2 mMC model induced by treatment of small interference RNA was established. Groups with and without low CCT2 induction examined in normal and high (H) glucose conditions revealed the following major results: (1) low CCT2 or H glucose showed the ability to attenuate F/G-actin ratio; (2) groups with low F/G-actin ratio all showed less cell contraction; (3) suppression of CCT2 may reduce the proliferation and migration which were originally induced by H glucose. In conclusion, CCT2 can be used as a specific regulator for mMC contraction, proliferation, and migration affected by glucose, which mechanism may involve the alteration of F-actin, particularly for cell contraction.

scholarly journals IGFBP7 As a Potential Therapeutic Target for AML

Blood ◽  
2018 ◽  
Vol 132 (Supplement 1) ◽  
pp. 5134-5134
Author(s):  
Yina Niu ◽  
Shuiyan Wu ◽  
Shaoyan Hu
Keyword(s):  
Cell Lines ◽  
Conflicts Of Interest ◽  
Fold Increase ◽  
Dependent Manner ◽  
Mice Model ◽  
Cell Counts ◽  
And Migration ◽  
Proliferation And Migration

Abstract Insulin-like growth factor binding proteins (IGFBPs) are secretory factors that play essential roles in regulation of insulin-like growth factors (IGFs) in tissue as well as in modulating IGF binding to its receptors. IGFBP7, known as IGFBP-related protein 1 (IGFBP-rP1), mac25/angiomodulin, function as a potential tumor suppressor in various human solid cancers, including breast, prostate, gastric and liver cancer. We have reported the overexpression of IGFBP7 in the context of acute myeloid leukemia (AML), showing that IGFBP7 expression level in AML patients is significantly increased compared with controls (P<0.001). IGFBP7 expression was obviously decreased in AML patients achieving complete remission (P<0.01), and was significantly increased in relapsed AML patients (P<0.01). In addition, AML patients with high expression of IGFBP7 had shorter overall survival. Here, we investigate the role and mechanism of IGFBP7 in the development and progression of AML. In order to study the role of IGFBP7 in AML, stable cell lines expressing IGFBP7 and control in AML cells were constructed using lentiviral packaging system. Expression microarray assay was carried out to analyze the global gene level changes driven by IGFBP7. MTT and transwell assays were performed to evaluate the effect of IGFBP7 on cell proliferation and migration. Bioinformatics results found that IGFBP7 appeared to utilize multiple cellular processes for its oncogenic roles, including adhesion, migration, and proliferation. Experimental data showed overexpression of IGFBP7 in K562 cells resulted in a 2-3 fold increase in migration in contrast to control cells. Moreover, enforced expression of IGFBP7 also led to phosphorylation of Akt and Erk, whose activities inactivation by pharmacologically inhibitors resulted in the loss of ability to migrating. Finally, knockdown of IGFBP7 in cells with high IGFBP7 level, their migration abilities were significantly decreased. To assess the role of IGFBP7 in leukemogenesis in vivo, the same numbers of K562/IGFBP7 and K562-Vector cells, U937-shIGFBP7 and U937-shNEG cells were injected into NOD-SCID mice by tail vein injection, respectively. About two weeks later, it was showed that mice of K562/IGFBP7 and U937 groups displayed higher white blood cell counts compared with mice of K562-Vector and U937-shIGFBP7 groups, respectively. Mice of K562/IGFBP7 and U937 groups had more severe splenomegaly and hepatomagaly compared with its corresponding control groups. We further characterized the molecular mechanism underlying leukemogenesis driven by IGFBP7 in AML cell lines. The global expression profiling and molecular biological experiments showed PI3K/AKT signaling was activated by overexpression of IGFBP7, and knockdown of IGFBP7 in AML cells led to a decrease of PI3K/AKT activity in PTEN-dependent manner. IGFBP7 promotes proliferation and migration of AML cells, the promotion could be suppressed by both RNA interference and pharmacological inhibition of PI3K/AKT pathway. Immuno-precipitation assay showed that IGFBP7 associated with AXAN2 and induced PTEN degradation. The expression of ANXA2 was significantly positive correlated with the expression ANXA2 in AML patients. The expression of IGFBP7 in AML, overexpression as well as knockdown of IGFBP7 in leukemia cells and in mice model, all suggest that IGFBP7 is a potential proto-oncogene. Collectively this work suggests that targeting IGFBP7 activity may be an effective therapeutic strategy for AML. Disclosures No relevant conflicts of interest to declare.

NPM-ALK Regulated GSK3β Phosphorylation Results in Mcl-1 and CDC25A Accumulation and Enhanced Oncogenic Potential

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 586-586
Author(s):  
Scott RP McDonnell ◽  
Steven R Hwang ◽  
Venkatesha Basrur ◽  
Kevin P Conlon ◽  
Damian Fermin ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Colony Formation ◽  
Kinase Activity ◽  
Cell Lymphoma ◽  
Dependent Manner ◽  
Colony Formation Assay ◽  
Oncogenic Potential ◽  
Anaplastic Lymphoma ◽  
Dose Dependent

Abstract Abstract 586 Anaplastic large cell lymphoma (ALCL) is the most common type of pediatric peripheral T-cell lymphoma. ALCLs are frequently characterized by translocations involving the anaplastic lymphoma kinase (ALK) gene. In 70–80% of these cases, the chromosomal aberration t(2;5)(p23;q35) results in the juxtaposition of ALK with nucleophosmin (NPM) and the subsequent expression of the NPM-ALK tyrosine kinase. NPM-ALK is an oncogenic tyrosine kinase which induces numerous signaling pathways that drive proliferation and abrogate apoptosis. However, the mechanisms that lead to activation of downstream growth regulatory molecules in ALCLs have not been completely elucidated. Using a mass spectrometry-based phosphoproteomic screen, we identified GSK3β, as a potential signaling mediator of NPM-ALK. Using a selective inhibitor of ALK, we demonstrated that the tyrosine kinase activity of ALK regulates the phosphorylation of GSK3β at serine-9 (pS9-GSK3β) in a time and dose-dependent manner. Expression of NPM-ALK in 293T cells led to increased phosphorylation of GSK3β at serine-9 compared to kinase-defective K210R mutant NPM-ALK but did not affect total GSK3β levels. Inducible knockdown of ALK in SU-DHL-1 cells also led to decreased phosphorylation of GSK3β at serine-9 without affecting total GSK3β levels. Selective inhibition of PI3Kδ by CAL-101 resulted in decreased phosphorylation of GSK3β at serine-9 in a dose dependent manner without affecting total GSK3β or NPM-ALK activity. Ablation of ALK kinase activity resulted in proteasomal degradation of GSK3β substrates Mcl-1 and CDC25A. This degradation was recovered upon chemical inhibition of GSK3β (GSK3 IX). To address the role of GSK3β in ALCL proliferation, WST-1 assay revealed that ALK inhibition resulted in a decrease in cell viability which was rescued by GSK3β inhibition. ALK inhibition resulted in significant cellular apoptosis as detected by propidium iodide and Annexin V staining followed by flow cytometry. This apoptotic response was rescued by GSK3β inhibition. The effect of GSK3β on cellular oncogenic potential was addressed by colony formation assay using ALCL-derived cell lines. While ALK inhibition resulted in decreased colony numbers, simultaneous ALK and GSK3β inhibition recovered colony numbers compared to ALK inhibition alone. Additionally, stable GSK3β knockdown conferred resistance to growth inhibitory effect of ALK inhibition as determined by colony formation assay. Furthermore, pS9-GSK3β and its known substrate, CDC25A were selectively expressed in neoplastic cells of ALK+ALCL tissue biopsies and showed a significant correlation (p<0.001). Conversely, ALK-ALCL tissue biopsies showed no significant correlation of pS9-GSK3β and CDC25A expression (p<0.2). Our results demonstrate that NPM-ALK signals through PI3K/AKT to phosphorylate GSK3β at serine-9. This phosphorylation inhibits GSK3β kinase activity which results in the accumulation of CDC25A and Mcl-1 thus providing growth advantage and protection from apoptosis. These findings provide support for the role of GSK3β as a novel mediator of NPM-ALK oncogenesis. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Astragalin Attenuates UVB Radiation-induced Actinic Keratosis Formation

2018 ◽  
Vol 18 (7) ◽  
pp. 1001-1008 ◽  
Author(s):  
Na Li ◽  
Kun Zhang ◽  
Xin Mu ◽  
Qiong Tian ◽  
Wenli Liu ◽  
...  
Keyword(s):  
P38 Mapk ◽  
Actinic Keratosis ◽  
Kinase Assay ◽  
Dependent Manner ◽  
Hacat Cells ◽  
Induced Expression ◽  
Mapk Activity ◽  
Dose Dependent

Background: Actinic Keratosis (AK), is the most common precancerous skin lesion induced by the excessive Ultraviolet B (UVB) and is a significant threat to the public health. UVB exposure causes oxidative DNA damage and is considered to be a significant contributor to AK and subsequent development of skin cancer. Besides, activation of p38 MAPK also plays a significant role in the development of AK. Objective: This study aimed at the development of a nature compound which can inhibit UVB-induced AK. Method: MTS Cell Proliferation Assay Kit was used to detect the toxicity of astragalin. HE-staining, Immunohistochemical, Western blot and Enzyme Linked Immunosorbent Assay were applied to examine the clinicopathologic feature of AK and the change of p38 MAPK signal pathway treated with astraglin under the condition of UVB in vitro and in vivo. </P><P> Results：In our clinical findings revealed that p38 MAPK, phospho-MSK1, and γ -H2AX were significantly highly expressed in human AK tissue than the normal healthy skin tissue. Moreover, in vitro studies showed that UVB induced the phospho-MSK1 and γ-H2AX in a time- and dose-dependent manner in HaCaT cells. Further, in vitro kinase assay demonstrated that astragalin could directly bind to p38 MAPK and suppress p38 MAPK activity. Furthermore, astragalin exhibited no toxicity and suppressed the UVB-induced expression of phospho- MSK1 and γ -H2AX by suppressing p38 MAPK activity in a time-dependent and dose-dependent manner in HaCaT cells. The in vivo studies with animal UV model demonstrated that astragalin inhibited UVB-induced expression of phospho-MSK1 and γ-H2AX in Babl/c mice. Conclusion: These results suggested that p38 MAPK is a direct valid molecular target of astragalin for the attenuation of UVB-induced AK. Furthermore, astragalin could be a potential promising novel natural therapeutic agent for the prevention and management of UVB-induced AK with high target specificity and low toxicity.

CD40-Dependent Activation of Phosphatidylinositol 3-Kinase/Akt Pathway Inhibits Apoptosis of Human Cultured Mesangial Cells Induced by Oxidized LDL

2005 ◽  
Vol 18 (2) ◽  
pp. 327-337 ◽  
Author(s):  
I. Deambrosis ◽  
E. Scalabrino ◽  
M.C. Deregibus ◽  
G. Camussi ◽  
B. Bussolati
Keyword(s):  
Enzymatic Activity ◽  
Mesangial Cells ◽  
Oxidized Ldl ◽  
Kinase Assay ◽  
Akt Pathway ◽  
Dependent Manner ◽  
Glomerular Diseases ◽  
Apoptotic Effect ◽  
Cd40 Stimulation ◽  
Dose Dependent

Deposition of atherogenic lipoproteins is associated with various glomerular diseases. In particular, oxidized LDL (oxLDL) may affect mesangial cells and favour the development of glomerulosclerosis. The aim of the present study was to investigate on cultured human mesangial cells (HMC) whether oxLDL induces apoptosis by a mechanism dependent on the inhibition of Akt survival pathway, and whether the engagement of mesangial CD40 by its ligand CD154 inhibits the apoptotic effect of oxLDL. Tunel assays demonstrated that incubation of HMC for 24h with oxLDL, but not with unmodified LDL, induced a dose-dependent increase in apoptosis of HMC associated with a decrease in Akt phosphorylation. Enzymatic kinase assay showed that also the Akt activity was reduced in a dose-dependent manner by treatment with oxLDL. Stimulation of mesangial CD40 with sCD154 rescued HMC from oxLDL-dependent apoptosis, while two unrelated pharmacological inhibitors of PI3K LY294002 and wortmannin abrogated this anti-apoptotic effect, suggesting an involvement of the PI3K/Akt pathway. Moreover CD40 stimulation maintained an elevated phosphorylation of Akt and preserved its enzymatic activity in the presence of oxLDL. Indeed, CD154 induced a rapid enhancement in Akt enzymatic activity, that was temporarily correlated with the association of CD40 with TRAF3, TRAF6, c-Cbl and the p85 subunit of PI3K. In conclusion, these results suggest that CD40 stimulation protects HMC from toxic effects of oxLDL by promoting PI3K/Akt-dependent cell survival.

scholarly journals Erratum

2021 ◽  
Vol 28 (6) ◽  
pp. 675-679
Author(s):  
Chang Li ◽  
Shuohui Gao ◽  
Xiaoping Li ◽  
Chang Li ◽  
Lianjun Ma
Keyword(s):  
Colon Cancer ◽  
Cell Proliferation ◽  
Underlying Mechanism ◽  
Dependent Manner ◽  
Anesthetic Drug ◽  
And Migration ◽  
Dose Dependent ◽  
Local Anesthetic Drug ◽  
Hct116 Cells ◽  
Proliferation And Migration

Colon cancer is one of the most lethal varieties of cancer. Chemotherapy remains as one of the principal treatment approaches for colon cancer. The anticancer activity of procaine (PCA), which is a local anesthetic drug, has been explored in different studies. In our study, we aimed to explore the anticancer effect of PCA on colon cancer and its underlying mechanism. The results showed that PCA significantly inhibited cell viability, increased the percentage of apoptotic cells, and decreased the expression level of RhoA in HCT116 cells in a dose-dependent manner (p<0.05 or p<0.01). Moreover, PCA increased the proportion of HCT116 cells in the G1 phase as well as downregulated cyclin D1 and cyclin E expressions (p<0.05). In addition, we found that PCA remarkably inhibited cell migration in HCT116 cells (p<0.01). However, all these effects of PCA on cell proliferation, apoptosis, and migration were significantly reversed by PCA+pc-RhoA (p<0.05 or p<0.01). PCA also significantly decreased the levels of p-ERK, p-p38MAPK, and p-FAK, but PCA+pc-RhoA rescued these effects. Furthermore, the ERK inhibitor (PD098059), p38MAPK inhibitor (SB203580), and FAK inhibitor (Y15) reversed these results. These data indicate that PCA inhibited cell proliferation and migration but promoted apoptosis as well as inactivated the ERK/MAPK/FAK pathways by regulation of RhoA in HCT116 cells.

scholarly journals Mechanism of resistin-induced enhancement of proliferation and migration of ovarian cancer cells

2020 ◽  
Author(s):  
Li Pang ◽  
Xian-li Li
Keyword(s):  
Ovarian Cancer ◽  
Wound Healing ◽  
Cancer Cells ◽  
Molecular Mechanisms ◽  
Ovarian Cancer Cells ◽  
Dependent Manner ◽  
Ovarian Epithelial Carcinoma ◽  
And Migration ◽  
Proliferation And Migration

IntroductionResistin, a novel hormone secreted by human adipocytes and mononuclear cells, is associated with obesity, insulin resistance, and inflammation. Recent studies showed that resistin plays a key role in ovarian cancer cells. In this study, we investigated the potential of resistin to regulate the proliferation and migration of ovarian cancer cells.Material and methodsA series of in vitro functional experiments were carried out to elucidate the role of resistin in ovarian cancer progression and the molecular mechanisms underlying its role.ResultsResistin enhanced the proliferation of human ovarian epithelial carcinoma cells (HO-8910) in a time- and dose-dependent manner (30–100 ng/ml). Furthermore, HO-8910 cells cultured in adipocyte-conditioned medium showed dramatically increased rates of proliferation. Resistin knockout during adipocyte culture attenuated the proliferation of HO-8910 cells treated with adipocyte-conditioned media, indicating that resistin may promote HO-8910 cell proliferation via the mechanistic target of a rapamycin (mTOR)-mediated signaling pathway. Resistin (30–100 ng/ml) also enhanced wound-healing rates in a time- and concentration-dependent manner. Co-culturing HO-8910 cells with adipocytes also increased the wound-healing rates. Resistin expression was inhibited by miR-124-1 transcriptional activity, and resistin-mediated HO-8910 cell migration was also regulated by miR-124-1. Furthermore, we also confirmed the role of resistin in promoting tumor growth in vivo.ConclusionsThese findings suggest that resistin may serve as an effective therapeutic target for ovarian epithelial carcinoma, especially in patients who are obese.

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