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Experimental cell research 18건

  1. [해외논문]   IFC/ Editorial Board   SCI SCIE


    Experimental cell research v.361 no.2 ,pp. IFC - IFC , 2017 , 0014-4827 ,

    초록

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  2. [해외논문]   Study on the role of Hsa-miR-31-5p in hypertrophic scar formation and the mechanism   SCI SCIE

    Wang, X. (Department of Dermatology and Dermatologic Surgery, Shanghai 9th People's Hospital, Shanghai Jiao Tong University School of Medicine, 639 Zhi Zao Ju Road, Shanghai 200011, PR China ) , Zhang, Y. (Department of Orthopedics, Shanghai Tongji Hospital, Tongji University School of Medicine, 389 Xincun Road, Shanghai 200065, PR China ) , Jiang, B.H. (Department of Plastic and Reconstructive Surgery, The First Affiliated Hospital of Bengbu Medical College, Bengbu Medical College, Bengbu, An'hui, PR China ) , Zhang, Q. (People's Hospital of Dancheng County, Dancheng City, Henan Province, PR China ) , Zhou, R.P. (Department of Plastic and Reconstructive Surgery, Shanghai 9th People's Hospital, Shanghai Jiao Tong University School of Medicine, 639 Zhi Zao Ju Road, Shanghai 200011, PR China ) , Zhang, L. (Department of Plastic and Reconstructive Surgery, The First Affiliated Hospital of Bengbu Medical College, Bengbu Medical College, Bengbu, An'hui, PR China ) , Wang, Chen (Department of Plastic and Reconstructive Surgery, Shanghai 9th People's Hospital, Shanghai Jiao Tong)
    Experimental cell research v.361 no.2 ,pp. 201 - 209 , 2017 , 0014-4827 ,

    초록

    Abstract Hypertrophic scar (HS) formation is associated with the fibrosis of fibrocytes caused by excessive extracellular matrix (ECM) synthesis and deposition, the initial event of HS formation. Our high throughput screen of miRNA expression profiles identified hsa-miR31-5p, whose transcription level was most differentially in normal skin fibroblasts (NS) and HS among other miRNAs. The level of hsa-miR31-5p in HS was significantly higher than in NS. In-vitro functional experiments showed hsa-miR31-5p knockdown remarkably suppressed the proliferation of hypertrophic scar fibroblasts (HSFBs) under hypoxia, promoted cell invasion, and inhibited the expression of Collagen I and III and Fibronectin (FN), suggesting that hsa-miR31-5p knockdown effectively reduces HS formation caused by excessive ECM synthesis and deposition in HSFBs under hypoxia. Mechanism study showed that the regulation of HS formation by hsa-miR31-5p was mediated by its target gene, factor-inhibiting HIF-1 (FIH): under hypoxia, hsa-miR31-5p down-regulated FIH and thus increased the level of hypoxia inducible factor-1α (HIF-1α), which subsequently activated the HIF-1α fibrosis regulation pathway in HSFBs, and stimulated the proliferation and ECM synthesis in HSFBs, eventually resulting in fibrosis and scar formation. The data also show that knockdown of hsa-miR31-5p in HSFBs impaired the trend of increased proliferation, reduced invasion and excessive ECM synthesis and deposition caused by HIF-1a activation under hypoxia through upregulating FIH, indicating that knockdown of hsa-miR31-5p effectively inhibits the formation of HS. In conclusion, hsa-miR31 -5p plays an important role in HS formation by inhibiting FIH and regulating the HIF-1α pathway. Therefore, hsa-miR31 -5p may be a novel therapeutic target for HS. Highlights The level of miR31-5p in HS was higher than in NS. MiR31-5p plays a central role for hypoxia induced ECM synthesis and contraction. Blocking miR31-5p inhibits HIF-1a activation in hypoxic via upregulating FIH.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  3. [해외논문]   Smad7 alleviates glomerular mesangial cell proliferation via the ROS-NF-κB pathway   SCI SCIE

    Lin, Nana (Correspondence to: The Second Affiliated Hospital of Guangzhou Medical University, No. 195 Dongfeng Xi Road, Guangzhou 510182, China.) , Ji, Zequan , Huang, Cuiwen
    Experimental cell research v.361 no.2 ,pp. 210 - 216 , 2017 , 0014-4827 ,

    초록

    Abstract Objective The aim of this study was to demonstrate that altered gene expression of Smad7regulated NF-κB expression and ROS production on Ang II (Angiotensin II)-induced rat glomerular mesangial cell (GMC) proliferation. Methods pAdTrack-CMV-Smad7 was transduced into rat GMC by adeno-transduction using an ADV (adenovirus)-mediated vector in vivo. Diphenylene iodonium chloride (DPI) pre-treated GMC, and blocked ROS generation as determined by DCFH-DA method. Altered expressions of IκBα and p65 were monitored by Western blot analysis and immunofluorescence. GMC proliferation was tested by the Cell Counting Kit-8 assay. Apoptosis of GMC was detected by flow cytometric analysis. Results Over-expression of Smad7 dampened the ability of Ang II to promote ROS synthesis and inhibited the ability of Ang II to decrease functional expression of IκBα. Moreover, Smad7 increased nuclear IκBα expression. Smad7 did not significantly influence the capacity of Ang II to increase protein expression of NF-κB p65. However, immunofluorescence analysis showed that Smad7 reduced nuclear NF-κB p65 level. Further, over-expression of Smad7 promoted GMC apoptosis by inhibiting NF-κB activation, which alleviated the Ang II-promoted proliferation of GMC. Conclusions Smad7 influenced NF-κB expression by regulating ROS generation, and induced GMC apoptosis to counter the Ang II-promoted proliferation. Highlights Smad7 alleviates glomerular mesangial cell proliferation. Smad7 regulates NF-κB through a mechanism involving ROS production. Smad7 affects not only cell proliferation but also cell apoptosis.

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    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  4. [해외논문]   Hemoglobin pretreatment endows rat cortical astrocytes resistance to hemin-induced toxicity via Nrf2/HO-1 pathway   SCI SCIE

    Yang, Yong (Department of Neurosurgery, Ruijin Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200025, China ) , Xi, Zhiyu (Department of Neurosurgery, Ruijin Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200025, China ) , Xue, Yuan (Zhenjiang Center for Disease Control and Prevention, Zhenjiang 212000, China ) , Ren, Jie (Department of Neurosurgery, Ruijin Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200025, China ) , Sun, Yuhao (Department of Neurosurgery, Ruijin Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200025, China ) , Wang, Baofeng (Department of Neurosurgery, Ruijin Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200025, China ) , Zhong, Zhihong (Department of Neurosurgery, Ruijin Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200025, China ) , Yang, Guo-yuan (Neuroscience and Neuroengineering Research Center, Med-X Research Institute, Shanghai Jiao Tong University, Shanghai 200030, China ) , Sun, Qingfang (Department of Neurosurgery, Ruijin Hospital, Shanghai Jiao Ton) , Bian, Liuguan
    Experimental cell research v.361 no.2 ,pp. 217 - 224 , 2017 , 0014-4827 ,

    초록

    Abstract Oxidative stress mediated secondary injury contributes to neurological deterioration after intracerebral hemorrhage (ICH). Astrocytes, the most dominant cells in the central nervous system (CNS), play key roles in maintaining redox homeostasis by providing oxidative stress defense. Hemoglobin (Hb), the primary component released by hemolysis, is an effective activator of astrocytes. Hemin, the product of Hb degradation, is highly toxic due to the induction of reactive oxygen species (ROS). We speculate that Hb-activated astrocytes are resistant to hemin-induced toxicity. To verify our speculation, Hb-pretreated astrocytes were exposed to hemin, intracellular ROS accumulation and cell apoptosis were evaluated. Heme oxygenase 1 (HO-1) and nuclear transcription factor-erythroid 2 related factor (Nrf2) expression were observed to explore the potential mechanism. The results demonstrated that Hb induced upregulation and nuclear translocation of Nrf2 in astrocytes, resulted in HO-1 upregulation, which contributed to reduced ROS accumulation and apoptosis rate. Knocking down Nrf2 expression by siRNA suppressed Hb-induced upregulation of HO-1 expression and increased the susceptibility of Hb-pretreated astrocytes to hemin-induced toxicity. Taken together, Hb-activated astrocytes acquired resistance to hemin-induced toxicity via Nrf2/HO-1 pathway. This phenomenon can be considered as the adaptive self-defense in the pathological process of ICH. Hb pre-warned astrocytes and enhanced their capability of handling the coming hemin “flood”. Nrf2/HO-1 may be employed as a target for neuroprotection after ICH. Highlights Hb-pretreatment endowed astrocytes the resistance to hemin-induced toxicity. Hb-pretreatment induced HO-1 expression and prevented hemin-induced ROS production. Hb-pretreatment induced Nrf2 expression and promoted its nuclear translocation. Nrf2 knockdown suppressed Hb-induced upregulation of HO-1 expression. Nrf2 knockdown increased the susceptibility of Hb-pretreated astrocytes to hemin.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  5. [해외논문]   The zinc finger protein CG12744 is essential for differentiation and regeneration after infection in the adult Drosophila midgut   SCI SCIE

    Liu, Qiang (Corresponding author.) , Jin, Li Hua
    Experimental cell research v.361 no.2 ,pp. 225 - 235 , 2017 , 0014-4827 ,

    초록

    Abstract Pluripotent stem cell activity is essential to maintain regeneration and homeostasis in the Drosophila midgut following environmental challenges. Although multiple pathways have been implicated in epithelial renewal, the underlying regulatory mechanisms and correlations between relevant genes and pathways remain elusive. In this study, we show that the zinc finger protein CG12744 plays an important role in the differentiation and regeneration of epithelial cells in response to oral infection with Erwinia carotovora carotovora 15 . Knocking down CG12744 in enteroblasts decreased the post-infection proportion of enteroblasts and enterocytes and increased the post-infection number of enteroendocrine cells. In addition, in precursors, CG12744 affected the Osa , jun-N-terminal kinase and bone morphogenetic protein signaling pathways to control enterocyte differentiation. Finally, CG12744 maintained epithelial architecture and cell fate in enterocytes following an acute infectious challenge. Highlights CG12744 promotes EC differentiation by regulating Osa and JNK levels after infection. CG12744 suppresses EE differentiation after infection. CG12744 regulates the maintenance of epithelial architecture after infection.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  6. [해외논문]   Functional analysis of the cfdp1 gene in zebrafish provides evidence for its crucial role in craniofacial development and osteogenesis   SCI SCIE

    Celauro, Emanuele (Istituto Pasteur Italia Fondazione Cenci-Bolognetti, Dipartimento di Biologia e Biotecnologie ''Charles Darwin'', Sapienza Università) , Carra, Silvia (di Roma, Roma, Italy ) , Rodriguez, Adriana (Dipartimento di Bioscienze, Università) , Cotelli, Franco (degli Studi di Milano, Milano, Italy ) , Dimitri, Patrizio (Institute for Bioengineering of Catalonia, Barcelona, Spain )
    Experimental cell research v.361 no.2 ,pp. 236 - 245 , 2017 , 0014-4827 ,

    초록

    Abstract The CFDP1 proteins have been linked to craniofacial development and osteogenesis in vertebrates, though specific human syndromes have not yet been identified. Alterations of craniofacial development represent the main cause of infant disability and mortality in humans. For this reason, it is crucial to understand the cellular functions and mechanism of action of the CFDP1 protein in model vertebrate organisms. Using a combination of genomic, molecular and cell biology approaches, we have performed a functional analysis of the cfdp1 gene and its encoded protein, zCFDP1 , in the zebrafish model system. We found that zCFDP1 is present in the zygote, is rapidly produced after MTZ transition and is highly abundant in the head structures. Depletion of zCFDP1, induced by an ATG-blocking morpholino, produces considerable defects in craniofacial structures and bone mineralization. Together, our results show that zCFDP1 is an essential protein required for proper development and provide the first experimental evidence showing that in vertebrates it actively participates to the morphogenesis of craniofacial territories. Highlights The zebrafish cfdp1 gene maps to chromosome 8 and is 2222bp long with seven exons and six introns. The cfdp1 gene is highly expressed since very early embryonic stages until the completion of organogenesis. The zebrafish CFDP1 protein is highly abundant in the head structures. CFDP1 is an essential protein that actively participates to the correct definition and morphogenesis of craniofacial territories in the zebrafish model system.

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    회원님의 원문열람 권한에 따라 열람이 불가능 할 수 있으며 권한이 없는 경우 해당 사이트의 정책에 따라 회원가입 및 유료구매가 필요할 수 있습니다.이동하는 사이트에서의 모든 정보이용은 NDSL과 무관합니다.

    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  7. [해외논문]   PPARγ agonist efatutazone and gefitinib synergistically inhibit the proliferation of EGFR-TKI-resistant lung adenocarcinoma cells via the PPARγ/PTEN/Akt pathway   SCI SCIE

    Ni, Jie (Nanjing Medical University Affiliated Cancer Hospital, Department of Clinical Cancer Research Center, Jiangsu Cancer Hospital, Jiangsu Institute of Cancer Research, Nanjing, Jiangsu, China ) , Zhou, Lei-lei (Department of Oncology, Huai'an First People's Hospital, Nanjing Medical University, Huai'an, Jiangsu, China ) , Ding, Li (The Jiangsu Province Research Institute for Clinical Medicine, the First Affiliated Hospital with Nanjing Medical University, Nanjing 210029, China ) , Zhao, Xia (Department of Oncology, Yancheng First People's Hospital, Nanjing Medical University, Yancheng, Jiangsu, China ) , Cao, Haixia (Nanjing Medical University Affiliated Cancer Hospital, Department of Clinical Cancer Research Center, Jiangsu Cancer Hospital, Jiangsu Institute of Cancer Research, Nanjing, Jiangsu, China ) , Fan, Fan (Nanjing Medical University Affiliated Cancer Hospital, Department of Clinical Cancer Research Center, Jiangsu Cancer Hospital, Jiangsu Institute of Cancer Research, Nanjing, Jiangsu, China ) , Li, Huizi (Nanjing Medical University Affiliated Cancer Hospital) , Lou, Rui , Du, Yuanyuan , Dong, Shuchen , Liu, Siwen , Wang, Zhuo , Ma, Rong , Wu, Jianzhong , Feng, Jifeng
    Experimental cell research v.361 no.2 ,pp. 246 - 256 , 2017 , 0014-4827 ,

    초록

    Abstract Development of acquired resistance to EGFR-TKI therapy continues to be a serious clinical problem in Lung adenocarcinoma management. Peroxisome proliferator-activated receptor gamma (PPARγ) agonists demonstrate anti-tumor activity likely via transactivating genes that regulate cell proliferation, differentiation and apoptosis. Efatutazone, a novel later generation PPARγ agonist, selectively activates PPARγ target genes and has antiproliferative effects in a range of malignancies. However, the exact function and molecular mechanism of PPARγ agonists efatutazone in EGFR-TKI gefitinib-resistance of Lung adenocarcinoma has not been determined. In this study, we studied the development of acquired resistance to an EGFR-TKI gefitinib in lung adenocarcinoma cells and investigated the antiproliferative effects of efatutazone in the acquired resistant cells. The treatment of gefitinib-resistant cells with efatutazone reduced the growth of gefitinib-resistant cells in a dose- and time-dependent manner, and facilitated the anti-proliferative effects of gefitinib. Mechanistic investigations suggested that efatutazone acted by upregulating protein expression of PPARγ, phosphatase and tensin homolog (PTEN), inactivating the Akt pathway, followed by dephosphorylation of p21Cip1 at Thr145 without affecting the transcriptional levels. Our results suggested that efatutazone, alone or in combination with gefitinib, might offer therapeutic effects in lung adenocarcinoma. Highlights The low expression of PPARG predicts poor overall survival for patients with lung adenocarcinoma. Treatment with efatutazone and gefitinib produced a synergistic effect on inhibiting proliferation of EGFR-TKI-resistant cells. The PPARγ/PTEN/Akt/p21 signaling pathway might be involved in above synergistic effect. Efatutazone is a potential therapeutic agent for the NSCLC patients who develop acquired resistance to EGFRT-KI.

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    NDSL에서는 해당 원문을 복사서비스하고 있습니다. 아래의 원문복사신청 또는 장바구니담기를 통하여 원문복사서비스 이용이 가능합니다.

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  8. [해외논문]   Inflammation-driven colon neoplasmatogenesis in uPA-deficient mice is associated with an increased expression of Runx transcriptional regulators   SCI SCIE

    Afaloniati, Hara (Laboratory of Biochemistry and Toxicology, School of Veterinary Medicine, Faculty of Health Sciences, Aristotle University of Thessaloniki, Thessaloniki, Greece ) , Karagiannis, George S. (Department of Anatomy & Structural Biology, Albert Einstein College of Medicine, Bronx, NY, United States ) , Hardas, Alexandros (Laboratory of Pathology, School of Veterinary Medicine, Faculty of Health Sciences, Aristotle University of Thessaloniki, Thessaloniki, Greece ) , Poutahidis, Theofilos (Laboratory of Pathology, School of Veterinary Medicine, Faculty of Health Sciences, Aristotle University of Thessaloniki, Thessaloniki, Greece ) , Angelopoulou, Katerina (Laboratory of Biochemistry and Toxicology, School of Veterinary Medicine, Faculty of Health Sciences, Aristotle University of Thessaloniki, Thessaloniki, Greece)
    Experimental cell research v.361 no.2 ,pp. 257 - 264 , 2017 , 0014-4827 ,

    초록

    Abstract Deregulation of the bone morphogenetic protein (BMP) pathway has been documented in colorectal cancer (CRC). Previously, we investigated possible associations between urokinase-type plasminogen activator (uPA) deficiency and expression of extracellular constituents of BMP signaling in a newly developed mouse model of inflammation-driven intestinal neoplasmatogenesis, in which chronic colitis and CRC are induced using dextran sodium sulfate (DSS). In this report, we explored the contribution of intracellular components of Smad-mediated BMP signal transduction using the same model. Interestingly, upon DSS treatment, we noticed an overexpression of Runx1/2/3 transcription factors in both wild-type and uPA-deficient mice. Moreover , Runx1 and Runx2 expression levels exhibited an even higher increase in DSS-treated/uPA-deficient mice as compared to DSS-treated/wild-type animals. In all experimental conditions, in situ investigation of Runx-expressing cell types, revealed detection of all three Runx in the immune cells, yet in the DSS-treated/uPA-deficient mice Runx1 and Runx2 were also identified in the preneoplastic epithelium of advanced high-grade dysplasia and carcinoma in-situ colonic lesions. Finally, the uPA-deficient pro-tumorigenic colitic microenvironment exhibited increased levels of the Runx-induced target genes Snai2 , Bim and Claudin1 , known to have a role in tumor development and progression. These findings suggest that the absence of uPA correlates with increased levels of Runx transcriptional regulators in a way that promotes inflammation-associated carcinogenesis. Highlights Inflammation-induced cancer-prone uPA -/- mouse colon has increased Runx expression. Immune cells and colonic preneoplastic epithelia are major cellular sources of Runx. Runx1/2 in uPA -/- mouse preneoplastic colonic epithelia correlates with cancer risk. Snai2 , Bim and Claudin1 are overexpressed in uPA -/- mouse proneoplastic colitis.

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  9. [해외논문]   VANGL2 interacts with integrin αv to regulate matrix metalloproteinase activity and cell adhesion to the extracellular matrix   SCI SCIE

    Jessen, Tammy N. (Corresponding author.) , Jessen, Jason R.
    Experimental cell research v.361 no.2 ,pp. 265 - 276 , 2017 , 0014-4827 ,

    초록

    Abstract Planar cell polarity (PCP) proteins are implicated in a variety of morphogenetic processes including embryonic cell migration and potentially cancer progression. During zebrafish gastrulation, the transmembrane protein Vang-like 2 (VANGL2) is required for PCP and directed cell migration. These cell behaviors occur in the context of a fibrillar extracellular matrix (ECM). While it is thought that interactions with the ECM regulate cell migration, it is unclear how PCP proteins such as VANGL2 influence these events. Using an in vitro cell culture model system, we previously showed that human VANGL2 negatively regulates membrane type-1 matrix metalloproteinase (MMP14) and activation of secreted matrix metalloproteinase 2 (MMP2). Here, we investigated the functional relationship between VANGL2, integrin αvβ3, and MMP2 activation. We provide evidence that VANGL2 regulates cell surface integrin αvβ3 expression and adhesion to fibronectin, laminin, and vitronectin. Inhibition of MMP14/MMP2 activity suppressed the cell adhesion defect in VANGL2 knockdown cells. Furthermore, our data show that MMP14 and integrin αv are required for increased proteolysis by VANGL2 knockdown cells. Lastly, we have identified integrin αvβ3 as a novel VANGL2 binding partner. Together, these findings begin to dissect the molecular underpinnings of how VANGL2 regulates MMP activity and cell adhesion to the ECM. Highlights VANGL2 regulates cell adhesion to ECM proteins. VANGL2 function influences cell surface integrin αvβ3 expression. Inhibition of MMP activity rescues the adhesion defect in VANGL2 knockdown cells. Integrin αv is required for VANGL2-dependent MMP2 activation. VANGL2 binds integrin αvβ3.

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  10. [해외논문]   Vascular endothelial growth factor mediates ceramide 1-phosphate-stimulated macrophage proliferation   SCI SCIE

    Ouro, Alberto (Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country (UPV/EHU), 48080 Bilbao, Spain ) , Arana, Lide (Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country (UPV/EHU), 48080 Bilbao, Spain ) , Riazy, Maziar (Department of Medicine. University of British Columbia and Vancouver Coastal Health Research Institute, Vancouver, British Columbia, Canada ) , Zhang, Peng (Department of Medicine. University of British Columbia and Vancouver Coastal Health Research Institute, Vancouver, British Columbia, Canada ) , Gomez-Larrauri, Ana (Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country (UPV/EHU), 48080 Bilbao, Spain ) , Steinbrecher, Urs (Department of Medicine. University of British Columbia and Vancouver Coastal Health Research Institute, Vancouver, British Columbia, Canada ) , Duronio, Vincent (Department of Medicine. University of British Columbia and Vancouver Coastal Health Research Institute, Vancouver, Britis) , Gomez-Muñ , oz, Antonio
    Experimental cell research v.361 no.2 ,pp. 277 - 283 , 2017 , 0014-4827 ,

    초록

    Abstract The bioactive sphingolipid ceramide 1-phosphate (C1P) regulates cell division in a variety of cell types including macrophages. However, the mechanisms involved in this action are not completely understood. In the present work we show that C1P stimulates the release of vascular endothelial growth factor (VEGF) in RAW264.7 macrophages, and that this growth factor is essential for stimulation of cell proliferation by C1P. The stimulation of VEGF release was dependent upon activation of the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (PKB-1 also known as Akt-1), and mitogen-activated protein kinase-kinase (MEK)/extracellularly regulated kinase-2 (ERK-2) pathways, as inhibition of these kinases with selective pharmacological inhibitors or with specific gene silencing siRNA, abrogated VEGF release. A key observation was that sequestration of VEGF with a neutralizing antibody, or treatment with VEGF siRNA abolished C1P-stimulated macrophage growth. Also, inhibition of the pathways involved in C1P-stimulated VEGF release inhibited the stimulation of macrophage growth by C1P. Moreover, blockade of VEGF receptor-2 (VEGFR-2), which is the primary receptor for VEGF, with the pharmacological inhibitor DMH4, or with specific VEGFR-2 siRNA, substantially inhibited C1P-stimulated cell growth. It can be concluded that stimulation of VEGF release is a key factor in the promotion of macrophage proliferation by C1P. Highlights C1P promotes macrophage proliferation through stimulation of VEGF secretion. C1P-stimulated VEGF secretion is mediated by the PI3K/Akt-1 and MEK/ERK-2 pathways. Blockade of VEGF receptor-2 inhibited C1P-stimulated macrophage proliferation. Graphical abstract [DISPLAY OMISSION]

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