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We are analyzing https://link.springer.com/article/10.1186/1471-2407-11-443.

Title:
Nck2 promotes human melanoma cell proliferation, migration and invasion in vitro and primary melanoma-derived tumor growth in vivo | BMC Cancer
Description:
Background Nck1 and Nck2 adaptor proteins are involved in signaling pathways mediating proliferation, cytoskeleton organization and integrated stress response. Overexpression of Nck1 in fibroblasts has been shown to be oncogenic. Through the years this concept has been challenged and the consensus is now that overexpression of either Nck cooperates with strong oncogenes to transform cells. Therefore, variations in Nck expression levels in transformed cells could endorse cancer progression. Methods Expression of Nck1 and Nck2 proteins in various cancer cell lines at different stages of progression were analyzed by western blots. We created human primary melanoma cell lines overexpressing GFP-Nck2 and investigated their ability to proliferate along with metastatic characteristics such as migration and invasion. By western blot analysis, we compared levels of proteins phosphorylated on tyrosine as well as cadherins and integrins in human melanoma cells overexpressing or not Nck2. Finally, in mice we assessed tumor growth rate of human melanoma cells expressing increasing levels of Nck2. Results We found that expression of Nck2 is consistently increased in various metastatic cancer cell lines compared with primary counterparts. Particularly, we observed significant higher levels of Nck2 protein and mRNA, as opposed to no change in Nck1, in human metastatic melanoma cell lines compared with non-metastatic melanoma and normal melanocytes. We demonstrated the involvement of Nck2 in proliferation, migration and invasion in human melanoma cells. Moreover, we discovered that Nck2 overexpression in human primary melanoma cells correlates with higher levels of proteins phosphorylated on tyrosine residues, assembly of Nck2-dependent pY-proteins-containing molecular complexes and downregulation of cadherins and integrins. Importantly, we uncovered that injection of Nck2-overexpressing human primary melanoma cells into mice increases melanoma-derived tumor growth rate. Conclusions Collectively, our data indicate that Nck2 effectively influences human melanoma phenotype progression. At the molecular level, we propose that Nck2 in human primary melanoma promotes the formation of molecular complexes regulating proliferation and actin cytoskeleton dynamics by modulating kinases or phosphatases activities that results in increased levels of proteins phosphorylated on tyrosine residues. This study provides new insights regarding cancer progression that could impact on the therapeutic strategies targeting cancer.
Website Age:
28 years and 1 months (reg. 1997-05-29).

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Keywords {🔍}

nck, melanoma, cells, cell, human, pubmed, primary, cancer, article, google, scholar, cas, metastatic, levels, protein, figure, expression, proteins, lines, overexpressing, compared, progression, migration, growth, gfpnck, proliferation, tyrosine, increased, invasion, tumor, specific, gfp, control, mice, actin, central, journal, file, results, metastasis, breast, role, total, antibodies, molecular, signaling, western, research, biol, authors,

Topics {✒️}

org/lab/meenhard-herlyn-dvm-dsc/page/melanoma-cell-lines-metastatic-melanoma-cell-lines n-wasp-arp2/3 complex pathway aude picard-cloutier & louise larose melanoma-derived tumor growth platelet-derived growth factor nck2-dependent py-protein complexes human cancer-related deaths pinch-integrin-linked kinase interaction open access article melanoma skin cancer mesoderm-derived embryonic structures pigment cell research/sponsored cell-ecm contacts mediated article labelle-côt� full size image anti-cancer drug therapy mitogen-activated protein kinase specific p-tyr antibody pre-publication history article download pdf c-src differentially regulates unique c-terminal sh2 potent insulin-mimetic agent bcr-abl kinase regulates human primary melanoma pigment-producing melanocytes localized human primary tumor nck2-dependent py-proteins nck2-dependent py-proteins human primary wm278 melanoma cell lines anti-vinculin specific antibody wm278 cells overexpressing gst-nck fusion proteins primary melanoma cells analyze phospho-tyrosine proteins human metastatic melanoma anti-nck specific antibodies human melanoma cells anti-phosphotyrosine western blot cell-cell adhesion [40] metastatic cell lines melanoma overexpressing nck2 promotes cell motility malignant skin cancers melanoma cell proliferation overexpressing high levels cancer cell lines anti-nck1 specific antibodies melanoma-derived tumors

Schema {🗺️}

WebPage:
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         headline:Nck2 promotes human melanoma cell proliferation, migration and invasion in vitro and primary melanoma-derived tumor growth in vivo
         description:Nck1 and Nck2 adaptor proteins are involved in signaling pathways mediating proliferation, cytoskeleton organization and integrated stress response. Overexpression of Nck1 in fibroblasts has been shown to be oncogenic. Through the years this concept has been challenged and the consensus is now that overexpression of either Nck cooperates with strong oncogenes to transform cells. Therefore, variations in Nck expression levels in transformed cells could endorse cancer progression. Expression of Nck1 and Nck2 proteins in various cancer cell lines at different stages of progression were analyzed by western blots. We created human primary melanoma cell lines overexpressing GFP-Nck2 and investigated their ability to proliferate along with metastatic characteristics such as migration and invasion. By western blot analysis, we compared levels of proteins phosphorylated on tyrosine as well as cadherins and integrins in human melanoma cells overexpressing or not Nck2. Finally, in mice we assessed tumor growth rate of human melanoma cells expressing increasing levels of Nck2. We found that expression of Nck2 is consistently increased in various metastatic cancer cell lines compared with primary counterparts. Particularly, we observed significant higher levels of Nck2 protein and mRNA, as opposed to no change in Nck1, in human metastatic melanoma cell lines compared with non-metastatic melanoma and normal melanocytes. We demonstrated the involvement of Nck2 in proliferation, migration and invasion in human melanoma cells. Moreover, we discovered that Nck2 overexpression in human primary melanoma cells correlates with higher levels of proteins phosphorylated on tyrosine residues, assembly of Nck2-dependent pY-proteins-containing molecular complexes and downregulation of cadherins and integrins. Importantly, we uncovered that injection of Nck2-overexpressing human primary melanoma cells into mice increases melanoma-derived tumor growth rate. Collectively, our data indicate that Nck2 effectively influences human melanoma phenotype progression. At the molecular level, we propose that Nck2 in human primary melanoma promotes the formation of molecular complexes regulating proliferation and actin cytoskeleton dynamics by modulating kinases or phosphatases activities that results in increased levels of proteins phosphorylated on tyrosine residues. This study provides new insights regarding cancer progression that could impact on the therapeutic strategies targeting cancer.
         datePublished:2011-10-12T00:00:00Z
         dateModified:2011-10-12T00:00:00Z
         pageStart:1
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            Melanoma
            Melanoma Cell
            Focal Adhesion Kinase
            Melanoma Cell Line
            Human Melanoma Cell
            Cancer Research
            Oncology
            Surgical Oncology
            Health Promotion and Disease Prevention
            Biomedicine
            general
            Medicine/Public Health
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      headline:Nck2 promotes human melanoma cell proliferation, migration and invasion in vitro and primary melanoma-derived tumor growth in vivo
      description:Nck1 and Nck2 adaptor proteins are involved in signaling pathways mediating proliferation, cytoskeleton organization and integrated stress response. Overexpression of Nck1 in fibroblasts has been shown to be oncogenic. Through the years this concept has been challenged and the consensus is now that overexpression of either Nck cooperates with strong oncogenes to transform cells. Therefore, variations in Nck expression levels in transformed cells could endorse cancer progression. Expression of Nck1 and Nck2 proteins in various cancer cell lines at different stages of progression were analyzed by western blots. We created human primary melanoma cell lines overexpressing GFP-Nck2 and investigated their ability to proliferate along with metastatic characteristics such as migration and invasion. By western blot analysis, we compared levels of proteins phosphorylated on tyrosine as well as cadherins and integrins in human melanoma cells overexpressing or not Nck2. Finally, in mice we assessed tumor growth rate of human melanoma cells expressing increasing levels of Nck2. We found that expression of Nck2 is consistently increased in various metastatic cancer cell lines compared with primary counterparts. Particularly, we observed significant higher levels of Nck2 protein and mRNA, as opposed to no change in Nck1, in human metastatic melanoma cell lines compared with non-metastatic melanoma and normal melanocytes. We demonstrated the involvement of Nck2 in proliferation, migration and invasion in human melanoma cells. Moreover, we discovered that Nck2 overexpression in human primary melanoma cells correlates with higher levels of proteins phosphorylated on tyrosine residues, assembly of Nck2-dependent pY-proteins-containing molecular complexes and downregulation of cadherins and integrins. Importantly, we uncovered that injection of Nck2-overexpressing human primary melanoma cells into mice increases melanoma-derived tumor growth rate. Collectively, our data indicate that Nck2 effectively influences human melanoma phenotype progression. At the molecular level, we propose that Nck2 in human primary melanoma promotes the formation of molecular complexes regulating proliferation and actin cytoskeleton dynamics by modulating kinases or phosphatases activities that results in increased levels of proteins phosphorylated on tyrosine residues. This study provides new insights regarding cancer progression that could impact on the therapeutic strategies targeting cancer.
      datePublished:2011-10-12T00:00:00Z
      dateModified:2011-10-12T00:00:00Z
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      pageEnd:19
      license:https://creativecommons.org/licenses/by/2.0
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      keywords:
         Melanoma
         Melanoma Cell
         Focal Adhesion Kinase
         Melanoma Cell Line
         Human Melanoma Cell
         Cancer Research
         Oncology
         Surgical Oncology
         Health Promotion and Disease Prevention
         Biomedicine
         general
         Medicine/Public Health
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            type:ImageObject
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      author:
            name:Mélissa Labelle-Côté
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                     type:PostalAddress
                  type:Organization
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                     type:PostalAddress
                  type:Organization
            type:Person
            name:Salma Ismaïl
            affiliation:
                  name:McGill University
                  address:
                     name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
                     type:PostalAddress
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                  address:
                     name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
                     type:PostalAddress
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            name:McGill University
            address:
               name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
               type:PostalAddress
            type:Organization
      name:Salma Ismaïl
      affiliation:
            name:McGill University
            address:
               name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
               type:PostalAddress
            type:Organization
      name:Aude Picard-Cloutier
      affiliation:
            name:McGill University
            address:
               name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
               type:PostalAddress
            type:Organization
      name:Peter M Siegel
      affiliation:
            name:McGill University
            address:
               name:Department of Biochemistry and Goodman Cancer Research Centre, McGill University, Montreal, Canada
               type:PostalAddress
            type:Organization
      name:Louise Larose
      affiliation:
            name:McGill University
            address:
               name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Programmes de biologie moléculaire, Faculté de Médecine, Université de Montréal, Montréal, Canada
      name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
      name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
      name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
      name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada
      name:Department of Biochemistry and Goodman Cancer Research Centre, McGill University, Montreal, Canada
      name:Polypeptide Laboratory, Division of Endocrinology, Department of Medicine and Research Institute of the McGill University Health Centre, McGill University, Montreal, Canada

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