Cell Proliferation and Migration Are Modulated by Cdk-1-Phosphorylated Endothelial-Monocyte Activating Polypeptide II
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{"title"=>"Cell proliferation and migration are modulated by Cdk-1-phosphorylated Endothelial-Monocyte Activating Polypeptide II", "type"=>"journal", "authors"=>[{"first_name"=>"Margaret A.", "last_name"=>"Schwarz", "scopus_author_id"=>"35431114000"}, {"first_name"=>"Janet", "last_name"=>"Thornton", "scopus_author_id"=>"7402781853"}, {"first_name"=>"Haiming", "last_name"=>"Xu", "scopus_author_id"=>"57198604029"}, {"first_name"=>"Niranjan", "last_name"=>"Awasthi", "scopus_author_id"=>"6602424393"}, {"first_name"=>"Roderich E.", "last_name"=>"Schwarz", "scopus_author_id"=>"35600206700"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"22412987", "sgr"=>"84863268634", "doi"=>"10.1371/journal.pone.0033101", "scopus"=>"2-s2.0-84863268634", "pui"=>"364386620", "issn"=>"19326203"}, "id"=>"08dc0e29-386a-398d-a571-6fde3e71835a", "abstract"=>"BACKGROUND: Endothelial-Monocyte Activating Polypeptide (EMAP II) is a secreted protein with well-established anti-angiogenic activities. Intracellular EMAP II expression is increased during fetal development at epithelial/mesenchymal boundaries and in pathophysiologic fibroproliferative cells of bronchopulmonary dysplasia, emphysema, and scar fibroblast tissue following myocardial ischemia. Precise function and regulation of intracellular EMAP II, however, has not been explored to date.\\n\\nMETHODOLOGY/PRINCIPAL FINDINGS: Here we show that high intracellular EMAP II suppresses cellular proliferation by slowing progression through the G2M cell cycle transition in epithelium and fibroblast. Furthermore, EMAP II binds to and is phosphorylated by Cdk1, and exhibits nuclear/cytoplasmic partitioning, with only nuclear EMAP II being phosphorylated. We observed that extracellular secreted EMAP II induces endothelial cell apoptosis, where as excess intracellular EMAP II facilitates epithelial and fibroblast cells migration.\\n\\nCONCLUSIONS/SIGNIFICANCE: Our findings suggest that EMAP II has specific intracellular effects, and that this intracellular function appears to antagonize its extracellular anti-angiogenic effects during fetal development and pulmonary disease progression.", "link"=>"http://www.mendeley.com/research/cell-proliferation-migration-modulated-cdk1phosphorylated-endothelialmonocyte-activating-polypeptide", "reader_count"=>8, "reader_count_by_academic_status"=>{"Researcher"=>3, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>1, "Student > Master"=>1, "Professor"=>2}, "reader_count_by_user_role"=>{"Researcher"=>3, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>1, "Student > Master"=>1, "Professor"=>2}, "reader_count_by_subject_area"=>{"Engineering"=>1, "Biochemistry, Genetics and Molecular Biology"=>1, "Agricultural and Biological Sciences"=>2, "Medicine and Dentistry"=>3, "Unspecified"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"United States"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/670374"], "description"=>"<p>EMAP II translation and transcription were examined in chemically synchronized cells throughout the phases of cell cycle. Western blot analysis indicated that upon exiting G0, EMAP II protein was increased throughout cell cycle and was phosphorylated at G2M (A,B). EMAP II transcription was minimally impacted during the different phases of cell cycle (C,D) (these experiments were performed a minimum of 4 times).</p>", "links"=>[], "tags"=>["ii", "phosphorylated", "g2m"], "article_id"=>340865, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101.g003", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_EMAP_II_is_phosphorylated_at_G2M_phase_of_cell_cycle_/340865", "title"=>"EMAP II is phosphorylated at G2M phase of cell cycle.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 00:14:25"}
  • {"files"=>["https://ndownloader.figshare.com/files/670703"], "description"=>"<p>Two potential Cdk1 phosphorylation sites were identified, aa 84 threonine, and serine at aa 232 (A). Using recombinant EMAP II protein isolates (B) in a Cdk1 assay, only the N-terminal and full-length EMAP II were phosphorylated by Cdk1 (C). Point mutation within the threonine (aa 84) to change the amino acid to either asparagine or alanine eliminated Cdk1 phosphorylation, thus confirming that the 84 aa threonine was the site of Cdk1 phosphorylation of EMAP II (D) (these experiments were performed 3 times).</p>", "links"=>[], "tags"=>["phosphorylates", "emap", "ii", "amino"], "article_id"=>341187, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101.g006", "stats"=>{"downloads"=>0, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cdk1_phosphorylates_EMAP_II_at_amino_acid_84_threonine_/341187", "title"=>"Cdk1 phosphorylates EMAP II at amino acid 84, threonine.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 00:19:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/670286"], "description"=>"<p>Confluent cells were wounded using a rubber policeman, wounding site marked, and examined for migration 15 hours post wounding. The black line represents the wounded margin. Cells overexpressing pFEII-GFP (B,C) had a marked increase in migration as compared empty vector control (pEGFP-N3, A,C) (p<0.0001) (n = 9 in triplicate performed on 3 different occasions).</p>", "links"=>[], "tags"=>["emap", "ii", "increases"], "article_id"=>340774, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101.g002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overexpression_of_EMAP_II_increases_cell_migration_/340774", "title"=>"Overexpression of EMAP II increases cell migration.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 00:12:54"}
  • {"files"=>["https://ndownloader.figshare.com/files/670158"], "description"=>"<p>Cell doubling, proliferation and progression through cell cycle were examined in clonal A549 cell populations overexpressing either EMAP II (pFEII-GFP) or GFP (pEGFP-N3). Western analysis of cell lysates using either EMAP II (A) or GFP (B) antibody confirmed expression. EMAP II overexpressing cells were found to have a marked delay in cell doubling (C, p<0.05), growth rate (D, p<0.001), and a delay in exiting the G2M phase of cell cycle as noted at 14 and 15 hours post synchronized cell release (*, E) as compared to the empty vector control (pEGFP-N3) (these experiments were performed a minimum of 4 times).</p>", "links"=>[], "tags"=>["ii", "overexpression", "delays"], "article_id"=>340648, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_EMAP_II_overexpression_delays_cell_proliferation_/340648", "title"=>"EMAP II overexpression delays cell proliferation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 00:10:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/670620"], "description"=>"<p>A Cdk1 binding domain, TPLH, was identified in EMAP II's N-terminal region at aa 84–87 (A). Immunoprecipitation using Cdk1 determined that EMAP II binds to Cdk1 during S and G2M phase of cell cycle (B) (these experiments were performed 4 times).</p>", "links"=>[], "tags"=>["ii", "contains", "cdk1", "binding", "immuno-precipitates", "g2m", "phases"], "article_id"=>341107, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101.g005", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_EMAP_II_contains_a_Cdk1_binding_site_and_immuno_precipitates_with_Cdk1_during_S_and_G2M_phases_of_cell_cycle_/341107", "title"=>"EMAP II contains a Cdk1 binding site and immuno-precipitates with Cdk1 during S and G2M phases of cell cycle.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 00:18:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/670528"], "description"=>"<p>EMAP II distribution was assessed in chemically synchronized cell populations. Immunofluoresence indicated EMAP II expression is predominately nuclear in G0 (A,B) and S (C,D) phase, whereas in G2M (E/F) nuclear EMAP II is reduced. Western blot analysis (G) of isolated nuclear and cytoplasmic fractions indicates EMAP II expression is maintained in both compartments through out cell cycle (these experiments were performed 4 times). PSORT II analysis determined there were three classical types of nuclear localizing sequences (NLS): pat4, pat7, and a bipartite NLS (H). Proteins K and R composition predicts that 87% of EMAP II is subcompartmentalization to the nucleus EMAP II's (I). Magnification in A–F: 1000×.</p>", "links"=>[], "tags"=>["ii", "undergoes", "partitioning"], "article_id"=>341012, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101.g004", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_EMAP_II_undergoes_nuclear_cytoplasmic_partitioning_during_cell_cycle_/341012", "title"=>"EMAP II undergoes nuclear/cytoplasmic partitioning during cell cycle.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 00:16:52"}
  • {"files"=>["https://ndownloader.figshare.com/files/670785"], "description"=>"<p>A phosphorylated pThr84-EMAP II antibody was obtained (A) and phospo-EMAP II was examined in nuclear and cytoplasmic fractions during cell cycle. Phospho-EMAP II was found in the nuclear fraction G0-S phase of cell cycle with only the phosphorylated form found in the cytoplasm during G2M. Unphosphorylated EMAP II (capable of recognizing unphosphorylated and phosphorylated EMAP II) was confined to the cytoplasm as only a single band corresponding with the phosphorylated form was found in the nuclear isolates (B). Lamin B nuclear envelope confirmed nuclear isolate specificity (these experiments were performed a minimum of 4 times).</p>", "links"=>[], "tags"=>["emap", "ii", "predominately", "localized"], "article_id"=>341274, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101.g007", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phosphorylated_EMAP_II_is_predominately_localized_in_the_nuclear_fraction_/341274", "title"=>"Phosphorylated EMAP II is predominately localized in the nuclear fraction.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 00:21:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/343004"], "description"=>"<div><h3>Background</h3><p>Endothelial-Monocyte Activating Polypeptide (EMAP II) is a secreted protein with well-established anti-angiogenic activities. Intracellular EMAP II expression is increased during fetal development at epithelial/mesenchymal boundaries and in pathophysiologic fibroproliferative cells of bronchopulmonary dysplasia, emphysema, and scar fibroblast tissue following myocardial ischemia. Precise function and regulation of intracellular EMAP II, however, has not been explored to date.</p> <h3>Methodology/Principal Findings</h3><p>Here we show that high intracellular EMAP II suppresses cellular proliferation by slowing progression through the G2M cell cycle transition in epithelium and fibroblast. Furthermore, EMAP II binds to and is phosphorylated by Cdk1, and exhibits nuclear/cytoplasmic partitioning, with only nuclear EMAP II being phosphorylated. We observed that extracellular secreted EMAP II induces endothelial cell apoptosis, where as excess intracellular EMAP II facilitates epithelial and fibroblast cells migration.</p> <h3>Conclusions/Significance</h3><p>Our findings suggest that EMAP II has specific intracellular effects, and that this intracellular function appears to antagonize its extracellular anti-angiogenic effects during fetal development and pulmonary disease progression.</p> </div>", "links"=>[], "tags"=>["proliferation", "are", "modulated", "cdk-1-phosphorylated", "endothelial-monocyte", "activating", "polypeptide", "ii"], "article_id"=>127806, "categories"=>["Cell Biology", "Developmental Biology"], "users"=>["Margaret A. Schwarz", "Janet Thornton", "Haiming Xu", "Niranjan Awasthi", "Roderich E. Schwarz"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0033101", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Cell_Proliferation_and_Migration_Are_Modulated_by_Cdk_1_Phosphorylated_Endothelial_Monocyte_Activating_Polypeptide_II/127806", "title"=>"Cell Proliferation and Migration Are Modulated by Cdk-1-Phosphorylated Endothelial-Monocyte Activating Polypeptide II", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-03-08 02:10:06"}

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Relative Metric

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