Hematopoietic Protein-1 Regulates the Actin Membrane Skeleton and Membrane Stability in Murine Erythrocytes
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{"title"=>"Hematopoietic Protein-1 Regulates the Actin Membrane Skeleton and Membrane Stability in Murine Erythrocytes", "type"=>"journal", "authors"=>[{"first_name"=>"Maia M.", "last_name"=>"Chan", "scopus_author_id"=>"36600019000"}, {"first_name"=>"Jason M.", "last_name"=>"Wooden", "scopus_author_id"=>"7005973693"}, {"first_name"=>"Mark", "last_name"=>"Tsang", "scopus_author_id"=>"8574256900"}, {"first_name"=>"Diana M.", "last_name"=>"Gilligan", "scopus_author_id"=>"35466541100"}, {"first_name"=>"Dinesh K.", "last_name"=>"Hirenallur-S", "scopus_author_id"=>"41161320100"}, {"first_name"=>"Greg L.", "last_name"=>"Finney", "scopus_author_id"=>"16678340100"}, {"first_name"=>"Eric", "last_name"=>"Rynes", "scopus_author_id"=>"22939166600"}, {"first_name"=>"Michael", "last_name"=>"MacCoss", "scopus_author_id"=>"7006289326"}, {"first_name"=>"Julita A.", "last_name"=>"Ramirez", "scopus_author_id"=>"35216079900"}, {"first_name"=>"Heon", "last_name"=>"Park", "scopus_author_id"=>"16162834600"}, {"first_name"=>"Brian M.", "last_name"=>"Iritani", "scopus_author_id"=>"6602963497"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"23424621", "sgr"=>"84873723728", "doi"=>"10.1371/journal.pone.0054902", "scopus"=>"2-s2.0-84873723728", "pui"=>"368331937", "issn"=>"19326203"}, "id"=>"13767c70-3bcc-3202-b988-8c7e7b80565a", "abstract"=>"Hematopoietic protein-1 (Hem-1) is a hematopoietic cell specific member of the WAVE (Wiskott-Aldrich syndrome verprolin-homologous protein) complex, which regulates filamentous actin (F-actin) polymerization in many cell types including immune cells. However, the roles of Hem-1 and the WAVE complex in erythrocyte biology are not known. In this study, we utilized mice lacking Hem-1 expression due to a non-coding point mutation in the Hem1 gene to show that absence of Hem-1 results in microcytic, hypochromic anemia characterized by abnormally shaped erythrocytes with aberrant F-actin foci and decreased lifespan. We find that Hem-1 and members of the associated WAVE complex are normally expressed in wildtype erythrocyte progenitors and mature erythrocytes. Using mass spectrometry and global proteomics, Coomassie staining, and immunoblotting, we find that the absence of Hem-1 results in decreased representation of essential erythrocyte membrane skeletal proteins including α- and β- spectrin, dematin, p55, adducin, ankyrin, tropomodulin 1, band 3, and band 4.1. Hem1⁻/⁻ erythrocytes exhibit increased protein kinase C-dependent phosphorylation of adducin at Ser724, which targets adducin family members for dissociation from spectrin and actin, and subsequent proteolysis. Increased adducin Ser724 phosphorylation in Hem1⁻/⁻ erythrocytes correlates with decreased protein expression of the regulatory subunit of protein phosphatase 2A (PP2A), which is required for PP2A-dependent dephosphorylation of PKC targets. These results reveal a novel, critical role for Hem-1 in the homeostasis of structural proteins required for formation and stability of the actin membrane skeleton in erythrocytes.", "link"=>"http://www.mendeley.com/research/hematopoietic-protein1-regulates-actin-membrane-skeleton-membrane-stability-murine-erythrocytes", "reader_count"=>14, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Researcher"=>3, "Student > Ph. D. Student"=>2, "Student > Postgraduate"=>2, "Student > Master"=>2, "Other"=>1, "Professor"=>1, "Student > Bachelor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Researcher"=>3, "Student > Ph. D. Student"=>2, "Student > Postgraduate"=>2, "Student > Master"=>2, "Other"=>1, "Professor"=>1, "Student > Bachelor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>3, "Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>6, "Medicine and Dentistry"=>1, "Immunology and Microbiology"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>6}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>3}}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/484694", "https://ndownloader.figshare.com/files/484695", "https://ndownloader.figshare.com/files/484697", "https://ndownloader.figshare.com/files/484698", "https://ndownloader.figshare.com/files/484701", "https://ndownloader.figshare.com/files/484703"], "description"=>"<div><p>Hematopoietic protein-1 (Hem-1) is a hematopoietic cell specific member of the WAVE (Wiskott-Aldrich syndrome verprolin-homologous protein) complex, which regulates filamentous actin (F-actin) polymerization in many cell types including immune cells. However, the roles of Hem-1 and the WAVE complex in erythrocyte biology are not known. In this study, we utilized mice lacking Hem-1 expression due to a non-coding point mutation in the <em>Hem1</em> gene to show that absence of Hem-1 results in microcytic, hypochromic anemia characterized by abnormally shaped erythrocytes with aberrant F-actin foci and decreased lifespan. We find that Hem-1 and members of the associated WAVE complex are normally expressed in wildtype erythrocyte progenitors and mature erythrocytes. Using mass spectrometry and global proteomics, Coomassie staining, and immunoblotting, we find that the absence of Hem-1 results in decreased representation of essential erythrocyte membrane skeletal proteins including α- and β- spectrin, dematin, p55, adducin, ankyrin, tropomodulin 1, band 3, and band 4.1. <em>Hem1<sup>−/−</sup></em> erythrocytes exhibit increased protein kinase C-dependent phosphorylation of adducin at Ser724, which targets adducin family members for dissociation from spectrin and actin, and subsequent proteolysis. Increased adducin Ser724 phosphorylation in <em>Hem1<sup>−/−</sup></em> erythrocytes correlates with decreased protein expression of the regulatory subunit of protein phosphatase 2A (PP2A), which is required for PP2A-dependent dephosphorylation of PKC targets. These results reveal a novel, critical role for Hem-1 in the homeostasis of structural proteins required for formation and stability of the actin membrane skeleton in erythrocytes.</p> </div>", "links"=>[], "tags"=>["hematopoietic", "protein-1", "regulates", "actin", "membrane", "skeleton", "murine", "erythrocytes"], "article_id"=>156544, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0054902.s001", "https://dx.doi.org/10.1371/journal.pone.0054902.s002", "https://dx.doi.org/10.1371/journal.pone.0054902.s003", "https://dx.doi.org/10.1371/journal.pone.0054902.s004", "https://dx.doi.org/10.1371/journal.pone.0054902.s005", "https://dx.doi.org/10.1371/journal.pone.0054902.s006"], "stats"=>{"downloads"=>0, "page_views"=>43, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Hematopoietic_Protein_1_Regulates_the_Actin_Membrane_Skeleton_and_Membrane_Stability_in_Murine_Erythrocytes__/156544", "title"=>"Hematopoietic Protein-1 Regulates the Actin Membrane Skeleton and Membrane Stability in Murine Erythrocytes", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-02-12 01:49:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/490353"], "description"=>"<p>Flow cytometric analyses of splenocytes from <i>Hem1<sup>−/−</sup></i> vs. wildtype (wt) littermate control mice. (A) Live-gated, Ter119<sup>+</sup> cells (left panels) are shown plotted by cell-surface display of CD44 vs. Ter119<sup>+</sup> (middle panels) or CD44 vs forward scatter (right panels). Gates defining different erythroid progenitor populations (I-V) are shown. (B) (<i>left</i>) Erythroid progenitor populations are shown as percent of Ter119<sup>+</sup> cells. Bars represent mean +/− SEM for three animals per genotype. The asterisks indicate statistical significance: (*), <i>p</i><0.01; (**), <i>p</i><0.001. (<i>right</i>) <i>Hem1<sup>−/−</sup></i> erythroblasts have normal morphology. Shown are representative photos of WT and <i>Hem1<sup>−/−</sup></i> erythroblasts.</p>", "links"=>[], "tags"=>["hem1", "impair"], "article_id"=>160866, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.g002", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Loss_of_Hem1_does_not_impair_erythropoiesis_/160866", "title"=>"Loss of Hem1 does not impair erythropoiesis.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-12 00:14:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/490985"], "description"=>"<p>SDS-PAGE analysis of purified erythrocyte ghosts was used to evaluate relative levels of erythrocyte membrane skeletal proteins between WT and <i>Hem1<sup>−/−</sup></i> mice. (A) Coomassie-stained polyacrylamide gel (representative of 6 animals per genotype). Lanes contain equivalent amounts of total protein. β-actin immunoblot is shown below. (B) Immunoblots of erythrocyte membrane ghosts from purified WT and <i>Hem1<sup>−/−</sup></i> erythrocytes, loaded according to total protein and equivalent β-actin. Each pair is representative of results for at least 5 individuals of each genotype. (C) Activation of PKC results in increased phosphorylation of adducin on Serine 724. Purified WT and <i>Hem1<sup>−/−</sup></i> erythrocytes were stimulated with the phorbol ester PMA (20 ng/ml) and were harvested and lysed at the indicated timepoints post-stimulation. A representative immunoblot of three separate experiments is shown (3 animals per genotype). (D) Erythrocyte ghosts from <i>Hem1<sup>−/−</sup></i> mice contain increased PP2A catalytic subunit (PP2Ac) and decreased PP2A regulatory subunit (PP2Ar) protein relative to WT erythrocytes. Shown are total protein levels determined by immunoblot. Numbers below each scan represent relative protein expression levels in <i>Hem1<sup>−/−</sup></i> versus WT samples. Samples were loaded according to levels of total protein. (E) WT and <i>Hem1<sup>−/−</sup></i> erythroblasts were stimulated in Okadaic acid (OA) and were harvested and lysed at the indicated timepoints post-stimulation. A representative immunoblot of 3 separate experiments is shown. Samples were loaded based on equivalent cell number.</p>", "links"=>[], "tags"=>["erythrocytes", "phospho-adducin", "levels", "membrane", "skeletal"], "article_id"=>161492, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.g005", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Hem1_8722_8722_erythrocytes_contain_increased_phospho_adducin_and_decreased_levels_of_essential_membrane_skeletal_proteins_/161492", "title"=>"<i>Hem1<sup>−/−</sup></i> erythrocytes contain increased phospho-adducin and decreased levels of essential membrane skeletal proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-12 00:24:52"}
  • {"files"=>["https://ndownloader.figshare.com/files/491360"], "description"=>"<p>(<i>top</i>) The red cell membrane in WT mice consists of a lipid bilayer embedded with two main complexes of structural proteins: The ankyrin complex and the junctional complex (also known as the 4.1R complex), which are connected by horizontal flexible helices of α- and β- spectrin heterodimers and tetramers. Stability of the complexes is regulated in part by phosphorylation of adducin (on Serine 724 in mice) by protein kinase C (PKC), which leads to decreased F-actin capping and dissociation of spectrin from actin. Since PKC-mediated serine phosphorylation is typically opposed by protein phosphatase 2A (PP2A), we propose that PP2A dephosphorylates adducin. PP2A, PKC (bottom), and Hem-1 (top) have all been shown to associate with Rac1. Loss of Hem-1 results in decreased PP2a regulatory subunit B (PP2Ar) and structural subunit A protein expression and increased PKC-mediated phosphorylation of Ser724 on adducin (bottom). Phospho-adducin is then degraded, resulting in the dissociation of spectrin from actin and decreased stability of junctional complex proteins and the membrane cytoskeleton. GPA (Glycophorin A), GPC (Glycophorin C), PP2Ac (protein phosphatase 2A catalytic subunit), PP2Ar (protein phosphatase 2A regulatory subunit).</p>", "links"=>[], "tags"=>["erythrocyte", "membrane", "cytoskeleton", "wildtype", "hem-1", "null"], "article_id"=>161870, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.g007", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_of_the_erythrocyte_membrane_cytoskeleton_in_wildtype_and_Hem_1_null_mice_/161870", "title"=>"Model of the erythrocyte membrane cytoskeleton in wildtype and Hem-1 null mice.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-12 00:31:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/491154"], "description"=>"<p>Purified WT (open diamonds, <i>n</i> = 4 mice) and <i>Hem1<sup>−/−</sup></i> (filled triangles, <i>n</i> = 3 mice) erythrocytes (5×10<sup>8</sup> per mouse) were labeled with CFSE dye and transfused via retro-orbital injection into <i>Rag2<sup>−/−</sup>γ<sub>c</sub><sup>−/−</sup></i> host mice. Host mice were tail bled starting Day 1 post-transfusion and samples were analyzed via flow cytometry to determine the percentage of CFSE-labeled erythrocytes. Percent CFSE labeled cells remaining post transfusion were determined relative to Day 1 (100% labeling). <i>P</i>-values are noted above each time-point.</p>", "links"=>[], "tags"=>["transfused", "erythrocytes", "compared", "wt"], "article_id"=>161666, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.g006", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Lifespan_of_transfused_Hem1_8722_8722_erythrocytes_is_decreased_compared_to_transfused_WT_erythrocytes_/161666", "title"=>"Lifespan of transfused <i>Hem1<sup>−/−</sup></i> erythrocytes is decreased compared to transfused WT erythrocytes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-12 00:27:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/490118"], "description"=>"<p>(A) Peripheral blood smears from (i) WT and (ii) <i>Hem1<sup>−/−</sup></i> mice were stained with Wright-Giemsa stain. Shown are representative blood smears (approximately 20 individuals per genotype). Note poikilocytosis, polychromasia, hypochromia, and anisocytosis of <i>Hem1<sup>−/−</sup></i> erythrocytes as well as the increased presence of acanthocytes, schistocytes, dacryocytes, and keratocytes. Original magnification ×600. (B) Confocal microscopy images of WT and <i>Hem1<sup>−/−</sup></i> erythrocytes stained for actin (Actin), β-spectrin (Spectrin), and combined (Merge). Representative of 5 animals per genotype. Note decreased membrane actin and spectrin, and increased areas of aggregated actin in <i>Hem1<sup>−/−</sup></i> versus WT erythrocytes (yellow arrows), many of which co-localize at the periphery with β-spectrin. Most <i>Hem1<sup>−/−</sup></i> erythrocytes (identified by biconcave shape) contain actin foci, as noted through multiple cross sections. No WT erythrocytes were identified with actin foci. A single layer is shown. Alexa Fluor 488 phalloidin stain and anti-β-spectrin labeled with Alexa Fluor 568 are shown, original magnification ×1000.</p>", "links"=>[], "tags"=>["erythrocytes", "morphologically", "abnormal", "condensed", "f-actin"], "article_id"=>160625, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.g001", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Hem1_8722_8722_erythrocytes_are_morphologically_abnormal_and_contain_condensed_F_actin_foci_/160625", "title"=>"<i>Hem1<sup>−/−</sup></i> erythrocytes are morphologically abnormal and contain condensed F-actin foci.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-12 00:10:25"}
  • {"files"=>["https://ndownloader.figshare.com/files/491487"], "description"=>"<p><i>n</i> = 2 WT mice (4 technical replicates) and 2 <i>Hem1<sup>−/−</sup></i> mice (4 technical replicates).</p>*<p>Fold difference in <i>Hem1<sup>−/−</sup></i> vs WT erythrocytes. <i>p = </i>0.05.</p>", "links"=>[], "tags"=>["differences", "soluble", "fractions", "proteomics", "wt"], "article_id"=>161998, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.t002", "stats"=>{"downloads"=>0, "page_views"=>32, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Protein_differences_identified_in_soluble_fractions_via_proteomics_in_Hem1_8722_8722_versus_Wt_erythrocytes_/161998", "title"=>"Protein differences identified in soluble fractions via proteomics in <i>Hem1<sup>−/−</sup></i> versus Wt erythrocytes.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-12 00:33:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/490759"], "description"=>"<p>(A) Chromatographic alignments of replicate runs for WT and <i>Hem1<sup>−/−</sup></i> erythrocytes. Alignments of 5 WT (positive inflection line) and 8 <i>Hem1<sup>−/−</sup></i> (negative inflection line) erythrocyte technical replicate µLC-MS runs are shown in a base peak plot (ion intensity vs. retention time). Individual replicates are shown in distinct colors for each genotype. (B) CRAWDAD detection of chromatographic difference regions for 55 kDa erythrocyte membrane protein peptide TAELSPFIVFIAPTDQGTQTEALQQLQK (i), actin peptide SYELPDGQVITIGNER (ii), ankyrin 1 peptide AGKEPSLWAPESA (iii), band 3 peptide YLPSPAKPDPNLYN (iv), band 4.1 peptide LIDRPAPHFER (v), band 4.2 peptide AAQYRPLTVSVR (vi), dematin peptide STSPPPSPEVWAESR (vii), glycophorin A peptide GDNSVPLSSIEQTPNEESSNV (viii), spectrin alpha peptide AEQVDGVINLGNSLIER (ix), spectrin beta peptide FAALEKPTTLELK (x), and tropomodulin 1 peptide LADLTGPIIPK (xi). Aligned replicate µLC-MS runs from the WT and <i>Hem1</i><sup>−/−</sup> erythrocyte series are shown in blue and red, respectively. Mean intensity values are shown in solid lines and ±1 SD in dashed lines. Difference regions for each peptide indicated with arrows.</p>", "links"=>[], "tags"=>["erythrocytes", "differential", "membrane", "proteins", "revealed"], "article_id"=>161273, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.g004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_WT_and_Hem1_8722_8722_erythrocytes_show_differential_expression_of_key_membrane_and_structural_proteins_as_revealed_by_proteomics_/161273", "title"=>"WT and <i>Hem1<sup>−/−</sup></i> erythrocytes show differential expression of key membrane and structural proteins as revealed by proteomics.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-12 00:21:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/491533"], "description"=>"<p><i>n</i> = 2 WT mice (5 technical replicates) and 3 <i>Hem1<sup>−/−</sup></i> mice (8 technical replicates).</p>*<p>Fold difference in <i>Hem1<sup>−/−</sup></i> versus WT erythrocytes. <i>p</i>≤0.05.</p>", "links"=>[], "tags"=>["differences", "insoluble", "proteomics", "wt"], "article_id"=>162040, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.t001", "stats"=>{"downloads"=>0, "page_views"=>35, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Protein_differences_identified_in_insoluble_fraction_via_proteomics_in_WT_and_Hem1_8722_8722_erythrocytes_/162040", "title"=>"Protein differences identified in insoluble fraction via proteomics in WT and <i>Hem1<sup>−/−</sup></i> erythrocytes.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-12 00:34:00"}
  • {"files"=>["https://ndownloader.figshare.com/files/490622"], "description"=>"<p>(A) (<i>Left</i>) Real-time PCR of FAC-sorted erythroblasts from WT mice shows relative expression of <i>Hem1</i> and WAVE complex (<i>Abi1, Abi2, Sra1</i>, and <i>Wave2</i>) mRNA normalized to <i>β-actin</i>. Expression of <i>Hem1</i> mRNA is shown relative to kidney mRNA. Expression of WAVE component mRNAs are shown relative to a C<sub>T</sub> value of 38, which represents an arbitrary low expressing tissue. (*), <i>p</i><0.0007; (**), <i>p</i><0.0004; (***), <i>p</i><0.0001. <i>n</i> = 3 mice per genotype. (<i>Right</i>) Expression of WAVE complex mRNA are shown in Hem1 erythroblasts versus WT erythroblasts. <i>Abi2 p<0.0004</i> (B) Immunoblots of purified erythrocyte ghosts from WT and <i>Hem1<sup>−/−</sup></i> mice, loaded according to equivalent levels of β-actin. Each lane is representative of at least 3 individuals per genotype. Hem-1 protein (upper band, 110 kDa) is not detectable in erythrocyte ghosts from <i>Hem1<sup>−/−</sup></i> mice. Although <i>Abi2</i> mRNA levels are reduced in <i>Hem1<sup>−/−</sup></i> erythrocytes, Abi2 protein levels are relatively normal, likely due to post-transcriptional and/or post-translational regulation. Numbers below each scan represent protein expression levels in <i>Hem1<sup>−/−</sup></i> relative to WT samples. Samples were loaded based on equivalent total protein.</p>", "links"=>[], "tags"=>["mrna", "wildtype"], "article_id"=>161139, "categories"=>["Biochemistry", "Cell Biology", "Hematology"], "users"=>["Maia M. Chan", "Jason M. Wooden", "Mark Tsang", "Diana M. Gilligan", "Dinesh K. Hirenallur-S", "Greg L. Finney", "Eric Rynes", "Michael MacCoss", "Julita A. Ramirez", "Heon Park", "Brian M. Iritani"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0054902.g003", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_WAVE_complex_mRNA_and_protein_in_wildtype_WT_and_Hem1_8722_8722_mouse_erythrocytes_/161139", "title"=>"Expression of WAVE complex mRNA and protein in wildtype (WT) and <i>Hem1<sup>−/−</sup></i> mouse erythrocytes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-12 00:18:59"}

PMC Usage Stats | Further Information

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Relative Metric

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