Inhibition of TTR Aggregation-Induced Cell Death – A New Role for Serum Amyloid P Component
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{"title"=>"Inhibition of TTR Aggregation-Induced Cell Death - A New Role for Serum Amyloid P Component", "type"=>"journal", "authors"=>[{"first_name"=>"Karin", "last_name"=>"Andersson", "scopus_author_id"=>"57197044793"}, {"first_name"=>"Malgorzata", "last_name"=>"Pokrzywa", "scopus_author_id"=>"18936671600"}, {"first_name"=>"Ingrid", "last_name"=>"Dacklin", "scopus_author_id"=>"7801457291"}, {"first_name"=>"Erik", "last_name"=>"Lundgren", "scopus_author_id"=>"7102011789"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"368294485", "sgr"=>"84873493924", "issn"=>"19326203", "pmid"=>"23390551", "scopus"=>"2-s2.0-84873493924", "doi"=>"10.1371/journal.pone.0055766"}, "id"=>"0e2a709d-2693-3c17-ba91-3fd37c4c5973", "abstract"=>"Serum amyloid P component (SAP) is a glycoprotein that is universally found associated with different types of amyloid deposits. It has been suggested that it stabilizes amyloid fibrils and therefore protects them from proteolytic degradation.", "link"=>"http://www.mendeley.com/research/inhibition-ttr-aggregationinduced-cell-death-new-role-serum-amyloid-p-component", "reader_count"=>5, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>2, "Student > Postgraduate"=>1, "Student > Master"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>2, "Student > Postgraduate"=>1, "Student > Master"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Agricultural and Biological Sciences"=>2, "Neuroscience"=>1, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>2}, "Unspecified"=>{"Unspecified"=>1}}, "group_count"=>0}

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  • {"files"=>["https://ndownloader.figshare.com/files/482338", "https://ndownloader.figshare.com/files/482339", "https://ndownloader.figshare.com/files/482342"], "description"=>"<div><h3>Background</h3><p>Serum amyloid P component (SAP) is a glycoprotein that is universally found associated with different types of amyloid deposits. It has been suggested that it stabilizes amyloid fibrils and therefore protects them from proteolytic degradation.</p> <h3>Methodology/Principal Findings</h3><p>In this paper, we show that SAP binds not only to mature amyloid fibrils but also to early aggregates of amyloidogenic mutants of the plasma protein transthyretin (TTR). It does not inhibit fibril formation of TTR mutants, which spontaneously form amyloid <em>in vitro</em> at physiological pH. We found that SAP prevents cell death induced by mutant TTR, while several other molecules that are also known to decorate amyloid fibrils do not have such effect. Using a <em>Drosophila</em> model for TTR-associated amyloidosis, we found a new role for SAP as a protective factor in inhibition of TTR-induced toxicity. Overexpression of mutated TTR leads to a neurological phenotype with changes in wing posture. SAP-transgenic flies were crossed with mutated TTR-expressing flies and the results clearly confirmed a protective effect of SAP on TTR-induced phenotype, with an almost complete reduction in abnormal wing posture. Furthermore, we found <em>in vivo</em> that binding of SAP to mutated TTR counteracts the otherwise detrimental effects of aggregation of amyloidogenic TTR on retinal structure.</p> <h3>Conclusions/Significance</h3><p>Together, these two approaches firmly establish the protective effect of SAP on TTR-induced cell death and degenerative phenotypes, and suggest a novel role for SAP through which the toxicity of early amyloidogenic aggregates is attenuated.</p> </div>", "links"=>[], "tags"=>["inhibition", "ttr", "aggregation-induced", "serum", "amyloid", "component"], "article_id"=>155769, "categories"=>["Biotechnology", "Neuroscience", "Cell Biology", "Genetics"], "users"=>["Karin Andersson", "Malgorzata Pokrzywa", "Ingrid Dacklin", "Erik Lundgren"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055766.s001", "https://dx.doi.org/10.1371/journal.pone.0055766.s002", "https://dx.doi.org/10.1371/journal.pone.0055766.s003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Inhibition_of_TTR_Aggregation_Induced_Cell_Death_A_New_Role_for_Serum_Amyloid_P_Component__/155769", "title"=>"Inhibition of TTR Aggregation-Induced Cell Death – A New Role for Serum Amyloid P Component", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-02-04 01:36:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/495863"], "description"=>"<p><i>(A)</i> SAP was co-incubated with pre-aggregated TTR under physiological conditions. The complexes were immunoprecipitated with a SAP-specific antibody (DAKO) and the presence of TTR was detected on immunoblots using a polyclonal anti-TTR antibody (DAKO). SAP bound to pre-fibrillar aggregates of TTR-D and TTR-A, and the precipitates were found in the pellet fraction (left panel), whereas TTR wt and TTR V30M were found unbound in the supernatants (right panel). Bands: 16 kDa–monomer; 36 kDa–dimer. <i>(B)</i> SDS-PAGE analysis of TTR variants. Immunoblot shows that the TTR-A mutant is sensitive to SDS and easily dissociates into monomers in contrast to TTRwt or TTRV30M that keep the dimers intact. (<i>C</i>) Effect of SAP on aggregation of TTR. The TTR-A mutant was aggregated at 37°C for 0–5 days in the presence (+) or absence (−) of 3 µM SAP and subjected to immunoblotting under native conditions. TTR was detected with a TTR-specific antibody. SAP did not affect the aggregation kinetics of the TTR-A mutant, since the migration pattern of TTR-A in the gel decreased with time as the protein formed higher-molecular-weight aggregates–and was identical irrespective of whether or not SAP was present. After 5 days, the TTR-A formed aggregates that did not enter the separation gel.</p>", "links"=>[], "tags"=>["binds", "pre-fibrillar", "aggregates", "ttr"], "article_id"=>166382, "categories"=>["Biotechnology", "Neuroscience", "Cell Biology", "Genetics"], "users"=>["Karin Andersson", "Malgorzata Pokrzywa", "Ingrid Dacklin", "Erik Lundgren"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055766.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SAP_binds_to_pre_fibrillar_aggregates_of_TTR_in_vitro_/166382", "title"=>"SAP binds to pre-fibrillar aggregates of TTR <i>in vitro</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-04 01:46:22"}
  • {"files"=>["https://ndownloader.figshare.com/files/495953"], "description"=>"<p><i>(A)</i> The effect of SAP on TTR-induced toxicity. IMR-32 cells were incubated with the indicated concentrations of either TTR-A (▴) or TTR-D (•) for 12 h. Solid lines represent the toxic response when cells were incubated with the respective proteins, and dashed lines represent experiments with the addition of 3 µM SAP. One-way ANOVA with sequential Bonferroni <i>post-hoc</i> test revealed significant protective effects of SAP on cells in the presence of either TTR-A or TTR-D (<i>P = </i>0.004 and <i>P = </i>0.003, respectively) <i>(B)</i> The effect of SAP on H<sub>2</sub>O<sub>2</sub>-induced cytotoxicity. IMR-32 cells were treated with different concentrations of H<sub>2</sub>O<sub>2</sub> (in the range 0–5 mM) without addition of (▪) or in the presence of 1,000 U/ml catalase (▴) or 3 µM SAP (•). Oxidative stress-induced toxicity in IMR-32 cells was significantly reduced by catalase treatment (<i>P</i><0.001; one-way ANOVA, sequential Bonferroni <i>post-hoc</i> test) but not by SAP treatment (<i>P = </i>0.4). Error bars indicate SD.</p>", "links"=>[], "tags"=>["sap", "amyloidogenic"], "article_id"=>166477, "categories"=>["Biotechnology", "Neuroscience", "Cell Biology", "Genetics"], "users"=>["Karin Andersson", "Malgorzata Pokrzywa", "Ingrid Dacklin", "Erik Lundgren"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055766.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effects_of_SAP_on_amyloidogenic_aggregates_/166477", "title"=>"Effects of SAP on amyloidogenic aggregates.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-04 01:47:57"}
  • {"files"=>["https://ndownloader.figshare.com/files/496027"], "description"=>"<p><i>(A)</i> TUNEL staining of cells treated with amyloid protofibrils in the presence of SAP. IMR-32 cells were exposed to 20 µM TTR-A (upper row) or 20 µM TTR-D (lower row). The apoptotic response of the cells incubated with the amyloidogenic aggregates was assessed by TUNEL in the absence of SAP (left panel) or in the presence of either 1.5 µM SAP (middle panel) or 3 µM SAP (right panel). The inserts show the total amount of seeded cells in the slide chambers. <i>(B)</i> Analysis of PARP cleavage in TTR-treated and TTR/SAP-treated IMR-32 cells. Western blot analysis of PARP cleavage fragment (89 kDa) was performed with a PARP-specific antibody in extracts from cells treated with 20 µM TTR-A alone or in the presence of either 1.5 µM SAP or 3 µM SAP, and the results were compared against the negative control (untreated cells; CTRL). Full-length PARP has a molecular mass of 116 kDa.</p>", "links"=>[], "tags"=>["prevents", "ttr-induced"], "article_id"=>166549, "categories"=>["Biotechnology", "Neuroscience", "Cell Biology", "Genetics"], "users"=>["Karin Andersson", "Malgorzata Pokrzywa", "Ingrid Dacklin", "Erik Lundgren"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055766.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SAP_prevents_TTR_induced_toxicity_/166549", "title"=>"SAP prevents TTR-induced toxicity.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-04 01:49:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/496132"], "description"=>"<p><i>(A)</i> Two independent TTR-A transgenic strains (<i>w; GMR-Gal4/+; UAS-TTR-A/+</i> designated TTRA-1 presented as white bars, and TTRA-2 as black bars) and three independent SAP-transgenic strains (<i>w; GMR-Gal4/+; UAS-SAP/+;</i> SAP-18, SAP-1 and SAP-5, represented by gray bars)–either alone or in combination with each other (black-dashed white bars)–were analyzed for occurrence of the dragged-wing posture (mean values; error bars indicate SD). Significant reduction in the frequency of abnormal wings (below 20%, red line) was observed upon co-expression of SAP in both strains of TTR-A (<i>P<</i>0.001 for all SAP/TTR-A and SAP/− vs. TTR-A genotypes; one-way ANOVA, sequential Bonferroni <i>post-hoc</i> test). <i>(B)</i> Dose-dependent reduction in the frequency of the dragged-wing phenotype in flies expressing both TTR-A and SAP. SAP had a significant protective effect against TTR-A toxicity, as seen from the mean value of the wing phenotype (descending red line). Expression levels of SAP (white bars) were quantified in nine independent UAS-SAP-transgenic lines and are presented as the fold change in relation to tubulin levels (mean values; error bars indicate SD). Representative immunoblots are shown in the panel below the diagram.</p>", "links"=>[], "tags"=>["dragged-wing", "phenotype", "flies", "co-expressed", "ttr-a"], "article_id"=>166644, "categories"=>["Biotechnology", "Neuroscience", "Cell Biology", "Genetics"], "users"=>["Karin Andersson", "Malgorzata Pokrzywa", "Ingrid Dacklin", "Erik Lundgren"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055766.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dose_dependent_reduction_of_the_frequency_of_the_dragged_wing_phenotype_in_fruit_flies_that_co_expressed_TTR_A_and_SAP_/166644", "title"=>"Dose-dependent reduction of the frequency of the dragged-wing phenotype in fruit flies that co-expressed TTR-A and SAP.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-04 01:50:44"}
  • {"files"=>["https://ndownloader.figshare.com/files/496230"], "description"=>"<p><i>(A–D)</i> TTR-A was detected with a TTR-specific monoclonal antibody (Mab39–44; in red) <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0055766#pone.0055766-Goldsteins2\" target=\"_blank\">[35]</a>, <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0055766#pone.0055766-Lundgren1\" target=\"_blank\">[58]</a>, and co-localized with SAP immunostaining (Epitomics; in green) in horizontal sections of heads of 2-week-old flies. <i>(E–H)</i> TTR-A was detected with TTR-specific polyclonal antibody (red). TTR-A aggregates were monitored with p-FTAA (green). (<i>A, B</i>) TTR-A secreted by the photoreceptors accumulated in the retinal compartment (<i>E, F</i>) and formed aggregates around the outer corneal layer (CL). This led to damage of the retinal array and leakage of TTR-A outside the CL. The two neighboring corneal lenses (arrows) are shown magnified at the upper left corner (insets). (<i>C</i>) SAP expressed alone in fly retina stayed soluble, as no p-FTAA aggregates were detected (<i>G</i>) and there were no degenerative changes. Co-localization of SAP with TTR-A prevented retinal damage in SAP/TTR-A fruit flies (<i>D</i>), and led to reduced p-FTAA staining in the CL (<i>H</i>). <i>Drosophila</i> genotypes: TTR-A/− (<i>w; GMR-Gal4/+; UAS-TTR-A/+</i>); TTR-A/TTR-A (<i>w; GMR-Gal4/GMR-Gal4; UAS-TTR-A/UAS-TTR-A</i>); −/SAP (<i>w; GMR-Gal4/+; +/UAS-SAP</i>); TTR-A/SAP (<i>w; GMR-Gal4/+; UAS-SAP/TTR-A</i>). Scale bar represents 50 µm.</p>", "links"=>[], "tags"=>["co-localizes", "ttr-a", "counteracts", "ttr-induced", "retinal"], "article_id"=>166752, "categories"=>["Biotechnology", "Neuroscience", "Cell Biology", "Genetics"], "users"=>["Karin Andersson", "Malgorzata Pokrzywa", "Ingrid Dacklin", "Erik Lundgren"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0055766.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SAP_co_localizes_with_TTR_A_in_Drosophila_eye_and_counteracts_TTR_induced_retinal_degeneration_/166752", "title"=>"SAP co-localizes with TTR-A in <i>Drosophila</i> eye and counteracts TTR-induced retinal degeneration.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-04 01:52:32"}

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  • {"unique-ip"=>"12", "full-text"=>"14", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"10", "full-text"=>"6", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
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  • {"unique-ip"=>"10", "full-text"=>"8", "pdf"=>"5", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"3", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
  • {"unique-ip"=>"9", "full-text"=>"8", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
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  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"6", "full-text"=>"4", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"5", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"7", "full-text"=>"8", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}

Relative Metric

{"start_date"=>"2013-01-01T00:00:00Z", "end_date"=>"2013-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[269, 466, 588, 697, 800, 896, 988, 1076, 1165, 1254, 1340, 1417]}, {"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[266, 468, 593, 703, 804, 903, 993, 1084, 1171, 1256, 1339, 1422, 1492]}, {"subject_area"=>"/Biology and life sciences/Cell biology", "average_usage"=>[272, 472, 600, 713, 815, 911, 1004, 1094, 1185, 1273, 1358, 1441]}, {"subject_area"=>"/Biology and life sciences/Organisms", "average_usage"=>[281, 484, 611, 728, 835, 934, 1030, 1123, 1214, 1299, 1383, 1464]}, {"subject_area"=>"/Biology and life sciences/Toxicology", "average_usage"=>[247, 444, 560, 669, 769, 863, 947, 1036, 1129, 1204, 1296, 1374, 1437]}, {"subject_area"=>"/Medicine and health sciences", "average_usage"=>[264, 460, 584, 692, 794, 887, 978, 1067, 1154, 1241, 1328, 1408, 1474]}]}
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