Apolipoprotein E: Isoform Specific Differences in Tertiary Structure and Interaction with Amyloid-β in Human Alzheimer Brain
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{"title"=>"Apolipoprotein E: Isoform specific differences in tertiary structure and interaction with amyloid-β in human Alzheimer brain", "type"=>"journal", "authors"=>[{"first_name"=>"Phillip B.", "last_name"=>"Jones", "scopus_author_id"=>"55474784700"}, {"first_name"=>"Kenneth W.", "last_name"=>"Adams", "scopus_author_id"=>"16506003800"}, {"first_name"=>"Anete", "last_name"=>"Rozkalne", "scopus_author_id"=>"23489980000"}, {"first_name"=>"Tara L.", "last_name"=>"Spires-Jones", "scopus_author_id"=>"22836973400"}, {"first_name"=>"Tammy T.", "last_name"=>"Hshieh", "scopus_author_id"=>"56658715100"}, {"first_name"=>"Tadafumi", "last_name"=>"Hashimoto", "scopus_author_id"=>"7404792924"}, {"first_name"=>"Christine A.F.", "last_name"=>"von Armin", "scopus_author_id"=>"36931888200"}, {"first_name"=>"Mathew", "last_name"=>"Mielke", "scopus_author_id"=>"7004869289"}, {"first_name"=>"Brian J.", "last_name"=>"Bacskai", "scopus_author_id"=>"7003973512"}, {"first_name"=>"Bradley T.", "last_name"=>"Hyman", "scopus_author_id"=>"35351120600"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-79551627202", "sgr"=>"79551627202", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0014586", "pmid"=>"21297948", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "pui"=>"361218301"}, "id"=>"e8704ec2-d35f-3239-b58c-015247f2407a", "abstract"=>"We applied a novel application of FLIM-FRET to in situ measurement and quantification of protein interactions to explore isoform specific differences in Aβ-ApoE interaction and ApoE tertiary conformation in senile plaques in human Alzheimer brain. ApoE3 interacts more closely with Aβ than ApoE4, but a greater proportion of Aβ molecules within plaques are decorated with ApoE4 than ApoE3, lending strong support to the hypothesis that isoform specific differences in ApoE are linked with Aβ deposition. We found an increased number of ApoE N-terminal fragments in ApoE4 plaques, consistent with the observation that ApoE4 is more easily cleaved than ApoE3. In addition, we measured a small but significant isoform specific difference in ApoE domain interaction. Based on our in situ data, supported by traditional biochemical data, we propose a pathway by which isoform specific conformational differences increase the level of cleavage at the hinge region of ApoE4, leading to a loss of ApoE function to mediate clearance of Aβ and thereby increase the risk of AD for carriers of the APOEε4 allele.", "link"=>"http://www.mendeley.com/research/apolipoprotein-e-isoform-specific-differences-tertiary-structure-interaction-amyloid%CE%B2-human-alzheime-1", "reader_count"=>65, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>20, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>15, "Student > Postgraduate"=>1, "Student > Master"=>9, "Other"=>2, "Student > Bachelor"=>10, "Professor"=>3}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>20, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>15, "Student > Postgraduate"=>1, "Student > Master"=>9, "Other"=>2, "Student > Bachelor"=>10, "Professor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>4, "Biochemistry, Genetics and Molecular Biology"=>4, "Agricultural and Biological Sciences"=>37, "Medicine and Dentistry"=>9, "Neuroscience"=>5, "Physics and Astronomy"=>1, "Chemistry"=>4, "Computer Science"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>9}, "Neuroscience"=>{"Neuroscience"=>5}, "Chemistry"=>{"Chemistry"=>4}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>37}, "Computer Science"=>{"Computer Science"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}, "Unspecified"=>{"Unspecified"=>4}}, "reader_count_by_country"=>{"United States"=>2, "Japan"=>1, "Brazil"=>1, "France"=>1, "Switzerland"=>1, "Spain"=>1}, "group_count"=>2}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/801264"], "description"=>"<p>a) Blots using terminal specific antibodies reveal that the LMW band, and the lower portion of the HMW band are almost exclusively composed of C-terminal fragments. b) Blots of fractional brain extracts show that some higher molecular weight fragments exist in the TBS fraction. The Triton fraction contains comparatively few fragments of any size. The bulk of the degraded ApoE, particularly the LMW band appears in the SDS and formic acid fractions, implying that the degraded C-terminal fragments of ApoE are associated with amyloid plaques.</p>", "links"=>[], "tags"=>["blots", "probing", "termini"], "article_id"=>471624, "categories"=>["Neuroscience", "Biophysics", "Mental Health"], "users"=>["Phillip B. Jones", "Kenneth W. Adams", "Anete Rozkalne", "Tara L. Spires-Jones", "Tammy T. Hshieh", "Tadafumi Hashimoto", "Christine A. F. von Armin", "Mathew Mielke", "Brian J. Bacskai", "Bradley T. Hyman"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014586.g003", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Western_blots_probing_for_the_termini_of_ApoE_/471624", "title"=>"Western blots probing for the termini of ApoE.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 20:49:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/801078"], "description"=>"<p>Inter-epitope distances are normalized to the Förster radius. a) A dense core senile plaque from the cortex of a patient homozygous for ApoEε3. Aβ (green) and ApoE NT (red) are extremely well co-localized which illustrates that the plaque is decorated with ApoE. b) Schematic showing the three FLIM-FRET measurements that were made. We independently measured the interacting fraction and distance between Aβ and both ApoE terminal domains as well between the two ApoE domains. c) ApoE CT is in closer apposition to Aβ than ApoE NT, consistent with the assumption that the hydrophobic lipid binding region interacts with Aβ. The difference in distance is small enough to suggest that ApoE envelops Aβ in a similar fashion than it is known to interact with lipids. d) A significantly greater proportion of Aβ is bound to ApoE in the case of ApoE4. The data suggest a reduced capacity of ApoE4 to induce clearance of Aβ. e) ApoE4 has a slightly tighter terminal interaction. This is surprising because a large difference in inter-terminal interaction is expected from the <i>in vitro</i> data. f) ApoE shows a significantly lower numbers of interacting terminal domains. These data are proof that ApoE4 undergoes a greater amount of cleavage either before or after binding to Aβ. Differential cleavage may mediate Aβ clearance or deposition.</p>", "links"=>[], "tags"=>["apoe", "conformation", "reveals", "aspects", "apoe4", "plaque"], "article_id"=>471422, "categories"=>["Neuroscience", "Biophysics", "Mental Health"], "users"=>["Phillip B. Jones", "Kenneth W. Adams", "Anete Rozkalne", "Tara L. Spires-Jones", "Tammy T. Hshieh", "Tadafumi Hashimoto", "Christine A. F. von Armin", "Mathew Mielke", "Brian J. Bacskai", "Bradley T. Hyman"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014586.g001", "stats"=>{"downloads"=>2, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_FLIM_FRET_study_of_ApoE_conformation_and_A_946_ApoE_interaction_reveals_multiple_aspects_of_ApoE4_associated_plaque_pathology_/471422", "title"=>"FLIM-FRET study of ApoE conformation and Aβ-ApoE interaction reveals multiple aspects of ApoE4 associated plaque pathology.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 20:48:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/801357"], "description"=>"<p>a) The FLIM-FRET data can be translated into real distances by multiplying by the Forster radius of A488 and Alexafluor 555 (7 nm). The structural differences between isoforms and interactions with Aβ are compared (not to scale but distances marked in nm). The Aβ-ApoE4 distance is larger than Aβ-ApoE3 despite the fact that the propensity for interaction is greater. ApoE4 shows a tighter inter-terminal interaction although the difference is not large. This result suggests that under these conditions ApoE conformation is influenced but not dominated the domain interaction. Nevertheless, this small conformational difference could lead to a differential vulnerability to cleavage at the hinge region leading to a larger number of orphan ApoE4 C-terminal fragments bound to Aβ. b) Our proposed model for the increased risk of senile plaque associated with ApoE4. Under normal conditions, ApoE acts as a bridging protein between Aβ and one of the lipoprotein receptor proteins, thereby mediating clearance across the cell membrane. In the Case of ApoE4, the conformational difference leads to enhanced vulnerability to cleavage, which in turn leads to a loss of clearance function and enhanced deposition.</p>", "links"=>[], "tags"=>["biophysics/protein folding", "neuroscience/neurobiology of disease and regeneration", "mental health/alzheimer disease"], "article_id"=>471719, "categories"=>["Neuroscience", "Biophysics", "Mental Health"], "users"=>["Phillip B. Jones", "Kenneth W. Adams", "Anete Rozkalne", "Tara L. Spires-Jones", "Tammy T. Hshieh", "Tadafumi Hashimoto", "Christine A. F. von Armin", "Mathew Mielke", "Brian J. Bacskai", "Bradley T. Hyman"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014586.g004", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Summary_of_findings_/471719", "title"=>"Summary of findings.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 20:50:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/801421"], "description"=>"<p>The genotype, age of the patient at death, sex and postmortem interval (PMI) is given where available from ADRC records. The check marks show which of the three experiments in which the brain was used. Some brains were used in more than one comparison depending on availability of tissue. For each of the 6 comparisons, the total number of plaques imaged (‘n’) is also given.</p>", "links"=>[], "tags"=>["cases", "flim-fret"], "article_id"=>471785, "categories"=>["Neuroscience", "Biophysics", "Mental Health"], "users"=>["Phillip B. Jones", "Kenneth W. Adams", "Anete Rozkalne", "Tara L. Spires-Jones", "Tammy T. Hshieh", "Tadafumi Hashimoto", "Christine A. F. von Armin", "Mathew Mielke", "Brian J. Bacskai", "Bradley T. Hyman"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014586.t001", "stats"=>{"downloads"=>1, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_List_of_cases_used_for_the_FLIM_FRET_study_/471785", "title"=>"List of cases used for the FLIM-FRET study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 20:50:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/801182"], "description"=>"<p>a) Using poly-clonal antibody, the distribution of ApoE fragments is clearly different between healthy aged brains and AD brains with further marked differences between genotypes. b) Comparisons of densitometry show significant increases in the amount of ApoE in Alzheimer brains, with the greatest amount in individuals homozygous for ApoE4. c) We also measured an increase in LMW (7–10 kDa) fragments in the case of AD, the presence of APOEε4 further amplifies the effect. The effect is similar but less subtle for HMW (17–34 kDa) fragments. In all cases asterisks indicate significance as assessed using ANOVA and Bonferonni-Dunn post-hoc test.</p>", "links"=>[], "tags"=>["blots", "homogenates", "patients", "aged"], "article_id"=>471543, "categories"=>["Neuroscience", "Biophysics", "Mental Health"], "users"=>["Phillip B. Jones", "Kenneth W. Adams", "Anete Rozkalne", "Tara L. Spires-Jones", "Tammy T. Hshieh", "Tadafumi Hashimoto", "Christine A. F. von Armin", "Mathew Mielke", "Brian J. Bacskai", "Bradley T. Hyman"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0014586.g002", "stats"=>{"downloads"=>2, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Western_blots_of_brain_homogenates_from_AD_patients_and_normal_aged_brains_/471543", "title"=>"Western blots of brain homogenates from AD patients and normal aged brains.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 20:49:09"}

PMC Usage Stats | Further Information

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Relative Metric

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