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{"title"=>"Changes in proteasome structure and function caused by HAMLET in tumor cells", "type"=>"journal", "authors"=>[{"first_name"=>"Lotta", "last_name"=>"Gustafsson", "scopus_author_id"=>"7203015117"}, {"first_name"=>"Sonja", "last_name"=>"Aits", "scopus_author_id"=>"23468829600"}, {"first_name"=>"Patrik", "last_name"=>"Önnerfjord", "scopus_author_id"=>"6601966697"}, {"first_name"=>"Maria", "last_name"=>"Trulsson", "scopus_author_id"=>"26022679000"}, {"first_name"=>"Petter", "last_name"=>"Storm", "scopus_author_id"=>"26533536900"}, {"first_name"=>"Catharina", "last_name"=>"Svanborg", "scopus_author_id"=>"7006063630"}], "year"=>2009, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"19365565", "doi"=>"10.1371/journal.pone.0005229", "sgr"=>"65349095292", "isbn"=>"1932-6203 (Electronic)", "scopus"=>"2-s2.0-65349095292", "issn"=>"19326203", "pui"=>"354520075"}, "id"=>"29f77719-578a-35fc-b3c1-88746d83f2be", "abstract"=>"BACKGROUND: Proteasomes control the level of endogenous unfolded proteins by degrading them in the proteolytic core. Insufficient degradation due to altered protein structure or proteasome inhibition may trigger cell death. This study examined the proteasome response to HAMLET, a partially unfolded protein-lipid complex, which is internalized by tumor cells and triggers cell death.\\n\\nMETHODOLOGY/PRINCIPAL FINDINGS: HAMLET bound directly to isolated 20S proteasomes in vitro and in tumor cells significant co-localization of HAMLET and 20S proteasomes was detected by confocal microscopy. This interaction was confirmed by co-immunoprecipitation from extracts of HAMLET-treated tumor cells. HAMLET resisted in vitro degradation by proteasomal enzymes and degradation by intact 20S proteasomes was slow compared to fatty acid-free, partially unfolded alpha-lactalbumin. After a brief activation, HAMLET inhibited proteasome activity in vitro and in parallel a change in proteasome structure occurred, with modifications of catalytic (beta1 and beta5) and structural subunits (alpha2, alpha3, alpha6 and beta3). Proteasome inhibition was confirmed in extracts from HAMLET-treated cells and there were indications of proteasome fragmentation in HAMLET-treated cells.\\n\\nCONCLUSIONS/SIGNIFICANCE: The results suggest that internalized HAMLET is targeted to 20S proteasomes, that the complex resists degradation, inhibits proteasome activity and perturbs proteasome structure. We speculate that perturbations of proteasome structure might contribute to the cytotoxic effects of unfolded protein complexes that invade host cells.", "link"=>"http://www.mendeley.com/research/changes-proteasome-structure-function-caused-hamlet-tumor-cells", "reader_count"=>23, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>8, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>4, "Student > Postgraduate"=>1, "Other"=>2, "Student > Bachelor"=>3, "Lecturer > Senior Lecturer"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>8, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>4, "Student > Postgraduate"=>1, "Other"=>2, "Student > Bachelor"=>3, "Lecturer > Senior Lecturer"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>4, "Materials Science"=>1, "Medicine and Dentistry"=>4, "Agricultural and Biological Sciences"=>14}, "reader_count_by_subdiscipline"=>{"Materials Science"=>{"Materials Science"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>4}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>14}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}}, "reader_count_by_country"=>{"Denmark"=>1, "Poland"=>1, "Israel"=>1}, "group_count"=>3}

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/901486"], "description"=>"<p>(A) HAMLET is formed when native α-lactalbumin releases the strongly bound Ca²⁺ and exposes a fatty-acid binding site, which permits oleic acid (C18:1, 9 <i>cis</i>) to interact and stabilize the partially unfolded state. The figure was generated using the crystal structure of human α-lactalbumin <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0005229#pone.0005229-Acharya1\" target=\"_blank\">[39]</a> and MOLMOL 2K.2 <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0005229#pone.0005229-Koradi1\" target=\"_blank\">[40]</a>. (B) Near-UV CD spectra were recorded in sodium phosphate buffer without EDTA. Native α-lactalbumin showed the expected minimum at 270 nm arising from the tyrosine and a maximum at 293 nm arising from the tryptophan residues. In HAMLET, α-lactalbumin showed a loss of signal at 270 nm and at 293 nm, typical of partial unfolding <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0005229#pone.0005229-Svensson1\" target=\"_blank\">[9]</a>, <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0005229#pone.0005229-Svensson2\" target=\"_blank\">[16]</a>. Apo α-lactalbumin was obtained by EDTA treatment and showed a similar loss of signal. (C) Effect of HAMLET on tumor cells and healthy cells. Glioblastoma cells and kidney carcinoma cells treated with HAMLET (34 µM, 1 and 3 hours) died while normal astrocytes and renal epithelial cells (HRTEC) remained viable. (D) Difference in uptake of HAMLET and α-lactalbumin by tumor cells. Lung carcinoma cells (A549) were exposed to 34 µM of Alexa Fluor 568-labeled HAMLET or α-lactalbumin (both red). (E) Quantification by flow cytometry of HAMLET or α-lactalbumin uptake by A549 cells (N = 10,000) after 1 and 3 hours of incubation.</p>", "links"=>[], "tags"=>["unfolded", "oleic"], "article_id"=>571937, "categories"=>["Cancer", "Cell Biology", "Biochemistry"], "users"=>["Lotta Gustafsson", "Sonja Aits", "Patrik Önnerfjord", "Maria Trulsson", "Petter Storm", "Catharina Svanborg"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0005229.g001", "stats"=>{"downloads"=>4, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_HAMLET_is_a_complex_of_partially_unfolded_945_lactalbumin_and_oleic_acid_/571937", "title"=>"HAMLET is a complex of partially unfolded α-lactalbumin and oleic acid.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 06:15:49"}
• {"files"=>["https://ndownloader.figshare.com/files/901599"], "description"=>"<p>(A) Binding of HAMLET to 20S proteasome subunits. 20S proteasomes were denatured, separated by SDS-PAGE and stained with Amido black or silver staining or blotted onto PVDF membranes. Left panels: Membranes were overlaid with 0.14 mM HAMLET and binding was detected by immunoblot using anti-α-lactalbumin antibodies. Right panels: Membranes were overlayed with ¹²⁵I-HAMLET and binding was detected by autoradiography. (B) Binding of HAMLET to 20S proteasome β5 subunit on a protein array. Protein arrays were probed with Alexa Fluor 568-labeled HAMLET and fluorescence intensity was measured. HAMLET bound to the 20S proteasome β5 subunit in a concentration-dependent manner. (C) Co-immunoprecipitation of lysates from HAMLET-treated A549 cells (34 µM, 1 hour) with anti-α-lactalbumin antibodies (IP anti-α-lact) or no antibodies (IP mock). Lysates and precipitates were examined by Western Blot using antibodies against the 20S proteasome core subunits. A very weak band was detected at ∼30 kDa. (D) Confocal images showing co-localization of Alexa Fluor 568-labeled HAMLET (34 µM, 1 hour) and 20S proteasomes (antibody against 20S proteasome core subunits) in the cell periphery and cytoplasm of A549 cells.</p>", "links"=>[], "tags"=>["hamlet", "proteasomes"], "article_id"=>572051, "categories"=>["Cancer", "Cell Biology", "Biochemistry"], "users"=>["Lotta Gustafsson", "Sonja Aits", "Patrik Önnerfjord", "Maria Trulsson", "Petter Storm", "Catharina Svanborg"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0005229.g002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interaction_of_HAMLET_with_proteasomes_in_vitro_and_in_tumor_cells_/572051", "title"=>"Interaction of HAMLET with proteasomes <i>in vitro</i> and in tumor cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 06:16:32"}
• {"files"=>["https://ndownloader.figshare.com/files/902150"], "description"=>"<p>(A–C) Changes in the staining of 20S proteasome subunits in A549 cells after HAMLET treatment (34 and 45 µM, 1 hour). Cells were stained with antibodies against the 20S proteasome core subunits (α5, α7, β1, β5, β5i and β7), antibodies against the β1 subunit or antibodies against the β5 subunit. (A) Confocal images showing increased core and β1 subunit staining, and decreased β5 subunit staining after HAMLET treatment (45 µM, 1 hour). (B) Fluorescence intensity was quantified in control and HAMLET-treated cells (34 and 45 µM, 1 hour). (C) The increase in core subunit staining after HAMLET was blocked by proteasome inhibition with MG132. (D) Western blot of cell extracts from cells treated with HAMLET (34 µM) for 1 and 6 hours, showing loss of 20S proteasomes staining after 6 hours. Antibodies against the 20S proteasome core subunits were used.</p>", "links"=>[], "tags"=>["20s", "proteasome", "staining", "hamlet", "carcinoma"], "article_id"=>572599, "categories"=>["Cancer", "Cell Biology", "Biochemistry"], "users"=>["Lotta Gustafsson", "Sonja Aits", "Patrik Önnerfjord", "Maria Trulsson", "Petter Storm", "Catharina Svanborg"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0005229.g006", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Changes_in_20S_proteasome_staining_after_HAMLET_treatment_of_carcinoma_cells_/572599", "title"=>"Changes in 20S proteasome staining after HAMLET treatment of carcinoma cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 06:19:22"}
• {"files"=>["https://ndownloader.figshare.com/files/901871"], "description"=>"<p>(A) Proteasome activity was monitored <i>in vitro</i> as chymotrypsin-dependent suc-LLVY-AMC cleavage (50 µM) over time and MG132 was used as proteasome inhibitor. Except for the first 10 minutes HAMLET reduced proteasome activity compared to the control. (B) Inhibition of proteasome activity in A549 cells. Cytoplasmic extracts were prepared from cells treated with HAMLET or native α-lactalbumin (34 µM) after 1, 3 and 6 hours of incubation and enzymatic activity was quantified by suc-LLVY-AMC cleavage (50 µM). MG132 was used to inhibit proteasome function.</p>", "links"=>[], "tags"=>["inhibits", "proteasome"], "article_id"=>572328, "categories"=>["Cancer", "Cell Biology", "Biochemistry"], "users"=>["Lotta Gustafsson", "Sonja Aits", "Patrik Önnerfjord", "Maria Trulsson", "Petter Storm", "Catharina Svanborg"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0005229.g004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_HAMLET_inhibits_proteasome_activity_/572328", "title"=>"HAMLET inhibits proteasome activity.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 06:17:59"}
• {"files"=>["https://ndownloader.figshare.com/files/901694"], "description"=>"<p>(A, B) HAMLET, partially unfolded α-lactalbumin (apo α-lactalbumin) or native α-lactalbumin was exposed to trypsin (E∶S 1∶50, by weight) (A) or chymotrypsin (E∶S 1∶100, by weight) (B) <i>in vitro</i> and fragments were detected by SDS-PAGE. Native α-lactalbumin was in 200 µM calcium acetate whereas partially unfolded α-lactalbumin was in 200 µM EDTA. Arrows indicate time points when all HAMLET was degraded. (C) HAMLET or partially unfolded α-lactalbumin (apo α-lact) (both 7 µM) were mixed with 6 µg of human erythrocyte 20S proteasomes and incubated for 2 hours at 37°C. The proteins were separated by SDS-PAGE and visualized by silver staining. MG132 was used to inhibit proteasome activity. The arrows indicate the molecular sizes of full length apo α-lactalbumin/HAMLET (14 kDa) and a smaller fragment (∼7 kDa).</p>", "links"=>[], "tags"=>["hamlet", "degradation", "proteasomal"], "article_id"=>572153, "categories"=>["Cancer", "Cell Biology", "Biochemistry"], "users"=>["Lotta Gustafsson", "Sonja Aits", "Patrik Önnerfjord", "Maria Trulsson", "Petter Storm", "Catharina Svanborg"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0005229.g003", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Resistance_of_HAMLET_to_degradation_by_proteasomal_enzymes_/572153", "title"=>"Resistance of HAMLET to degradation by proteasomal enzymes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 06:17:03"}
• {"files"=>["https://ndownloader.figshare.com/files/901994"], "description"=>"<p>(A, B) <i>In vitro</i> fragmentation of human 20S proteasomes after 20 minutes incubation with HAMLET (7 µM), compared to the α-lactalbumin control. (A) The proteins were separated by SDS-PAGE and gels were stained with Amido black. Changes in 20S proteasome subunits are indicated by arrows. The subunits identified by mass spectrometry are shown in the table. (B) Western Blot of samples from <i>in vitro</i> mixing experiment with 20S proteasomes and HAMLET or α-lactalbumin using antibodies against the 20S proteasome core subunits. (C) MALDI-TOF mass spectrometry of intact 20S proteasomes (top panel) and major changes after HAMLET treatment (bottom panel), indicated by arrows.</p>", "links"=>[], "tags"=>["changes", "20s", "proteasomes", "hamlet"], "article_id"=>572445, "categories"=>["Cancer", "Cell Biology", "Biochemistry"], "users"=>["Lotta Gustafsson", "Sonja Aits", "Patrik Önnerfjord", "Maria Trulsson", "Petter Storm", "Catharina Svanborg"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0005229.g005", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structural_changes_in_20S_proteasomes_after_HAMLET_treatment_in_vitro_/572445", "title"=>"Structural changes in 20S proteasomes after HAMLET treatment <i>in vitro</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 06:18:36"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime