Influence of Nonenzymatic Posttranslational Modifications on Constitution, Oligomerization and Receptor Binding of S100A12
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{"title"=>"Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12", "type"=>"journal", "authors"=>[{"first_name"=>"Kerstin", "last_name"=>"Augner", "scopus_author_id"=>"55858579200"}, {"first_name"=>"Jutta", "last_name"=>"Eichler", "scopus_author_id"=>"7102232257"}, {"first_name"=>"Wolfgang", "last_name"=>"Utz", "scopus_author_id"=>"7004350794"}, {"first_name"=>"Monika", "last_name"=>"Pischetsrieder", "scopus_author_id"=>"7003441067"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"25426955", "sgr"=>"84913554659", "doi"=>"10.1371/journal.pone.0113418", "scopus"=>"2-s2.0-84913554659", "pui"=>"600595843", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "issn"=>"19326203"}, "id"=>"dee8ff39-5493-3b18-95bf-1e1f5918f518", "abstract"=>"This study examined the effect of methylglyoxal (MGO)-derived nonenzymatic posttranslational modifications (nePTMs) on the binding affinity of S100A12 to its natural receptor for advanced glycation end-products (RAGE). Binding of MGO-modified S100A12 to RAGE decreased significantly with increasing MGO concentration and incubation time. Ca2+-induced S100A12 hexamerization was impaired only at higher MGO concentrations indicating that the loss of affinity is not predominantly caused by disturbance of ligand oligomerization. nePTM mapping showed carboxyethylation of lysine (CEL) and the N-terminus without preferential modification sites. Besides, hydroimidazolone, hemiaminals, argpyrimidine, and tetrahydropyrimidine rapidly formed at R21. Even at the highest modification rate, hexamerization of synthesized CEL-S100A12 was unaffected and RAGE-binding only slightly impaired. Thus, nePTMs at R21 seem to be the major cause of MGO-induced impairment of S100A12 oligomerization and RAGE binding.", "link"=>"http://www.mendeley.com/research/influence-nonenzymatic-posttranslational-modifications-constitution-oligomerization-receptor-binding", "reader_count"=>9, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>1, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>3, "Student > Master"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>1, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>3, "Student > Master"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>1, "Agricultural and Biological Sciences"=>3, "Medicine and Dentistry"=>1, "Chemistry"=>2, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>2}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>3}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}, "Unspecified"=>{"Unspecified"=>1}}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1807717"], "description"=>"<p>S100A12 was incubated with the indicated concentrations of pyruvate and sodium cyanoborohydride at 25 °C for 16 h to achieve a similar CEL-modification as present in methylglyoxal (MGO)-modified S100A12. Binding of the CEL-modified S100A12 to RAGE was investigated with surface plasmon resonance spectroscopy. The binding of the unincubated negative control was set as 100%. #, in all MGO-modified proteins, CEL modification rates were ≤ those of CEL-S100A12 at 3 mM. Values represent mean ± SD of three independent experiments with duplicate measurements; ***p<0.001, significant differences are related to the incubated control. The CEL-modifications did not inhibit the hexamerization of S100A12 because there was no elution behavior towards smaller molecular weight compared to the negative control (data not shown).</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252422, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.g004", "stats"=>{"downloads"=>0, "page_views"=>22, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_N_949_carboxyethyllysine_CEL_modifications_on_the_binding_of_S100A12_to_the_receptor_for_advanced_glycation_end_products_RAGE_/1252422", "title"=>"Effect of <i>N<sup>ε</sup></i>-carboxyethyllysine (CEL)-modifications on the binding of S100A12 to the receptor for advanced glycation end-products (RAGE).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807712"], "description"=>"<p>Structures of different advanced glycation end-products and their corresponding mass increase.</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252419, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.g003", "stats"=>{"downloads"=>2, "page_views"=>302, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structures_of_different_advanced_glycation_end_products_and_their_corresponding_mass_increase_/1252419", "title"=>"Structures of different advanced glycation end-products and their corresponding mass increase.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807730"], "description"=>"<p>The two subunits of the S100A12 dimer are shown in red and green. The C- and N-atoms of lysine or arginine side chains are colored white and blue, respectively.</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252436, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.g005", "stats"=>{"downloads"=>0, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Localization_of_resolved_lysine_A_or_arginine_B_side_chains_in_the_crystal_structure_of_S100A12_PDB_Code_2WCB_/1252436", "title"=>"Localization of resolved lysine (A) or arginine (B) side chains in the crystal structure of S100A12 (PDB-Code 2WCB).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807773"], "description"=>"<p>The intact protein was analyzed by MALDI-TOF-MS. All modifications were detected after one, three, and seven days of incubation. The table shows the results of three independent experiments; MGO, methylglyoxal; CEL, <i>N<sup>ε</sup></i>-carboxyethyllysine; CEA, carboxyethylarginine.</p><p>Overview of detected modifications of S100A12 after incubation with methylglyoxal at 37 °C.</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252464, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.t001", "stats"=>{"downloads"=>3, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overview_of_detected_modifications_of_S100A12_after_incubation_with_methylglyoxal_at_37_176_C_/1252464", "title"=>"Overview of detected modifications of S100A12 after incubation with methylglyoxal at 37 °C.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807770"], "description"=>"<p>The three dimers are shown in blue, red, and green. Nitrogen and oxygen atoms are shown in blue and red, respectively.</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252462, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.g007", "stats"=>{"downloads"=>0, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Environment_of_R21_in_the_S100A12_hexamer_PDBCode_2WCE_/1252462", "title"=>"Environment of R21 in the S100A12 hexamer (PDBCode 2WCE).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807705"], "description"=>"<p>S100A12 was incubated with different concentrations of MGO at 37 °C for 1, 3, and 7 days. Binding of the modified S100A12 to RAGE was investigated with surface plasmon resonance spectroscopy. The binding of the unincubated negative control was set as 100%. Values represent mean ± SD of three independent experiments with duplicate measurements; *p<0.05, ***p<0.001, significant differences are related to the control (0 µM MGO).</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252412, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.g001", "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effects_of_methylglyoxal_MGO_on_the_binding_of_S100A12_to_the_receptor_of_advanced_end_products_RAGE_/1252412", "title"=>"Effects of methylglyoxal (MGO) on the binding of S100A12 to the receptor of advanced end-products (RAGE).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807743"], "description"=>"<p>The three dimers of the S100A12 hexamer are shown in red, green, and blue, respectively.</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252444, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.g006", "stats"=>{"downloads"=>3, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Localization_of_arginine_side_chains_orange_in_the_S100A12_hexamer_PDB_Code_1GQM_/1252444", "title"=>"Localization of arginine side chains (orange) in the S100A12 hexamer (PDB-Code 1GQM).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807775"], "description"=>"<p>Peptides were analyzed with ultrahigh-performance liquid chromatography-electrospray ionization-tandem mass spectrometry after partial hydrolysis with GluC or chymotrypsin. Modifications were detected after one day of incubation with the exceptions as indicated in footnotes (a) and (c). The table shows the results of three independent experiments; <i><sup>a</sup></i> detected after three days, <i><sup>b</sup></i> five different peaks, <i><sup>c</sup></i> detected after seven days; MGO, methylglyoxal; CEL, <i>N<sup>ε</sup></i>-carboxyethyllysine; CEA, carboxyethylarginine.</p><p>Overview of detected modifications of S100A12 after incubation with methylglyoxal at 37°C for 1, 3, and 7 days.</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252467, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.t002", "stats"=>{"downloads"=>4, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overview_of_detected_modifications_of_S100A12_after_incubation_with_methylglyoxal_at_37_176_C_for_1_3_and_7_days_/1252467", "title"=>"Overview of detected modifications of S100A12 after incubation with methylglyoxal at 37°C for 1, 3, and 7 days.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-11-26 02:43:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1807710"], "description"=>"<p>S100A12 was incubated with different concentrations of MGO at 37 °C for 1, 3, and 7 days. Oligomerization behavior was analyzed with size-exclusion chromatography. The negative control incubated for the same time without MGO is shown in red. Chromatograms are representative for two independent experiments.</p>", "links"=>[], "tags"=>["rage", "cel", "modification", "nePTM", "mgo", "S 100A oligomerization", "Nonenzymatic Posttranslational Modifications", "S 100A"], "article_id"=>1252417, "categories"=>["Biological Sciences"], "users"=>["Kerstin Augner", "Jutta Eichler", "Wolfgang Utz", "Monika Pischetsrieder"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0113418.g002", "stats"=>{"downloads"=>0, "page_views"=>24, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Concentration_dependent_effect_of_methylglyoxal_MGO_on_the_ability_of_S100A12_to_form_hexamers_/1252417", "title"=>"Concentration-dependent effect of methylglyoxal (MGO) on the ability of S100A12 to form hexamers.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-11-26 02:43:45"}

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