e proteins Search Results


20s proteasome  (R&D Systems)
94
R&D Systems 20s proteasome
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
20s Proteasome, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant human extracellular e cadherin fragment  (R&D Systems)
93
R&D Systems recombinant human extracellular e cadherin fragment
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
Recombinant Human Extracellular E Cadherin Fragment, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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bmp4  (R&D Systems)
94
R&D Systems bmp4
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
Bmp4, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e 563 human usp4 protein r d systems  (R&D Systems)
93
R&D Systems e 563 human usp4 protein r d systems
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
E 563 Human Usp4 Protein R D Systems, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant mouse cathepsin e protein  (R&D Systems)
90
R&D Systems recombinant mouse cathepsin e protein
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
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elisa kit  (Elabscience Biotechnology)
94
Elabscience Biotechnology elisa kit
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
Elisa Kit, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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sandwich elisa working principle  (Elabscience Biotechnology)
93
Elabscience Biotechnology sandwich elisa working principle
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
Sandwich Elisa Working Principle, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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sars cov 2 s1rbd  (Elabscience Biotechnology)
94
Elabscience Biotechnology sars cov 2 s1rbd
The impairment can be mitigated by <t>proteasome</t> activators. (A) <t>20S</t> Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.
Sars Cov 2 S1rbd, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mbp  (Elabscience Biotechnology)
92
Elabscience Biotechnology mbp
Quantitative representation of Aβ-positive areas ( a ) in brain coronal sections, identified through immune histochemistry (IHC), in both AD model and wild-type mice. Quantitative measurement of Aβ concentrations via ELISA in both AD and wild type mice of the whole-brain ( b ), its vasculature ( c ) and parenchyma ( d ). ELISA quantification of both brain vasculature and parenchyma ( e ) in AD and wild type mice of key proteins involved in trafficking (LRP1, <t>PACSIN2,</t> <t>RAB5),</t> metabolism (GLUT1), tight junction proteins (ZO-1, CLDN11), and other stress-related proteins <t>(MBP,</t> MAP-2, SRB1). For all analyzes (n = 3)
Mbp, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tnf α  (Danaher Inc)
99
Danaher Inc tnf α
Quantitative representation of Aβ-positive areas ( a ) in brain coronal sections, identified through immune histochemistry (IHC), in both AD model and wild-type mice. Quantitative measurement of Aβ concentrations via ELISA in both AD and wild type mice of the whole-brain ( b ), its vasculature ( c ) and parenchyma ( d ). ELISA quantification of both brain vasculature and parenchyma ( e ) in AD and wild type mice of key proteins involved in trafficking (LRP1, <t>PACSIN2,</t> <t>RAB5),</t> metabolism (GLUT1), tight junction proteins (ZO-1, CLDN11), and other stress-related proteins <t>(MBP,</t> MAP-2, SRB1). For all analyzes (n = 3)
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e elh1297  (Elabscience Biotechnology)
94
Elabscience Biotechnology e elh1297
Quantitative representation of Aβ-positive areas ( a ) in brain coronal sections, identified through immune histochemistry (IHC), in both AD model and wild-type mice. Quantitative measurement of Aβ concentrations via ELISA in both AD and wild type mice of the whole-brain ( b ), its vasculature ( c ) and parenchyma ( d ). ELISA quantification of both brain vasculature and parenchyma ( e ) in AD and wild type mice of key proteins involved in trafficking (LRP1, <t>PACSIN2,</t> <t>RAB5),</t> metabolism (GLUT1), tight junction proteins (ZO-1, CLDN11), and other stress-related proteins <t>(MBP,</t> MAP-2, SRB1). For all analyzes (n = 3)
E Elh1297, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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immunosorbent assay elisa kit  (Elabscience Biotechnology)
94
Elabscience Biotechnology immunosorbent assay elisa kit
NAT10 polarizes macrophages toward the M2 type through CCL2 . (A) Macrophages were polarized by treating them with the supernatant of ICC cells for 24 h. (B) After co-culturing ICC cells and macrophages for 24 h, the macrophages underwent polarization. (C) Co-culturing ICC cells with macrophages for 24 h resulted in the polarization of macrophages towards the M2 phenotype. (D) Immunofluorescence showed that CD86 expression increased and CD163 expression decreased in NAT10-knockdown tumors ( n = 6). Scale bars: 50 μm. (E and F) Western blot and <t>ELISA</t> showed that NAT10 knockdown decreased CCL2 expression levels in ICC cells and cell supernatant. (G) CCL2-knockdown cell lines were constructed and verified at the protein level. (H) Flow cytometry confirmed that CCL2 knockdown reduced the polarization of macrophages toward M2. (I) Immunofluorescence showed that CD86 expression increased and CD163 expression decreased in CCL2-knockdown tumors ( n = 6). Scale bars: 50 μm. Data are representative of three or more independent experimental replicates. Data are displayed as the mean ± SD. P -values were determined by Student’s t-test and one-way ANOVA in panels. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. ICC, intrahepatic cholangiocarcinoma; ELISA, enzyme-linked <t>immunosorbent</t> assay; SD, standard deviation; ANOVA, analysis of variance
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Image Search Results


The impairment can be mitigated by proteasome activators. (A) 20S Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.

Journal: bioRxiv

Article Title: β-Amyloid impairs Proteasome structure and function. Proteasome activation mitigates amyloid induced toxicity and cognitive deficits

doi: 10.1101/2024.10.23.619877

Figure Lengend Snippet: The impairment can be mitigated by proteasome activators. (A) 20S Proteasome chymotrypsin-like peptidase activity is inhibited by oligomeric Aβ42, but not by Aβ42 monomers or fibrils. N = 4. Asterisks denote statistically significant differences (p<0.05). Right: atomic force microscopy (AFM) images of Aβ particles (tapping mode in air). The occasional larger particles in the “monomer” preparation are likely spontaneously forming oligomers. ( B ) Morphometric analysis of the 20S proteasome particles imaged by AFM (tapping mode in liquid) reveals shifts in the particles’ dimensions upon incubation with oligomeric Aβ42. 827 control 20S particles (incubated with a vehicle) and 1181 particles incubated with 2 µM oligomeric Aβ42 were analysed. Solid lines are fittings for the frequencies of control (black) and oligo-treated (red) particles. Since almost all particles are in to-view position, the “length” parameter generated during the particle analysis corresponds to the diameter of the 20S α face. The diameters are raw numbers without correction for tip broadening. When the correction of 2 pixels for SNL probe is applied, the diameter for peak 1 (raw: 14 - 15 nm) falls into 10 – 11 nm range, in excellent agreement with the crystal structure of the human 20S proteasome . See Results for putative assignment of proteasome forms to the numbered peaks. (C) Incubation with oligomeric Aβ42 shifts the conformational equilibrium of 20S core particles imaged by AFM (tapping mode in liquid) toward less open-gate and closed-gate forms, but more intermediate forms. (D) Oligomeric Aβ42 does not significantly affect degradation of oxidized hemoglobin. Degradation of hemoglobin is enhanced by a range of oligomeric Aβ42 concentrations. N=4 samples. ( E, F ) Treatment of the 20S proteasome with activators TAT1-DEN or TAT1-TOD partially protects from inhibition inflicted by the oligomeric Aβ42. ( G ) Incubation with the proteasome activator TAT1-DEN induces a dramatic shift toward open-gate forms, even in the presence of 2 µM of oligomeric Aβ42. The numbers in columns indicate percent of conformers. The number of particles analyzed: 733 (vehicle control), 843 (with oligo Aβ42), 270 (with 1 µM TAT1-DEN) and 171 (with oligo Aβ42and TAT1-DEN). Average ± SD, n= 5 to 9 fields.

Article Snippet: Purified 20S Proteasome (R&D Systems, Cat# E-360), purified 26S Proteasome (R&D Systems, Cat# E-365).

Techniques: Activity Assay, Microscopy, Incubation, Control, Generated, Particle Size Analysis, Inhibition

(A) Native page immunoblot depicting purified 20S and 26S proteasome under incubation with oligomeric Aβ42. Immunoblot performed against proteasome β5 subunit and accompanying total protein silver stain. Arrows depict 26S and 20S proteasome assemblages. (B) Native page immunoblot depicting purified 26S proteasome under incubation with varying concentrations of oligomeric Aβ42. Top image shows a representative set, histogram represents N=3 per condition. (C) Model for impact of Aβ on proteasome processes. *p < 0 . 05, Student’s t test was used unless otherwise stated. N represents the number of animals or samples per group .

Journal: bioRxiv

Article Title: β-Amyloid impairs Proteasome structure and function. Proteasome activation mitigates amyloid induced toxicity and cognitive deficits

doi: 10.1101/2024.10.23.619877

Figure Lengend Snippet: (A) Native page immunoblot depicting purified 20S and 26S proteasome under incubation with oligomeric Aβ42. Immunoblot performed against proteasome β5 subunit and accompanying total protein silver stain. Arrows depict 26S and 20S proteasome assemblages. (B) Native page immunoblot depicting purified 26S proteasome under incubation with varying concentrations of oligomeric Aβ42. Top image shows a representative set, histogram represents N=3 per condition. (C) Model for impact of Aβ on proteasome processes. *p < 0 . 05, Student’s t test was used unless otherwise stated. N represents the number of animals or samples per group .

Article Snippet: Purified 20S Proteasome (R&D Systems, Cat# E-360), purified 26S Proteasome (R&D Systems, Cat# E-365).

Techniques: Clear Native PAGE, Western Blot, Purification, Incubation, Silver Staining

Quantitative representation of Aβ-positive areas ( a ) in brain coronal sections, identified through immune histochemistry (IHC), in both AD model and wild-type mice. Quantitative measurement of Aβ concentrations via ELISA in both AD and wild type mice of the whole-brain ( b ), its vasculature ( c ) and parenchyma ( d ). ELISA quantification of both brain vasculature and parenchyma ( e ) in AD and wild type mice of key proteins involved in trafficking (LRP1, PACSIN2, RAB5), metabolism (GLUT1), tight junction proteins (ZO-1, CLDN11), and other stress-related proteins (MBP, MAP-2, SRB1). For all analyzes (n = 3)

Journal: bioRxiv

Article Title: Multivalent Targeting of Blood-Brain Barrier LRP1 for Neurovascular Recovery Therapy for Alzheimer’s Disease

doi: 10.1101/2024.05.06.592767

Figure Lengend Snippet: Quantitative representation of Aβ-positive areas ( a ) in brain coronal sections, identified through immune histochemistry (IHC), in both AD model and wild-type mice. Quantitative measurement of Aβ concentrations via ELISA in both AD and wild type mice of the whole-brain ( b ), its vasculature ( c ) and parenchyma ( d ). ELISA quantification of both brain vasculature and parenchyma ( e ) in AD and wild type mice of key proteins involved in trafficking (LRP1, PACSIN2, RAB5), metabolism (GLUT1), tight junction proteins (ZO-1, CLDN11), and other stress-related proteins (MBP, MAP-2, SRB1). For all analyzes (n = 3)

Article Snippet: Protein concentrations for various proteins, including LRP1 (NOVUS, NBP3-00449), PACSIN2 (Anruike, YX-160103M), RAB5 (abbexa, abx154598), GLUT1 (Anruike, YX-071242M), Claudin11 (Anruike, YX-031229M), ZO1 (Elabscience, E-EL-M1161), MBP (Elabscience, E-EL-M0805), MAP-2 (Anruike, YX-120118M), SRB1 (Anruike, ARK-756321A), and Aβ (invitrogen, KMB3441) were determined using ELISA kits following the manufacturer protocols.

Techniques: Enzyme-linked Immunosorbent Assay

Pearson correlation coefficients for the colocalization of LRP1 and BBB endothelial cells (CD31) pre- and post A 39 -POs administration ( a ). Analysis performed on images derived from three independent experiments, with 6-7 vessels studied per trial. Quantification of Aβ content in cerebrovascular endothelial cells and brain parenchyma ( b ) (n = 3, statistical analyzis performed using unpaired t-tests, **** p<0.0001). ELISA measurements ( c ) of vascular and parenchymal proteins in 12-month-old WT, Sham APP/PS1, and APP/PS1 post A 39 -POs treatment mice, encompassing LRP1, PACSIN2, RAB5, GLUT1, Claudin 11, ZO-1, MBP, MAP-2, and SRB1. STED microscopy ( d ) of LRP1 (white) on the vessel wall (green), indicative of active transcytosis. Post-treatment, Aβ deposits around the BBB (red) are cleared with notable Aβ signal presence within the vascular lumen. For (b) and (c), statistical significance determined using one-way ANOVA, *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001, n ≥ 3.

Journal: bioRxiv

Article Title: Multivalent Targeting of Blood-Brain Barrier LRP1 for Neurovascular Recovery Therapy for Alzheimer’s Disease

doi: 10.1101/2024.05.06.592767

Figure Lengend Snippet: Pearson correlation coefficients for the colocalization of LRP1 and BBB endothelial cells (CD31) pre- and post A 39 -POs administration ( a ). Analysis performed on images derived from three independent experiments, with 6-7 vessels studied per trial. Quantification of Aβ content in cerebrovascular endothelial cells and brain parenchyma ( b ) (n = 3, statistical analyzis performed using unpaired t-tests, **** p<0.0001). ELISA measurements ( c ) of vascular and parenchymal proteins in 12-month-old WT, Sham APP/PS1, and APP/PS1 post A 39 -POs treatment mice, encompassing LRP1, PACSIN2, RAB5, GLUT1, Claudin 11, ZO-1, MBP, MAP-2, and SRB1. STED microscopy ( d ) of LRP1 (white) on the vessel wall (green), indicative of active transcytosis. Post-treatment, Aβ deposits around the BBB (red) are cleared with notable Aβ signal presence within the vascular lumen. For (b) and (c), statistical significance determined using one-way ANOVA, *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001, n ≥ 3.

Article Snippet: Protein concentrations for various proteins, including LRP1 (NOVUS, NBP3-00449), PACSIN2 (Anruike, YX-160103M), RAB5 (abbexa, abx154598), GLUT1 (Anruike, YX-071242M), Claudin11 (Anruike, YX-031229M), ZO1 (Elabscience, E-EL-M1161), MBP (Elabscience, E-EL-M0805), MAP-2 (Anruike, YX-120118M), SRB1 (Anruike, ARK-756321A), and Aβ (invitrogen, KMB3441) were determined using ELISA kits following the manufacturer protocols.

Techniques: Derivative Assay, Enzyme-linked Immunosorbent Assay, Microscopy

NAT10 polarizes macrophages toward the M2 type through CCL2 . (A) Macrophages were polarized by treating them with the supernatant of ICC cells for 24 h. (B) After co-culturing ICC cells and macrophages for 24 h, the macrophages underwent polarization. (C) Co-culturing ICC cells with macrophages for 24 h resulted in the polarization of macrophages towards the M2 phenotype. (D) Immunofluorescence showed that CD86 expression increased and CD163 expression decreased in NAT10-knockdown tumors ( n = 6). Scale bars: 50 μm. (E and F) Western blot and ELISA showed that NAT10 knockdown decreased CCL2 expression levels in ICC cells and cell supernatant. (G) CCL2-knockdown cell lines were constructed and verified at the protein level. (H) Flow cytometry confirmed that CCL2 knockdown reduced the polarization of macrophages toward M2. (I) Immunofluorescence showed that CD86 expression increased and CD163 expression decreased in CCL2-knockdown tumors ( n = 6). Scale bars: 50 μm. Data are representative of three or more independent experimental replicates. Data are displayed as the mean ± SD. P -values were determined by Student’s t-test and one-way ANOVA in panels. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. ICC, intrahepatic cholangiocarcinoma; ELISA, enzyme-linked immunosorbent assay; SD, standard deviation; ANOVA, analysis of variance

Journal: Journal of Translational Medicine

Article Title: N-acetyltransferase 10 affects the proliferation of intrahepatic cholangiocarcinoma and M2-type polarization of macrophages by regulating C-C motif chemokine ligand 2

doi: 10.1186/s12967-024-05664-z

Figure Lengend Snippet: NAT10 polarizes macrophages toward the M2 type through CCL2 . (A) Macrophages were polarized by treating them with the supernatant of ICC cells for 24 h. (B) After co-culturing ICC cells and macrophages for 24 h, the macrophages underwent polarization. (C) Co-culturing ICC cells with macrophages for 24 h resulted in the polarization of macrophages towards the M2 phenotype. (D) Immunofluorescence showed that CD86 expression increased and CD163 expression decreased in NAT10-knockdown tumors ( n = 6). Scale bars: 50 μm. (E and F) Western blot and ELISA showed that NAT10 knockdown decreased CCL2 expression levels in ICC cells and cell supernatant. (G) CCL2-knockdown cell lines were constructed and verified at the protein level. (H) Flow cytometry confirmed that CCL2 knockdown reduced the polarization of macrophages toward M2. (I) Immunofluorescence showed that CD86 expression increased and CD163 expression decreased in CCL2-knockdown tumors ( n = 6). Scale bars: 50 μm. Data are representative of three or more independent experimental replicates. Data are displayed as the mean ± SD. P -values were determined by Student’s t-test and one-way ANOVA in panels. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. ICC, intrahepatic cholangiocarcinoma; ELISA, enzyme-linked immunosorbent assay; SD, standard deviation; ANOVA, analysis of variance

Article Snippet: The levels of CCL2 in the cell supernatants were determined using an enzyme-linked immunosorbent assay (ELISA) kit (E-EL-H6005, Elabscience).

Techniques: Immunofluorescence, Expressing, Knockdown, Western Blot, Enzyme-linked Immunosorbent Assay, Construct, Flow Cytometry, Standard Deviation