scholarly journals High-Mobility Group Box-1 Protein a Potential Inflammatory Biomarker in Diabetic Retinopathy

10.5772/62524 ◽  
2016 ◽  
Author(s):  
Ghulam Mohammad
2014 ◽  
Vol 13 (1) ◽  
pp. 156 ◽  
Author(s):  
Yan Gong ◽  
Xin Jin ◽  
Quan-Shun Wang ◽  
Shi-Hui Wei ◽  
Bao-Ke Hou ◽  
...  

2004 ◽  
Vol 68 (6) ◽  
pp. 1165-1170 ◽  
Author(s):  
Roberta Palumbo ◽  
Marco E Bianchi

2004 ◽  
Vol 32 (Supplement) ◽  
pp. A103
Author(s):  
Tadashi Kaneko ◽  
Susumu Yamashita ◽  
Ryosuke Tsuruta ◽  
Shunji Kasaoka ◽  
Kiyoshi Okabayashi ◽  
...  

2019 ◽  
Vol 20 (11) ◽  
pp. 2733 ◽  
Author(s):  
Beatrice Senigagliesi ◽  
Carlotta Penzo ◽  
Luisa Ulloa Severino ◽  
Riccardo Maraspini ◽  
Sara Petrosino ◽  
...  

Plasticity is an essential condition for cancer cells to invade surrounding tissues. The nucleus is the most rigid cellular organelle and it undergoes substantial deformations to get through environmental constrictions. Nuclear stiffness mostly depends on the nuclear lamina and chromatin, which in turn might be affected by nuclear architectural proteins. Among these is the HMGA1 (High Mobility Group A1) protein, a factor that plays a causal role in neoplastic transformation and that is able to disentangle heterochromatic domains by H1 displacement. Here we made use of atomic force microscopy to analyze the stiffness of breast cancer cellular models in which we modulated HMGA1 expression to investigate its role in regulating nuclear plasticity. Since histone H1 is the main modulator of chromatin structure and HMGA1 is a well-established histone H1 competitor, we correlated HMGA1 expression and cellular stiffness with histone H1 expression level, post-translational modifications, and nuclear distribution. Our results showed that HMGA1 expression level correlates with nuclear stiffness, is associated to histone H1 phosphorylation status, and alters both histone H1 chromatin distribution and expression. These data suggest that HMGA1 might promote chromatin relaxation through a histone H1-mediated mechanism strongly impacting on the invasiveness of cancer cells.


2019 ◽  
Vol 44 (10) ◽  
pp. 1133-1143 ◽  
Author(s):  
Ghulam Mohammad ◽  
Ghada Maher Abdelaziz ◽  
Mohammad Mairaj Siddiquei ◽  
Ajmal Ahmad ◽  
Gert De Hertogh ◽  
...  

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e87574 ◽  
Author(s):  
Andrea Rachelle C. Santos ◽  
Galina Dvoriantchikova ◽  
Yiwen Li ◽  
Ghulam Mohammad ◽  
Ahmed M. Abu El-Asrar ◽  
...  

2021 ◽  
Author(s):  
Tongyao Wei ◽  
Jiamei Liu ◽  
Yi Tan ◽  
Ruohan Wei ◽  
Jinzheng Wang ◽  
...  

To answer how protein post-translational modifications (PTMs) affect protein function, conformation, sta-bility, localization and interaction with binders remains important in the biological study. However, the re-lated study has been dramatically hindered by the difficulty in obtaining homogenous proteins with site-specific PTMs of interest. Herein, we introduce a protein semi-synthesis strategy via salicylaldehyde ester-mediated chemical ligations (Ser/Thr ligation and Cys/Pen ligation). This methodology has enabled us to generate Lys (2/6/7/11) tetra-acetylated HMGB1 (high-mobility group box 1) protein, a 25 kDa proin-flammatory protein, in high purity. Further studies revealed that the tetra-acetylation may represent a regu-latory switch to control the HMGB1 signaling pathway by abolishing its interaction with lipopolysaccha-ride (LPS) and accelerating its degradation, consequently preventing cells from pyroptosis and lethality upon infectious injury.


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