scholarly journals The N-terminal domain of thrombomodulin sequesters high-mobility group-B1 protein, a novel antiinflammatory mechanism

2005 ◽  
Vol 115 (5) ◽  
pp. 1267-1274 ◽  
Author(s):  
Kazuhiro Abeyama ◽  
David M. Stern ◽  
Yuji Ito ◽  
Ko-ichi Kawahara ◽  
Yasushi Yoshimoto ◽  
...  
Keyword(s):  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Terminal Domain

High mobility group box 1 protein, a cue for stem cell recruitment

2004 ◽  
Vol 68 (6) ◽  
pp. 1165-1170 ◽  
Author(s):  
Roberta Palumbo ◽  
Marco E Bianchi
Keyword(s):  
Stem Cell ◽  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Cell Recruitment

SEQUENTIAL CSF CONCENTRATIONS OF HIGH MOBILITY GROUP BOX 1 PROTEIN, A NUCLEAR FACTOR, IN SUBARACHNOID HEMORRHAGE PATIENTS

2004 ◽  
Vol 32 (Supplement) ◽  
pp. A103
Author(s):  
Tadashi Kaneko ◽  
Susumu Yamashita ◽  
Ryosuke Tsuruta ◽  
Shunji Kasaoka ◽  
Kiyoshi Okabayashi ◽  
...  
Keyword(s):  
Subarachnoid Hemorrhage ◽  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Nuclear Factor

scholarly journals The High Mobility Group A1 (HMGA1) Chromatin Architectural Factor Modulates Nuclear Stiffness in Breast Cancer Cells

2019 ◽  
Vol 20 (11) ◽  
pp. 2733 ◽  
Author(s):  
Beatrice Senigagliesi ◽  
Carlotta Penzo ◽  
Luisa Ulloa Severino ◽  
Riccardo Maraspini ◽  
Sara Petrosino ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Protein A ◽  
High Mobility ◽  
Histone H1 ◽  
High Mobility Group ◽  
Expression Level ◽  
Essential Condition ◽  
Cellular Models ◽  
Hmga1 Expression

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.

scholarly journals Salicylaldehyde ester-mediated protein semi-synthesis enables studies on the tetra-acetylation of HMGB1

2021 ◽  
Author(s):  
Tongyao Wei ◽  
Jiamei Liu ◽  
Yi Tan ◽  
Ruohan Wei ◽  
Jinzheng Wang ◽  
...  
Keyword(s):  
Signaling Pathway ◽  
High Purity ◽  
Protein Function ◽  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Biological Study ◽  
Post Translational Modifications ◽  
Site Specific ◽  
Synthesis Strategy

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.

Glitazone-mediated vascular protection requires high mobility group A1 protein – a new PPARgamma coregulator

2010 ◽  
Vol 5 (S 01) ◽  
Author(s):  
M Bloch ◽  
A Prock ◽  
F Paonessa ◽  
A Foryst-Ludwig ◽  
K Kappert ◽  
...  
Keyword(s):  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Vascular Protection

scholarly journals Rhinosinusal Inflammation and High Mobility Group Box 1 Protein: A New Target for Therapy

ORL ◽  
2016 ◽  
Vol 78 (2) ◽  
pp. 77-85 ◽  
Author(s):  
Luisa Maria Bellussi ◽  
Serena Cocca ◽  
Lei Chen ◽  
Francesco Maria Passali ◽  
Condrut Sarafoleanu ◽  
...  
Keyword(s):  
Protein A ◽  
High Mobility ◽  
High Mobility Group
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