Related Experiment Video
Updated: Oct 16, 2025
06:12
Author Spotlight: A Novel Method for Comprehensive Cell Component Analysis of Cerebral Blood Clots
Published on: July 21, 2023
737
High Mobility Group Box 1 Protein in Cerebral Thromboemboli.
Fabian Essig1, Lilith Babilon1, Christoph Vollmuth1
1Department of Neurology, University Hospital Würzburg, 97080 Würzburg, Germany.
International Journal of Molecular Sciences
|October 23, 2021
Summary
High-mobility group box 1 protein (HMGB1) is a key component of blood clots in stroke patients. This damage-associated molecular pattern is strongly associated with neutrophils and platelets within these thromboemboli.
Area of Science:
- Neuroscience
- Immunology
- Cardiovascular Research
Background:
- High-mobility group box 1 protein (HMGB1) acts as a damage-associated molecular pattern.
- HMGB1 is implicated in neutrophil extracellular trap (NET) formation and thrombosis.
- NETs are frequently observed in cerebral thromboemboli.
Purpose of the Study:
- To investigate the presence and significance of HMGB1 in human thromboemboli from stroke patients with large vessel occlusion.
Main Methods:
- Analysis of HMGB1 expression in thromboemboli retrieved via mechanical thrombectomy from 37 stroke patients.
- Colocalization studies with neutrophils, NETs, and platelets.
- Correlation analysis between HMGB1 detection and cellular components.
Main Results:
- HMGB1 was detected in all analyzed thromboemboli, constituting 1.7% of the total area.
- HMGB1 colocalized with neutrophils and NETs, and was in proximity to platelets.
- HMGB1 levels strongly correlated with neutrophil (r = 0.58, p = 0.0002) and platelet counts (r = 0.51, p = 0.001).
Conclusions:
- HMGB1 is a significant component of thromboemboli responsible for large vessel occlusion stroke.
- HMGB1's presence is closely linked to neutrophil and platelet involvement in clot formation.
Related Concept Videos
01:19Membrane Asymmetry Regulating Transporters
6.0K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
6.0K
01:30Anticoagulant Drugs: Low-Molecular-Weight Heparins
1.0K
Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
1.0K
01:19Translocation of Proteins into the Mitochondria
8.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
8.1K
01:12Golgi Matrix Proteins
2.1K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.1K
01:42Microtubule Associated Proteins (MAPs)
4.9K
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
4.9K
00:49The Blood-brain Barrier
49.8K
Overview
49.8K