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A Uniform Shear Assay for Human Platelet and Cell Surface Receptors via Cone-plate Viscometry
Published on: June 5, 2019
Activation-dependent surface expression of LOX-1 in human platelets
1National Cardiovascular Center Research Institute, Suita, Osaka, 565-8565, Japan.
Biochemical and Biophysical Research Communications
|March 27, 2001
Summary
Lectin-like oxidized LDL receptor-1 (LOX-1) is present on human platelets and exposed upon activation. This receptor facilitates oxidized LDL binding, potentially contributing to thrombosis in conditions like unstable angina pectoris.
Area of Science:
- Cardiovascular Biology
- Platelet Physiology
- Atherosclerosis Research
Background:
- Lectin-like oxidized LDL receptor-1 (LOX-1) is known to bind oxidized low-density lipoprotein (OxLDL).
- LOX-1 expression has been documented in endothelial cells, macrophages, and smooth muscle cells.
Purpose of the Study:
- To investigate the presence and function of LOX-1 in human platelets.
- To explore the role of platelet LOX-1 in OxLDL binding and thrombosis.
Main Methods:
- Identification of LOX-1 mRNA and protein in human platelets and megakaryocytic cell lines.
- Flow cytometry to analyze LOX-1 surface expression on activated platelets.
- Inhibition studies using anti-LOX-1 antibody to assess OxLDL binding.
- Immunohistochemistry of atherosclerotic plaques.
Main Results:
- LOX-1 mRNA and protein were detected in human platelets and megakaryocytic cell lines.
- Platelet LOX-1 surface expression is activation-dependent.
- Anti-LOX-1 antibody significantly inhibited OxLDL binding to activated platelets.
- LOX-1 protein accumulation was observed at the site of thrombus in atherosclerotic plaques.
Conclusions:
- Human platelets express LOX-1, which is exposed on the surface following activation.
- Platelet LOX-1 mediates the binding of OxLDL to activated platelets.
- The LOX-1-platelet interaction may play a role in promoting thrombosis in atherosclerosis.
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