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Updated: Jun 2, 2026

Processing of Human Cardiac Tissue Toward Extracellular Matrix Self-assembling Hydrogel for In Vitro and In Vivo Applications
Published on: December 4, 2017
EMILIN2 (Elastin microfibril interface located protein), potential modifier of thrombosis
1Joseph J, Jacobs Center For Thrombosis and Vascular Biology, Department of Cardiovascular Medicine and Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA. hooverj@ccf.org.
Elastin microfibril interface located protein 2 (EMILIN2) is found in blood clots. Inhibiting EMILIN2 reduces platelet aggregation, suggesting a role for EMILIN2 in thrombosis.
Area of Science:
- Cardiovascular Biology
- Extracellular Matrix Proteins
- Thrombosis Research
Background:
- Elastin microfibril interface located protein 2 (EMILIN2) is an extracellular glycoprotein linked to cardiovascular development.
- Limited information exists regarding EMILIN2's specific function within the cardiovascular system.
- Other EMILIN proteins are implicated in elastogenesis and coagulation.
Purpose of the Study:
- To investigate the potential role of EMILIN2 in the process of thrombosis.
- To determine if EMILIN2 expression is altered during thrombus formation.
Main Methods:
- Analysis of EMILIN2 mRNA expression in various mouse tissues and cell types (macrophages, endothelial cells, fibroblasts).
- Immunohistochemical identification of EMILIN2 in mouse carotid arteries and aorta.
- Assessment of EMILIN2's role in thrombosis using a ferric chloride-induced carotid artery injury model in mice.
- Evaluation of platelet aggregation and de-aggregation following ADP stimulation and EMILIN2 inhibition.
Main Results:
- EMILIN2 mRNA was detected in multiple mouse tissues, with the highest levels in bone marrow.
- Macrophages exhibited higher EMILIN2 mRNA expression compared to endothelial cells and fibroblasts.
- EMILIN2 was localized to cells and the extracellular matrix in the carotid artery and aorta.
- EMILIN2 expression was significantly increased within thrombi after injury.
- Inhibition of EMILIN2 enhanced platelet de-aggregation.
Conclusions:
- EMILIN2 is present in thrombi and may contribute to their formation.
- EMILIN2's role in thrombosis is supported by its presence in the vessel wall and thrombus, and its influence on platelet aggregation.
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