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EMILIN2 (Elastin microfibril interface located protein), potential modifier of thrombosis.

Sa Q, Hoover-Plow JL - Thromb J (2011)

Bottom Line: Elastin microfibril interface located protein 2 (EMILIN2) is an extracellular glycoprotein associated with cardiovascular development.EMILIN2 was identified with cells and extracellular matrix by immunohistochemistry in the carotid and aorta.These results suggest EMILIN2 could play a role in thrombosis as a constituent of the vessel wall and/or a component of the thrombus.

View Article: PubMed Central - HTML - PubMed

Affiliation: Joseph 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.

ABSTRACT

Background: Elastin microfibril interface located protein 2 (EMILIN2) is an extracellular glycoprotein associated with cardiovascular development. While other EMILIN proteins are reported to play a role in elastogenesis and coagulation, little is known about EMILIN2 function in the cardiovascular system. The objective of this study was to determine whether EMILIN2 could play a role in thrombosis.

Results: EMILIN2 mRNA was expressed in 8 wk old C57BL/6J mice in lung, heart, aorta and bone marrow, with the highest expression in bone marrow. In mouse cells, EMILIN2 mRNA expression in macrophages was higher than expression in endothelial cells and fibroblasts. EMILIN2 was identified with cells and extracellular matrix by immunohistochemistry in the carotid and aorta. After carotid ferric chloride injury, EMILIN2 was abundantly expressed in the thrombus and inhibition of EMILIN2 increased platelet de-aggregation after ADP-stimulated platelet aggregation.

Conclusions: These results suggest EMILIN2 could play a role in thrombosis as a constituent of the vessel wall and/or a component of the thrombus.

No MeSH data available.


Related in: MedlinePlus

Localization of EMILIN2 in carotids. A, B. Sections from uninjured carotid were immunostained with E185 for EMILIN2. C, D, E. Ferric chloride induced vascular injury. Sections were immunostained with C. E185, D. Q-16, or F. P-selectin antibody. A, C, E, F. Magnification × 100 and B, D. × 400. G. Quantification of immunostaining. The values are mean ± SEM of the percent of EMILIN2 (E185)/vessel wall, EMILIN2 (E185)/thrombus area and P-selectin/thrombus area of 6 mice per strain. Six sections per mouse were analyzed for each mouse using Image-Pro Plus software. Modified from Sa et al [Mamm Genome 2010 21:337-349].
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Figure 3: Localization of EMILIN2 in carotids. A, B. Sections from uninjured carotid were immunostained with E185 for EMILIN2. C, D, E. Ferric chloride induced vascular injury. Sections were immunostained with C. E185, D. Q-16, or F. P-selectin antibody. A, C, E, F. Magnification × 100 and B, D. × 400. G. Quantification of immunostaining. The values are mean ± SEM of the percent of EMILIN2 (E185)/vessel wall, EMILIN2 (E185)/thrombus area and P-selectin/thrombus area of 6 mice per strain. Six sections per mouse were analyzed for each mouse using Image-Pro Plus software. Modified from Sa et al [Mamm Genome 2010 21:337-349].

Mentions: EMILIN2 was detected in the vessel wall of uninjured carotids (Figure 3A, B). The immunostaining was 55% ± 2 of the vessel wall area (Figure 3G, gray bar). EMILIN2 was detected in both cells and extracellular matrix. The aorta clearly defines the sites of Emilin2 (see additional file 3). To determine if EMILIN2 protein is incorporated into the thrombus, FeCl3 was used to induce thrombus formation in the carotid artery. After injury, carotid arteries were harvested and immunostained for EMILIN2 (Figure 3C, D). Strong (77% ± 2) (Figure 3G open bar) EMILIN2-specific staining was detected in thrombi, suggesting that EMILIN2 is associated most strongly with the thrombus rather than the vessel wall. This is consistent with the mRNA expression in the bone marrow cells, platelet, and plasma protein expression. No signal was detected in the sections stained with rabbit IgG or pre-immune rabbit serum. The staining of EMILIN2 in thrombi was confirmed by using the commercial EMILIN2 Q-16 antibody (Figure 3E).


EMILIN2 (Elastin microfibril interface located protein), potential modifier of thrombosis.

Sa Q, Hoover-Plow JL - Thromb J (2011)

Localization of EMILIN2 in carotids. A, B. Sections from uninjured carotid were immunostained with E185 for EMILIN2. C, D, E. Ferric chloride induced vascular injury. Sections were immunostained with C. E185, D. Q-16, or F. P-selectin antibody. A, C, E, F. Magnification × 100 and B, D. × 400. G. Quantification of immunostaining. The values are mean ± SEM of the percent of EMILIN2 (E185)/vessel wall, EMILIN2 (E185)/thrombus area and P-selectin/thrombus area of 6 mice per strain. Six sections per mouse were analyzed for each mouse using Image-Pro Plus software. Modified from Sa et al [Mamm Genome 2010 21:337-349].
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3113922&req=5

Figure 3: Localization of EMILIN2 in carotids. A, B. Sections from uninjured carotid were immunostained with E185 for EMILIN2. C, D, E. Ferric chloride induced vascular injury. Sections were immunostained with C. E185, D. Q-16, or F. P-selectin antibody. A, C, E, F. Magnification × 100 and B, D. × 400. G. Quantification of immunostaining. The values are mean ± SEM of the percent of EMILIN2 (E185)/vessel wall, EMILIN2 (E185)/thrombus area and P-selectin/thrombus area of 6 mice per strain. Six sections per mouse were analyzed for each mouse using Image-Pro Plus software. Modified from Sa et al [Mamm Genome 2010 21:337-349].
Mentions: EMILIN2 was detected in the vessel wall of uninjured carotids (Figure 3A, B). The immunostaining was 55% ± 2 of the vessel wall area (Figure 3G, gray bar). EMILIN2 was detected in both cells and extracellular matrix. The aorta clearly defines the sites of Emilin2 (see additional file 3). To determine if EMILIN2 protein is incorporated into the thrombus, FeCl3 was used to induce thrombus formation in the carotid artery. After injury, carotid arteries were harvested and immunostained for EMILIN2 (Figure 3C, D). Strong (77% ± 2) (Figure 3G open bar) EMILIN2-specific staining was detected in thrombi, suggesting that EMILIN2 is associated most strongly with the thrombus rather than the vessel wall. This is consistent with the mRNA expression in the bone marrow cells, platelet, and plasma protein expression. No signal was detected in the sections stained with rabbit IgG or pre-immune rabbit serum. The staining of EMILIN2 in thrombi was confirmed by using the commercial EMILIN2 Q-16 antibody (Figure 3E).

Bottom Line: Elastin microfibril interface located protein 2 (EMILIN2) is an extracellular glycoprotein associated with cardiovascular development.EMILIN2 was identified with cells and extracellular matrix by immunohistochemistry in the carotid and aorta.These results suggest EMILIN2 could play a role in thrombosis as a constituent of the vessel wall and/or a component of the thrombus.

View Article: PubMed Central - HTML - PubMed

Affiliation: Joseph 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.

ABSTRACT

Background: Elastin microfibril interface located protein 2 (EMILIN2) is an extracellular glycoprotein associated with cardiovascular development. While other EMILIN proteins are reported to play a role in elastogenesis and coagulation, little is known about EMILIN2 function in the cardiovascular system. The objective of this study was to determine whether EMILIN2 could play a role in thrombosis.

Results: EMILIN2 mRNA was expressed in 8 wk old C57BL/6J mice in lung, heart, aorta and bone marrow, with the highest expression in bone marrow. In mouse cells, EMILIN2 mRNA expression in macrophages was higher than expression in endothelial cells and fibroblasts. EMILIN2 was identified with cells and extracellular matrix by immunohistochemistry in the carotid and aorta. After carotid ferric chloride injury, EMILIN2 was abundantly expressed in the thrombus and inhibition of EMILIN2 increased platelet de-aggregation after ADP-stimulated platelet aggregation.

Conclusions: These results suggest EMILIN2 could play a role in thrombosis as a constituent of the vessel wall and/or a component of the thrombus.

No MeSH data available.


Related in: MedlinePlus