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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

EMILIN2 antibody inhibited mouse platelet aggregation. A, B, C. Platelet aggregation in platelet-rich plasma was induced by ADP and optically measured with an aggregometer. Platelets were pre-incubated with affinity purified rabbit anti-mouse EMILIN2 antibody (E185) or rabbit IgG as a control. A. Representative aggregation curves are shown. B. Quantification of aggregation results expressed as maximal amplitude of aggregation (mean ± SEM, n = 3-6). C. Quantification of platelet aggregation rate at 7 minutes after addition of ADP (mean ± SEM, n = 3-6). D. Representative platelet aggregation curves in platelet-rich plasma from B6-Chr17A/J mice. Concentrations of EMILIN2 antibody are indicated. Statistical differences between ADP or IgG and E185 were determined by ANOVA with a Newman-Kuels Multiple Comparison Test.
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Figure 4: EMILIN2 antibody inhibited mouse platelet aggregation. A, B, C. Platelet aggregation in platelet-rich plasma was induced by ADP and optically measured with an aggregometer. Platelets were pre-incubated with affinity purified rabbit anti-mouse EMILIN2 antibody (E185) or rabbit IgG as a control. A. Representative aggregation curves are shown. B. Quantification of aggregation results expressed as maximal amplitude of aggregation (mean ± SEM, n = 3-6). C. Quantification of platelet aggregation rate at 7 minutes after addition of ADP (mean ± SEM, n = 3-6). D. Representative platelet aggregation curves in platelet-rich plasma from B6-Chr17A/J mice. Concentrations of EMILIN2 antibody are indicated. Statistical differences between ADP or IgG and E185 were determined by ANOVA with a Newman-Kuels Multiple Comparison Test.

Mentions: The similar relative distribution of EMILIN2 and platelets in the thrombi suggested that EMILIN2 may regulate clot stability through a role in platelet aggregation. Pre-incubation of platelets with anti-EMILIN2 antibody inhibited the extent and rate of platelet aggregation induced by ADP (Figure 4A). Pre-incubation of platelets with EMILIN2 antibody inhibited the maximum amplitude of platelet aggregation by approximately 42% (Figure 4B). Moreover, the EMILIN2 antibody caused platelet de-aggregation in the presence of high ADP concentrations (20 μM) over induction time (Figure 4C). At 7 minutes after addition of 20 μM ADP, platelet de-aggregation in the presence of the antibody was inhibited by 90%. Inhibition of ADP-induced platelet aggregation by EMILIN2 antibody was dose dependent, with the highest inhibition achieved at 26 μg/ml (Figure 4D). These data suggest that EMILIN2 functions in stabilizing aggregated platelets.


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

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

EMILIN2 antibody inhibited mouse platelet aggregation. A, B, C. Platelet aggregation in platelet-rich plasma was induced by ADP and optically measured with an aggregometer. Platelets were pre-incubated with affinity purified rabbit anti-mouse EMILIN2 antibody (E185) or rabbit IgG as a control. A. Representative aggregation curves are shown. B. Quantification of aggregation results expressed as maximal amplitude of aggregation (mean ± SEM, n = 3-6). C. Quantification of platelet aggregation rate at 7 minutes after addition of ADP (mean ± SEM, n = 3-6). D. Representative platelet aggregation curves in platelet-rich plasma from B6-Chr17A/J mice. Concentrations of EMILIN2 antibody are indicated. Statistical differences between ADP or IgG and E185 were determined by ANOVA with a Newman-Kuels Multiple Comparison Test.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 4: EMILIN2 antibody inhibited mouse platelet aggregation. A, B, C. Platelet aggregation in platelet-rich plasma was induced by ADP and optically measured with an aggregometer. Platelets were pre-incubated with affinity purified rabbit anti-mouse EMILIN2 antibody (E185) or rabbit IgG as a control. A. Representative aggregation curves are shown. B. Quantification of aggregation results expressed as maximal amplitude of aggregation (mean ± SEM, n = 3-6). C. Quantification of platelet aggregation rate at 7 minutes after addition of ADP (mean ± SEM, n = 3-6). D. Representative platelet aggregation curves in platelet-rich plasma from B6-Chr17A/J mice. Concentrations of EMILIN2 antibody are indicated. Statistical differences between ADP or IgG and E185 were determined by ANOVA with a Newman-Kuels Multiple Comparison Test.
Mentions: The similar relative distribution of EMILIN2 and platelets in the thrombi suggested that EMILIN2 may regulate clot stability through a role in platelet aggregation. Pre-incubation of platelets with anti-EMILIN2 antibody inhibited the extent and rate of platelet aggregation induced by ADP (Figure 4A). Pre-incubation of platelets with EMILIN2 antibody inhibited the maximum amplitude of platelet aggregation by approximately 42% (Figure 4B). Moreover, the EMILIN2 antibody caused platelet de-aggregation in the presence of high ADP concentrations (20 μM) over induction time (Figure 4C). At 7 minutes after addition of 20 μM ADP, platelet de-aggregation in the presence of the antibody was inhibited by 90%. Inhibition of ADP-induced platelet aggregation by EMILIN2 antibody was dose dependent, with the highest inhibition achieved at 26 μg/ml (Figure 4D). These data suggest that EMILIN2 functions in stabilizing aggregated platelets.

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