Journal
MOLECULAR AND CELLULAR BIOCHEMISTRY
Volume 307, Issue 1-2, Pages 13-22Publisher
SPRINGER
DOI: 10.1007/s11010-007-9579-2
Keywords
albumin; alpha(5)beta 1 integrin; ERK; F-actin; intercellular adhesion molecule-1
Categories
Funding
- NHLBI NIH HHS [HL74185, HL71010, HL88012, R01 HL088012, HL80394, R01 HL071010, R01 HL080394, R01 HL080394-03, R01 HL074185, R01 HL080394-02] Funding Source: Medline
- NINDS NIH HHS [R01 NS051568, NS51568] Funding Source: Medline
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL080394, R01HL074185, R01HL088012, R01HL071010] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS051568] Funding Source: NIH RePORTER
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Many cardiovascular and cerebrovascular disorders are accompanied by an increased blood content of fibrinogen (Fg), a high molecular weight plasma adhesion protein. Fg is a biomarker of inflammation and its degradation products have been associated with microvascular leakage. We tested the hypothesis that at pathologically high levels, Fg increases endothelial cell (EC) permeability through extracellular signal regulated kinase (ERK) signaling and by inducing F-actin formation. In cultured ECs, Fg binding to intercellular adhesion molecule-1 and to alpha(5)beta(1) integrin, caused phosphorylation of ERK. Subsequently, F-actin formation increased and coincided with formation of gaps between ECs, which corresponded with increased permeability of ECs to albumin. Our data suggest that formation of F-actin and gaps may be the mechanism for increased albumin leakage through the EC monolayer. The present study indicates that elevated un-degraded Fg may be a factor causing microvascular permeability that typically accompanies cardiovascular and cerebrovascular disorders.
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