A novel role of h2‐calponin in regulating whole blood thrombosis and platelet adhesion during physiologic flow

Calponin is an actin filament‐associated protein reported in platelets, although the specific isoform expressed and functional role were not identified. The h2‐calponin isoform is expressed in myeloid‐derived peripheral blood monocytes, where it regulates adhesion. Our objective was to characterize...

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Bibliographic Details
Published in:Physiological reports 2014-12, Vol.2 (12), p.e12228-n/a
Main Authors: Hines, Patrick C., Gao, Xiufeng, White, Jennell C., D'Agostino, Ashley, Jin, Jian‐Ping
Format: Article
Language:English
Subjects:
Actin
Bleeding
Blood platelets
Calponin
Collagen
Cytoskeleton
Hemostasis
Localization
Microfluidics
Monocytes
Original Research
Peripheral blood
Phosphorylation
Physiology
Platelets
Proteins
shear
Thrombosis
Western blotting
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Summary:Calponin is an actin filament‐associated protein reported in platelets, although the specific isoform expressed and functional role were not identified. The h2‐calponin isoform is expressed in myeloid‐derived peripheral blood monocytes, where it regulates adhesion. Our objective was to characterize the presence and function of the h2 isoform of calponin in platelets. H2‐calponin was detected in human and mouse platelets via Western blotting. Immunofluorescent staining demonstrated h2‐calponin and actin colocalized in both human and wild‐type mouse platelets at rest and following collagen activation. The kinetics of platelet adhesion and whole blood thrombosis during physiologic flow was evaluated in a microfluidic flow‐based thrombosis assay. The time to initiation of rapid platelet/thrombus accumulation (lag time) was significantly longer in h2‐calponin knockout versus wild‐type mouse blood (130.02 ± 3.74 sec and 72.95 ± 16.23 sec, respectively, P 
ISSN:2051-817X
2051-817X
DOI:10.14814/phy2.12228