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  • Mechanical characterization of thromboemboli in acute ischemic stroke and laboratory embolus analogs.

Mechanical characterization of thromboemboli in acute ischemic stroke and laboratory embolus analogs.

AJNR. American journal of neuroradiology (2011-05-21)
J Y Chueh, A K Wakhloo, G H Hendricks, C F Silva, J P Weaver, M J Gounis
ZUSAMMENFASSUNG

Mechanical behavior of the thromboembolus is one of the key factors that determine the efficacy of thrombectomy devices for revascularization in AIS. We characterized the mechanical properties and composition of thromboemboli from clinical cases and compared them with commonly used EAs. Thromboemboli were obtained from patients with AIS by using aspiration devices and from carotid atherosclerotic plaques harvested during endarterectomy. In the laboratory, common EAs were created by varying blood donor species (human, porcine, and bovine), thrombin concentration, and presence of barium sulfate. Stiffness and elasticity of the specimens were measured with DMA. Scanning electron microscopy and histology were used to investigate the ultrastructure and composition of all specimens. Red thromboemboli from patients composed mainly of fibrin and erythrocytes were much softer than the calcified and cholesterol-rich material. Of the EAs created in the laboratory, those made from bovine blood presented the highest stiffness that was independent of thrombin concentration. Addition of thrombin increased the stiffness and elasticity of human and porcine EAs (P < .05). The presence of barium sulfate significantly reduced the elasticity of all EAs (P < .05). Endovascular device testing and development requires realistic EAs. The stiffness and elasticity of the cerebral thromboemboli analyzed in this study were closely matched by recalcified porcine EAs and thrombin-induced human EAs. Stiffness of the thrombus extracted from carotid endarterectomy specimens was similar with that of the thrombin-induced bovine and porcine EAs.

MATERIALIEN
Produktnummer
Marke
Produktbeschreibung

Sigma-Aldrich
Thrombin aus Rinderplasma, lyophilized powder, ≥2,000 NIH units/mg protein (E1%/280 = 19.5)