1004-59 Vascular Acoustic Emissions During Angioplasty: Potential Role in Identification of Induced Dissection

A fundamental mechanism of balloon angioplasty (BA) is plaque rupture. Rupture leading to dissection, however, has been implicated as an underlyIng factor responsible for both acute and chronic adverse outcomes. Acoustic emissions (AE) — transient sound waves generated by microstructural alterations of a material subjected to mechanical stress — may provide a novel means of characterizing BA-induced tissue trauma. Using a novel acoustic sensor system, we examined the relationship between cumulative AE energy released by human arterial tissue during BA and the observed pathologic injury. Post-mortem human arterial specimens (19) were subjected to identical SA with simultaneous monitoring of intraluminal pressure and AE. Sound energy was integrated throughout the pressurization period to obtain an estimate of the cumulative AE energy released during dilatation. Postangioplasty inspection revealed a marked difference in AE energy released by specimens that experienced traumatic dissection vs. non-dissection dilatation:Sound energy released by vascular tissue undergoing balloon angioplasty discriminates dissection from non-dissection tissue trauma. Given the deleterious role that dissection can play in SA, this novel system may provide a means of improving procedural outcome

Defective α2antiplasmin cross-linking and thrombus stability in a case of acquired factor XIII deficiency

This work was supported by grants FS/11/2/28579 (N.J.M) and from the British Heart Foundation and by the University of Aberdeen Development Trust (J.L.M) and Friends of Anchor (N.J.M & J.L.M).Peer reviewedPostprin

Influence of a natural and a synthetic inhibitor of factor XIIIa on fibrin clot rheology

We investigated the origins of greater clot rigidity associated with FXIIIa-dependent cross-linking. Fibrin clots were examined in which cross-linking was controlled through the use of two inhibitors: a highly specific active-center-directed synthetic inhibitor of FXIIIa, 1,3-dimethyl-4,5-diphenyl-2[2(oxopropyl)thio]imidazolium trifluoromethylsulfonate, and a patient-derived immunoglobulin directed mainly against the thrombin-activated catalytic A subunits of thrombin-activated FXIII. Cross-linked fibrin chains were identified and quantified by one- and two-dimensional gel electrophoresis and immunostaining with antibodies specific for the alpha- and gamma-chains of fibrin. Gamma-dimers, gamma-multimers, alpha(n)-polymers, and alpha(p)gamma(q)-hybrids were detected. The synthetic inhibitor was highly effective in preventing the production of all cross-linked species. In contrast, the autoimmune antibody of the patient caused primarily an inhibition of alpha-chain cross-linking. Clot rigidities (storage moduli, G') were measured with a cone and plate rheometer and correlated with the distributions of the various cross-linked species found in the clots. Our findings indicate that the FXIIIa-induced dimeric cross-linking of gamma-chains by itself is not sufficient to stiffen the fibrin networks. Instead, the augmentation of clot rigidity was more strongly correlated with the formation of gamma-multimers, alpha(n)-polymers, and alpha(p)gamma(q)-hybrid cross-links. A mechanism is proposed to explain how these cross-linked species may enhance clot rigidity