title: Strength and Persistence of Energy-Based Vessel Seals Rely on Tissue Water and Glycosaminoglycan Content.
abstract: Vessel ligation using energy-based surgical devices is steadily replacing conventional closure methods during minimally invasive and open procedures. In exploring the molecular nature of thermally-induced tissue bonds, novel applications for surgical resection and repair may be revealed. This work presents an analysis of the influence of unbound water and hydrophilic glycosaminoglycans on the formation and resilience of vascular seals via: (a) changes in pre-fusion tissue hydration, (b) the enzymatic digestion of glycosaminoglycans (GAGs) prior to fusion and (c) the rehydration of vascular seals following fusion. An 11% increase in pre-fusion unbound water led to an 84% rise in vascular seal strength. The digestion of GAGs prior to fusion led to increases of up to 82% in seal strength, while the rehydration of native and GAG-digested vascular seals decreased strengths by 41 and 44%, respectively. The effects of increased unbound water content prior to fusion combined with the effects of seal rehydration after fusion suggest that the heat-induced displacement of tissue water is a major contributor to tissue adhesion during energy-based vessel sealing. The effects of pre-fusion GAG-digestion on seal integrity indicate that GAGs are inhibitory to the bond formation process during thermal ligation. GAG digestion may allow for increased water transport and protein interaction during the fusion process, leading to the formation of stronger bonds. These findings provide insight into the physiochemical nature of the fusion bond, its potential for optimization in vascular closure and its application to novel strategies for vascular resection and repair.
authors.affiliation: Department of Mechanical Engineering, University of Colorado at Boulder, 1111 Engineering Drive; UCB 427, Boulder, CO, 80309, USA. eric.kramer@colorado.edu.
authors.forename: Eric A
authors.initials: EA
authors.lastname: Kramer
authors.affiliation: Department of Mechanical Engineering, University of Colorado at Boulder, 1111 Engineering Drive; UCB 427, Boulder, CO, 80309, USA.
authors.forename: James D
authors.initials: JD
authors.lastname: Cezo
authors.affiliation: Department of Mechanical Engineering, University of Colorado at Boulder, 1111 Engineering Drive; UCB 427, Boulder, CO, 80309, USA.
authors.forename: Douglas P
authors.initials: DP
authors.lastname: Fankell
authors.affiliation: ConMed Corporation, 14603 E Fremont Ave, Centennial, CO, 80112, USA.
authors.forename: Kenneth D
authors.initials: KD
authors.lastname: Taylor
authors.affiliation: Department of Mechanical Engineering, University of Colorado at Boulder, 1111 Engineering Drive; UCB 427, Boulder, CO, 80309, USA.
authors.forename: Mark E
authors.initials: ME
authors.lastname: Rentschler
authors.affiliation: Department of Mechanical Engineering, University of Colorado at Boulder, 1111 Engineering Drive; UCB 427, Boulder, CO, 80309, USA.
authors.forename: Virginia L
authors.initials: VL
authors.lastname: Ferguson
mesh_terms: D000818:Animals; D006025:Glycosaminoglycans / Q000737:chemistry* / Q000378:metabolism; D008026:Ligation; D013157:Splenic Artery / Q000737:chemistry* / Q000378:metabolism / Q000601:surgery; D013552:Swine; D014867:Water / Q000737:chemistry* / Q000378:metabolism
chemical_list: D006025:Glycosaminoglycans; C020341:glucosaminoglycans; D014867:Water
keywords: Collagen; Denaturation; Glycosaminoglycans; Ligation; Thermal; Tissue welding