11 September 1989 Argon Laser Welding Induces Degradation And Crosslinking Of Extracellular Matrix Protein: A Preliminary Report
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Extracellular matrix components from untreated and laser-welded skin and blood vessels were extracted with guanidine hydrochloride and separated by SDS polyacrylamide gel electrophoresis. When compared to matched, untreated tissues, protein electrophoretic profiles from laser-treated samples showed several changes. In both tissue types, the concentration of a protein normally migrating between alpha and beta chains of type I collagen decreased in laser-treated samples. However, laser-treated blood vessels showed significantly more low molecular weight protein, whereas significantly more high molecular weight protein appeared in laser-treated skin samples when compared to untreated tissue. These results suggest that the argon laser either degrades or crosslinks proteins in-vivo. Laser induced protein crosslinks may be the biochemical basis of laser welding.
© (1989) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Lyndon Su, Lyndon Su, Louann W. Murray, Louann W. Murray, Rodney A. White, Rodney A. White, George Kopchok, George Kopchok, Carol Guthrie, Carol Guthrie, Geoffrey H. White, Geoffrey H. White, } "Argon Laser Welding Induces Degradation And Crosslinking Of Extracellular Matrix Protein: A Preliminary Report", Proc. SPIE 1066, Laser Surgery: Advanced Characterization, Therapeutics, and Systems, (11 September 1989); doi: 10.1117/12.952030; https://doi.org/10.1117/12.952030


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