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Proceedings Paper

Argon Laser Welding Induces Degradation And Crosslinking Of Extracellular Matrix Protein: A Preliminary Report
Author(s): Lyndon Su; Louann W. Murray; Rodney A. White; George Kopchok; Carol Guthrie; Geoffrey H. White
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Paper Abstract

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.

Paper Details

Date Published: 11 September 1989
PDF: 9 pages
Proc. SPIE 1066, Laser Surgery: Advanced Characterization, Therapeutics, and Systems, (11 September 1989); doi: 10.1117/12.952030
Show Author Affiliations
Lyndon Su, UCLA Medical Center (United States)
Louann W. Murray, UCLA Medical Center (United States)
Rodney A. White, UCLA Medical Center (United States)
George Kopchok, UCLA Medical Center (United States)
Carol Guthrie, UCLA Medical Center (United States)
Geoffrey H. White, UCLA Medical Center (United States)


Published in SPIE Proceedings Vol. 1066:
Laser Surgery: Advanced Characterization, Therapeutics, and Systems
Kazuhiko Atsumi; Norman R. Goldblatt; Stephen N. Joffe, Editor(s)

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