Argon laser welding induces degradation and crosslinking of extracellular matrix protein: A preliminary report

Lyndon Su; Louann W. Murray; Rodney A. White; George Kopchok; Carol Guthrie; Geoffrey H. White

doi:10.1117/12.952030

Argon laser welding induces degradation and crosslinking of extracellular matrix protein: A preliminary report

Lyndon Su, Louann W. Murray^*, Rodney A. White, George Kopchok, Carol Guthrie, Geoffrey H. White

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

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.

Original language	English
Pages (from-to)	71-79
Number of pages	9
Journal	Proceedings of SPIE - The International Society for Optical Engineering
Volume	1066
DOIs	https://doi.org/10.1117/12.952030
Publication status	Published - 11 Sept 1989

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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.",

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AU - Su, Lyndon

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AU - Kopchok, George

AU - Guthrie, Carol

AU - White, Geoffrey H.

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N2 - 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.

AB - 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.

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Argon laser welding induces degradation and crosslinking of extracellular matrix protein: A preliminary report

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