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 journalArticle

    2 Citations (Scopus)


    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 languageEnglish
    Pages (from-to)71-79
    Number of pages9
    JournalProceedings of SPIE - The International Society for Optical Engineering
    Publication statusPublished - 11 Sep 1989

    Fingerprint Dive into the research topics of 'Argon laser welding induces degradation and crosslinking of extracellular matrix protein: A preliminary report'. Together they form a unique fingerprint.

  • Cite this