Crosslinking of extracellular matrix proteins: a preliminary report on a possible mechanism of argon laser welding.
In order to elucidate the biochemical mechanism of laser welding of tissues, we have compared protein profiles from argon laser-treated specimens with controls. 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 with matched, untreated tissues, protein electrophoretic profiles from laser-treated samples showed several changes. In both tissue types, argon laser treatment decreased the concentration of a 235 kd protein that migrates between the alpha and beta chains of type I collagen. Laser-treated blood vessels showed significantly more low molecular weight protein at the dye front than in control tissue, whereas significantly more high molecular weight protein appeared in laser-treated skin samples when compared with untreated tissue. These results suggest that the argon laser may either degrade or crosslink proteins in vivo. Laser-induced protein crosslinks may be the biochemical basis of argon laser welding.
Murray
L W
LW
Department of Pediatrics, Harbor/UCLA Medical Center, Torrance 90509.
Su
L
L
Kopchok
G E
GE
White
R A
RA
D000818:Animals; D001128:Argon; D001166:Arteriovenous Shunt, Surgical / Q000379:methods*; D003094:Collagen / Q000378:metabolism*; D004285:Dogs; D005109:Extracellular Matrix / Q000378:metabolism*; D005263:Femoral Artery / Q000378:metabolism / Q000601:surgery*; D005268:Femoral Vein / Q000378:metabolism / Q000601:surgery*; D005353:Fibronectins / Q000378:metabolism*; D006168:Guinea Pigs; D053685:Laser Therapy / Q000379:methods*; D013718:Tensile Strength; D014896:Welding / Q000379:methods*
D005353:Fibronectins; D001128:Argon; D003094:Collagen