Premium
Crosslinking of extracellular matrix proteins: A preliminary report on a possible mechanism of argon laser welding
Author(s) -
Murray Louann W.,
Su Lyndon,
Kopchok George E.,
White Rodney A.
Publication year - 1989
Publication title -
lasers in surgery and medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.888
H-Index - 112
eISSN - 1096-9101
pISSN - 0196-8092
DOI - 10.1002/lsm.1900090512
Subject(s) - extracellular matrix , mechanism (biology) , argon , welding , laser , chemistry , matrix (chemical analysis) , extracellular , biophysics , materials science , composite material , biochemistry , biology , optics , organic chemistry , physics , quantum mechanics
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.