Murray L W, Su L, Kopchok G E, White R A
Department of Pediatrics, Harbor/UCLA Medical Center, Torrance 90509.
Lasers Surg Med. 1989;9(5):490-6. doi: 10.1002/lsm.1900090512.
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.
为了阐明组织激光焊接的生化机制，我们将氩激光处理过的标本的蛋白质谱与对照进行了比较。用盐酸胍提取未处理和激光焊接的皮肤及血管的细胞外基质成分，并通过SDS聚丙烯酰胺凝胶电泳进行分离。与匹配的未处理组织相比，激光处理样本的蛋白质电泳谱显示出一些变化。在这两种组织类型中，氩激光处理均降低了一种迁移于I型胶原α链和β链之间的235 kd蛋白质的浓度。与对照组织相比，激光处理的血管在染料前沿显示出明显更多的低分子量蛋白质，而与未处理组织相比，激光处理的皮肤样本中出现了明显更多的高分子量蛋白质。这些结果表明，氩激光可能在体内降解或交联蛋白质。激光诱导的蛋白质交联可能是氩激光焊接的生化基础。
