The intravascular actin scavenger system depolymerizes and sequesters actin released after tissue injury. Studies were carried out to determine if this system is active in the extracellular space during wound repair. Using burn wound fluid as a noninvasive means for analyzing the wound environment, we measured actin accumulation and actin complex formation with the plasma proteins responsible for scavenger function. Actin at concentrations as high as 0.25 mg/ml ( approximately 5 micromol/L) was found in burn wound fluid samples from 9 of 11 patients. Wound fluid also contained the two plasma proteins that bind actin-gelsolin (both plasma and cytoplasmic forms) and Gc protein. Because actin in wound fluid was complexed with gelsolin and Gc protein, we conclude that the components of the actin scavenger system are functional in wound tissue. In addition, proteolysis of gelsolin, but not actin or Gc protein, appeared to occur at the wound site. Gelsolin proteolysis was accompanied by the appearance of 49 kd gelsolin fragments, and wound fluid samples lacking intact gelsolin also contained high metalloproteinase levels.