Collagen synthesis in intact skin is suppressed during wound healing

Simultaneous monitoring of total collagen synthesis as well as synthesis in intact skin and in the wound to verify the higher priority of wound healing after surgery. Synthesis of acute phase proteins is stimulated by surgical trauma. At the same time, production of albumin is inhibited and there is a net catabolism of skeletal muscle proteins. Similarly, the authors have found a transient inhibition of total collagen synthesis after surgery. The authors hypothesized a lower priority in synthesis of structural and peripheral collagen for the benefit of wound healing. The concentrations of the carboxyterminal propeptide of type I procollagen (PICP) and the aminoterminal propeptide of type III procollagen (PIIINP) were measured in suction blister fluid of intact skin and in wound fluid in ten surgical patients. PICP and PIIINP concentrations in serum were also measured. Specific radioimmunoassays were used. In peripheral skin, the median preoperative concentrations of PICP and PIIINP were 228 and 140 micrograms/L, respectively. On postoperative days 1, 2, 4 and 7, the median concentration of PICP was 145 (p = 0.01, Wilcoxon signed rank sum test), 102 (0.02), 159 (0.03), and 152 (0.06) micrograms/L, respectively. The postoperative medians of PIIINP were 68 (p = 0.17), 76 (0.04), 66 (0.06), and 56 (0.03) micrograms/L, respectively. At the same time, collagen synthesis in the wound increased dramatically from the second day on. After an initial decrease, propeptide concentrations in serum gradually increased from the fourth day on. Collagen synthesis is regulated for the benefit of the wound during the acute phase response.