Dipeptidyl peptidase IV and aminopeptidase in burn wound exudates: implications for wound healing.
Two catalytically active proteases, dipeptidyl peptidase IV (DP IV) and aminopeptidase (AP), not previously reported as present in burn wound exudates, have been identified by substrate specificity and susceptibility to known enzyme inhibitors. The ratio of the two enzymes in exudates is significantly different from the ratio in plasma collected from the same patient during the same time interval, suggesting that measurement of exudate components may be more significant than plasma activities in evaluating local conditions in the wound. A number of biologically significant substances are DP IV substrates, and the list can be considerably extended by the sequential action of AP and DP IV. Some polypeptides are converted to their biologically active form by DP IV action, while others are degraded to inactive forms. Either action generates X-Pro dipeptides, which have a demonstrably beneficial effect on wound healing. Although not resolved by molecular sizing or anion exchange chromatography, DP IV and AP in a burn wound exudate were purified by affinity chromatography.
Prager
M D
MD
Department of Surgery, University of Texas Southwestern Medical Center, Dallas 75235-9031.
Sabeh
F
F
Baxter
C R
CR
Atiles
L
L
Hartline
B
B
D000328:Adult; D000368:Aged; D000626:Aminopeptidases / Q000032:analysis*; D002056:Burns / Q000201:enzymology*; D002846:Chromatography, Affinity; D018819:Dipeptidyl Peptidase 4; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000032:analysis*; D005122:Exudates and Transudates / Q000201:enzymology*; D006801:Humans; D008297:Male; D008875:Middle Aged; D014945:Wound Healing / Q000502:physiology*
D000626:Aminopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D018819:Dipeptidyl Peptidase 4