A synthetic peptide representing the thrombin receptor-binding domain enhances wound closure in vivo.
Our studies of alpha-thrombin as a growth factor have led to the development of a synthetic peptide (p508) that in vitro competes with thrombin for binding to high affinity receptors, and enhances mitogenic activity. To determine if this peptide could be used to accelerate wound closure in vivo, full thickness 6 mm dermal biopsy wounds on the dorsal skin of anesthetized rats were treated with p508 peptide, thrombin or PBS as control. At day 7, the p508 treated wound areas were 20% to 50% smaller than either thrombin or PBS treated wound sites. This suggests that p508 enhances aspects of wound healing, and avoids the normal in vivo regulatory mechanisms of intact thrombin.
Pernia
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Department of Human Biological Chemistry & Genetics, University of Texas Medical Branch, Galveston 77550.
Berry
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Redin
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Carney
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DH
D000818:Animals; D008297:Male; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism / Q000494:pharmacology*; D011897:Random Allocation; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism; D018179:Receptors, Thrombin; D012867:Skin / Q000187:drug effects; D013917:Thrombin / Q000378:metabolism / Q000494:pharmacology*; D014945:Wound Healing / Q000187:drug effects*
D010455:Peptides; D011956:Receptors, Cell Surface; D018179:Receptors, Thrombin; D013917:Thrombin