Acceleration of soft tissue repair by a thrombin-derived oligopeptide

Douglas T. Cromack, Beatriz H. Porras-Reyes, Sung Shin Wee, Kevin C. Glenn, James A. Purdy, Darrell H. Carney, Thomas A. Mustoe

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Augmentation of thrombin-modulated chemotaxis and mitogenic activity within the early phase of soft tissue repair is now possible. Identification of high-affinity thrombin receptor binding domains within thrombin has enabled the synthesis of a family of peptides which interact with thrombin receptors and enhance in vitro mitogenesis. A single (5.0 μg/wound) application of the thrombin receptor-activating peptide (P517-30) significantly increased wound breaking strength from Day 5 (31% over controls) to Day 12. Two models of impaired healing created by radiotherapy (RT) were used to elucidate possible mechanisms of P517-30 action. Although P517-30 did not completely overcome the RT-induced healing impairments, it increased breaking strength under conditions of penetrating whole body RT-induced pancytopenia by 22% and of nonpenetrating surface RT-induced dermal cell damage by 42%. This suggests that P517-30 directly stimulates resident endothelial cells, fibroblasts, or other cells to overcome dermal and circulating monocytic deficits. These results suggest a method to accelerate wound healing with potential clinical applications and emphasize the activity of thrombin as a growth factor.

Original languageEnglish
Pages (from-to)117-122
Number of pages6
JournalJournal of Surgical Research
Volume53
Issue number2
DOIs
StatePublished - Aug 1992
Externally publishedYes

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    Cromack, D. T., Porras-Reyes, B. H., Wee, S. S., Glenn, K. C., Purdy, J. A., Carney, D. H., & Mustoe, T. A. (1992). Acceleration of soft tissue repair by a thrombin-derived oligopeptide. Journal of Surgical Research, 53(2), 117-122. https://doi.org/10.1016/0022-4804(92)90022-R