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1
* Department of Pathology,
Medicine and
Radiation Oncology, Duke University Medical Center, Durham, North Carolina 27710, USA
1Correspondence: Box 2603, MSRB, DUMC, Durham, NC 27710, USA. E-mail: green032{at}mc.duke.edu
Tissue transglutaminase (TG) is an enzyme that stabilizes the structure
of tissues by covalently ligating extracellular matrix molecules.
Expression and localization of TG are not well established during wound
healing. We performed punch biopsy wounds on anesthetized rats and
monitored the wound healing process by histological and
immunohistochemical methods. The TG antigen and activity are expressed
at sites of neovascularization in the provisional fibrin matrix within
24 h of wounding. Endothelial cells, macrophages, and skeletal
muscle cells expressed TG throughout the healing process. The TG
antigen within the wound was active in vivo based on the
detection of isopeptide bonds. The TG antigen increased four- to
fivefold by day 3 postwounding and was proteolytically degraded. TG
expression occurred in association with TGF-ß, TNF-
, IL-6, and
VEGF production in the wound. Recombinant TG increased vessel length
density (a measure of angiogenesis) when applied topically in rat
dorsal skin flap window chambers. We have established that TG is an
important tissue stabilizing enzyme that is active during wound healing
and can function to promote angiogenesis.—Haroon, Z. A.,
Hettasch, J. M., Lai, T.-S., Dewhirst, M. W., Greenberg,
C. S. Tissue transglutaminase is expressed, active, and directly
involved in rat dermal wound healing and angiogenesis.
Key Words: tissue repair • extracellular matrix • cross-linking • endothelial cells • TGF-ß
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