title: Localization of mRNAs representing collagenase and TIMP in sections of healing human burn wounds.
abstract: Interstitial collagenase, a matrix metalloproteinase, is known to be actively involved in remodeling of cutaneous tissues including those affected by trauma, neoplasia, and inflammation. Conversely, collagenase activity is blocked by tissue inhibitor of metalloproteinases (TIMP). Because both collagenase and TIMP are rapidly secreted into the extracellular matrix, their sites of synthesis remain ambiguous. To determine the site and sequence of collagenase and TIMP expression in cutaneous wound repair, we examined partial and full thickness excisions of human burn wounds representing days 2 to 34 postinjury. Prominent labeling for collagenase and TIMP was detected in epithelial cells at the burn margin and at the edges of surviving hair follicles and eccrine sweat structures in the wound bed. Within the dermis, cells expressing collagenase and TIMP were at first perivascular in location and later appeared at the interface zone between viable and nonviable dermis. A diversity of cell types including macrophages, fibroblasts, endothelial cells, and keratinocytes appeared to express mRNAs for collagenase and TIMP. Little if any labeling was detected in necrotic regions, in adjacent nonwounded dermis, or epidermis. Our data indicate that collagenase and TIMP are temporally and spatially regulated during cutaneous wound repair.
authors.affiliation: Department of Medicine (Dermatology), Vanderbilt University School of Medicine, Nashville, Tennessee.
authors.forename: G P
authors.initials: GP
authors.lastname: Stricklin
authors.forename: L
authors.initials: L
authors.lastname: Li
authors.forename: V
authors.initials: V
authors.lastname: Jancic
authors.forename: B A
authors.initials: BA
authors.lastname: Wenczak
authors.forename: L B
authors.initials: LB
authors.lastname: Nanney
mesh_terms: D000293:Adolescent; D000328:Adult; D000368:Aged; D001483:Base Sequence; D002056:Burns / Q000201:enzymology* / Q000473:pathology / Q000503:physiopathology*; D002648:Child; D002675:Child, Preschool; D017364:Collagenases / Q000032:analysis / Q000235:genetics*; D005260:Female; D005347:Fibroblasts / Q000737:chemistry / Q000201:enzymology / Q000473:pathology; D006023:Glycoproteins / Q000032:analysis / Q000235:genetics*; D006801:Humans; D017403:In Situ Hybridization; D007223:Infant; D008264:Macrophages / Q000737:chemistry / Q000201:enzymology / Q000473:pathology; D008297:Male; D008875:Middle Aged; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000032:analysis* / Q000235:genetics; D012867:Skin / Q000737:chemistry / Q000201:enzymology / Q000473:pathology; D013997:Time Factors; D019714:Tissue Inhibitor of Metalloproteinases; D014945:Wound Healing / Q000235:genetics* / Q000502:physiology
chemical_list: D006023:Glycoproteins; D012333:RNA, Messenger; D019714:Tissue Inhibitor of Metalloproteinases; D017364:Collagenases