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Patterns of matrix metalloproteinase and TIMP‐1 expression in chronic and normally healing human cutaneous wounds
Author(s) -
VAALAMO M.,
WECKROTH M.,
PUOLAKKAINEN P.,
KERE J.,
SAARINEN P.,
LAUHARANTA J.,
SAARIALHOKERE U.K.
Publication year - 1996
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1046/j.1365-2133.1996.d01-932.x
Subject(s) - matrilysin , matrix metalloproteinase , wound healing , collagenase , in situ hybridization , medicine , plasminogen activator , interstitial collagenase , gelatinase a , pathology , urokinase , chronic wound , metalloproteinase , messenger rna , biology , immunology , surgery , enzyme , biochemistry , gene
Summary The present study was carried out to characterize the patterns of expression of matrix metalloproteinases or their tissue inhibitor (TIMP‐1) in normally healing, acute vs. chronic, skin wounds. In situ hybridization was performed to localize collagenase, stromelysin‐1, stromelysin‐2, matrilysin, urokinase plasminogen activator (uPA) and TIMP‐1 mRNAs in 14 chronic venous ulcers and 10 normally healing wounds, representing different time points after wounding. Surgical wounds, made in piglets harvested at several time points, were studied as controls. Collagenase, stromelysin‐1 and ‐2, as well as uPa, were expressed in keratinocytes in both acute and chronic wounds, while epithelial TIMP‐1 mRNA was not detected in any chronic wound biopsies studied. However, TIMP‐1 was expressed at the epithelial edges of both acute human and pig wounds. Our results suggest that the balance between metalloenzymes and their inhibitor TIMP‐1, is disturbed, in poorly healing wounds.