Profiles of matrix metalloproteinases and their tissue inhibitors in intraperitoneal drainage fluid: Relationship to wound healing

被引:48
作者
Baker, EA [1 ]
Leaper, DJ [1 ]
机构
[1] Univ Hosp N Tees, Professorial Unit Surg, Stockton On Tees TS19 8PE, England
关键词
D O I
10.1046/j.1524-475X.2003.11406.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Matrix degradation and remodeling occurs during wound healing, thereby aiding tissue repair, angiogenesis, and cell migration. It is dependent on the balance between proteinases and their inhibitors, namely the matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Acute wound fluid samples (n = 58 patients) were collected daily from the intraperitoneal drain placed after colorectal surgery from the first postoperative day until drain removal. Three laboratory techniques were performed: enzyme linked immunosorbent assays (MMP-1, MMP-3, TIMP-1, TIMP-2), gelatinase activity assays (MMP-2, MMP-9), and quenched fluorescent substrate hydrolysis (total MMP activity). Levels were correlated with each postoperative day, wound healing, and surgical outcome (p < 0.05, Spearman's correlation). Significant negative (MMP-9, MMP-3, MMP-8, TIMP-2, total MMP activity) and positive (MMP-2, TIMP-1) correlations were observed with the postoperative day, e.g., total MMP-9: day 1, median, 121 (range, 12-189) ng/ml; day 3, 46 (8-179); day 5, 31 (0-155), day 7, 20 (6-58). Differences were also observed with the type of operation, estimated blood loss, and length of operation and with postoperative complications. MMPs and TIMPs are involved in wound healing after elective colorectal cancer surgery and their levels in drain fluid may act as markers of wound healing and surgical outcome.
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页码:268 / 274
页数:7
相关论文
共 29 条
[1]   MATRIX METALLOPROTEINASES - A REVIEW [J].
BIRKEDALHANSEN, H ;
MOORE, WGI ;
BODDEN, MK ;
WINDSOR, LJ ;
BIRKEDALHANSEN, B ;
DECARLO, A ;
ENGLER, JA .
CRITICAL REVIEWS IN ORAL BIOLOGY & MEDICINE, 1993, 4 (02) :197-250
[2]   TISSUE INHIBITOR OF METALLOPROTEINASES-1 IS DECREASES AND ACTIVATED GELATINASES ARE INCREASED IN CHRONIC WOUNDS [J].
BULLEN, EC ;
LONGAKER, MT ;
UPDIKE, DL ;
BENTON, R ;
LADIN, D ;
HOU, ZZ ;
HOWARD, EW .
JOURNAL OF INVESTIGATIVE DERMATOLOGY, 1995, 104 (02) :236-240
[3]  
COTTAM DW, 1993, INT J ONCOL, V2, P861
[4]   MATRIX-DEGRADING METALLOPROTEINASES [J].
ENNIS, BW ;
MATRISIAN, LM .
JOURNAL OF NEURO-ONCOLOGY, 1994, 18 (02) :105-109
[5]   Proteolysis in colorectal cancer [J].
Garbett, EA ;
Reed, MWR ;
Brown, NJ .
JOURNAL OF CLINICAL PATHOLOGY-MOLECULAR PATHOLOGY, 1999, 52 (03) :140-145
[6]  
Gomez DE, 1997, EUR J CELL BIOL, V74, P111
[7]   Expression and activity of matrix metalloproteinase-2 and-9 in experimental granulation tissue [J].
Inkinen, K ;
Turakainen, H ;
Wolff, H ;
Ravanti, L ;
Kähäri, VM ;
Ahonen, J .
APMIS, 2000, 108 (05) :318-328
[8]   COLLAGENASE EXPRESSION IS RAPIDLY INDUCED IN WOUND-EDGE KERATINOCYTES AFTER ACUTE INJURY IN HUMAN SKIN, PERSISTS DURING HEALING, AND STOPS AT REEPITHILIALIZATION [J].
INOUE, M ;
KRATZ, G ;
HAEGERSTRAND, A ;
STAHLEBACKDAHL, M .
JOURNAL OF INVESTIGATIVE DERMATOLOGY, 1995, 104 (04) :479-483
[9]   A NOVEL COUMARIN-LABELED PEPTIDE FOR SENSITIVE CONTINUOUS ASSAYS OF THE MATRIX METALLOPROTEINASES [J].
KNIGHT, CG ;
WILLENBROCK, F ;
MURPHY, G .
FEBS LETTERS, 1992, 296 (03) :263-266
[10]   Matrix metalloproteinases (MMPs) and their physiological inhibitors (TIMPs) are differentially expressed during excisional skin wound repair [J].
Madlener, M ;
Parks, WC ;
Werner, S .
EXPERIMENTAL CELL RESEARCH, 1998, 242 (01) :201-210