Wound fluids from human pressure ulcers contain elevated matrix metalloproteinase levels and activity compared to surgical wound fluids

被引:267
作者
Yager, DR
Zhang, LY
Liang, HX
Diegelmann, RF
Cohen, IK
机构
[1] Wound Healing Center, Div. of Plast. and Reconstr. Surgery, Medical College of Virginia, Richmond, VA
[2] Wound Healing Center, Box 980117, Richmond
关键词
collagenase; gelatinase; chronic wounds; C-14-collagen substrate;
D O I
10.1111/1523-1747.ep12365637
中图分类号
R75 [皮肤病学与性病学];
学科分类号
100206 ;
摘要
Fluid from acute surgical wounds and from nonhealing pressure ulcers was examined for the presence of several matrix metalloproteinases. Gelatin zymography demonstrated the presence of two major gelatinases with apparent molecular masses of 72 kDa and 92 kDa and two minor gelatinases with apparent mobilities of 68 kDa and 125 kDa, Antigen-specific sera identified the 72-kDa protein as matrix melloproteinase-2, The same sera also reacted with the 68-kDa protein, which is consistent with it being an activated form of matrix metalloproteinase-2, Antigen-specific sera identified the 92-kDa and 125-kDa proteins as matrix metalloproteinase-9, Levels of matrix metalloproteinase-2 and matrix metalloproteinase-9 were elevated more than 10-fold and 25-fold, respectively, in fluids from pressure ulcers compared with fluids from healing wounds, Examination of total potential and actual collagenolytic activity revealed that fluid from pressure ulcers contained significantly greater levels of both total and active collagenase compared with that of acute surgical wounds, In addition, an enzyme-linked immunosorbent assay demonstrated that fluids from pressure ulcers contained significantly more collagenase complexed with the inhibitor, tissue inhibitor of metalloproteinases. Together, these observations suggest that an imbalance exists between levels of matrix metalloproteinases and their inhibitors in the fluids of pressure ulcers and that this is primarily the result of elevated levels of the matrix metalloproteinases. The presence of excessive levels of activated forms of matrix-degrading enzymes at the wound surface of pressure ulcers may impede the healing of these wounds and may be relevant to the development of new rationales for treatment.
引用
收藏
页码:743 / 748
页数:6
相关论文
共 41 条
[1]   MATRIX METALLOPROTEINASE-2 IS AN INTERSTITIAL COLLAGENASE - INHIBITOR-FREE ENZYME CATALYZES THE CLEAVAGE OF COLLAGEN FIBRILS AND SOLUBLE NATIVE TYPE-I COLLAGEN GENERATING THE SPECIFIC 3/4-LENGTH AND 1/4-LENGTH FRAGMENTS [J].
AIMES, RT ;
QUIGLEY, JP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (11) :5872-5876
[2]   THE INVITRO RESPONSE OF FIBROBLASTS TO THE FLUID THAT ACCUMULATES UNDER A VAPOR-PERMEABLE MEMBRANE [J].
ALPER, JC ;
TIBBETTS, LL ;
SARAZEN, AA .
JOURNAL OF INVESTIGATIVE DERMATOLOGY, 1985, 84 (06) :513-515
[3]  
BERMAN M, 1983, INVEST OPHTH VIS SCI, V24, P1358
[4]   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
[5]   IMMUNOASSAYS FOR THE DETECTION OF HUMAN COLLAGENASE, STROMELYSIN, TISSUE INHIBITOR OF METALLOPROTEINASES (TIMP) AND ENZYME-INHIBITOR COMPLEXES [J].
COOKSLEY, S ;
HIPKISS, JB ;
TICKLE, SP ;
HOLMESIEVERS, E ;
DOCHERTY, AJP ;
MURPHY, G ;
LAWSON, ADG .
MATRIX, 1990, 10 (05) :285-291
[6]   DETERMINATION OF ENDOGENOUS CYTOKINES IN CHRONIC WOUNDS [J].
COOPER, DM ;
YU, EZ ;
HENNESSEY, P ;
KO, F ;
ROBSON, MC .
ANNALS OF SURGERY, 1994, 219 (06) :688-692
[7]   EVIDENCE FOR METALLOPROTEINASE AND METALLOPROTEINASE INHIBITOR IMBALANCE IN HUMAN OSTEOARTHRITIC CARTILAGE [J].
DEAN, DD ;
MARTELPELLETIER, J ;
PELLETIER, JP ;
HOWELL, DS ;
WOESSNER, JF .
JOURNAL OF CLINICAL INVESTIGATION, 1989, 84 (02) :678-685
[8]  
FINI ME, 1992, ACTA OPHTHALMOL, V70, P26
[9]   INTERSTITIAL COLLAGENASE IS REQUIRED FOR ANGIOGENESIS IN-VITRO [J].
FISHER, C ;
GILBERTSONBEADLING, S ;
POWERS, EA ;
PETZOLD, G ;
POORMAN, R ;
MITCHELL, MA .
DEVELOPMENTAL BIOLOGY, 1994, 162 (02) :499-510
[10]  
FREIJE JMP, 1994, J BIOL CHEM, V269, P16766