Wound fluids from human pressure ulcers contain elevated matrix metalloproteinase levels and activity compared to surgical wound fluids
Wound fluids from human pressure ulcers contain elevated matrix metalloproteinase levels and activity compared to surgical wound fluids
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DOI：
10.1111/1523-1747.ep12365637
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发表时间：
1996-11-01
影响因子：
6.5
通讯作者：
Cohen, IK
中科院分区：
文献类型：
--
作者：
Yager, DR;Zhang, LY;Cohen, IK
检查了几种基质金属蛋白酶的存在，检查了急性手术伤口和非彻底压力溃疡的液体。明胶酶学证明存在两个主要明胶酶，具有明显的分子质量为72 kDa和92 kDa和两个次要明胶酶，明显的迁移率为68 kDa和125 kDa，抗原特异性血清，抗原特异性血清，将72-KDA蛋白鉴定为Matrix mellopropopoinase-2，是Matrix Melloprotototion-2，n newar同样的血清也与68 kDa蛋白反应，这是一致的它是基质金属蛋白酶2的活化形式，抗原特异性血清将92 kDa和125 kDa蛋白鉴定为基质金属蛋白酶9与愈合的液体相比伤口，检查总潜力和实际胶原式活性表明，与急性手术伤口相比，压力溃疡的液体含有明显更高的总和活性胶原酶水平，此外，酶联免疫吸附测定表明，酶联的免疫吸引力表明，含有压力溃疡的液体。与抑制剂，金属蛋白酶的组织抑制剂复合的胶原酶明显更多。总之，这些观察结果表明，基质金属蛋白酶及其抑制剂在压溃疡的液体中存在不平衡，这主要是基质金属蛋白酶水平升高的结果。在压力溃疡的伤口表面存在过多的激活形式的基质降解酶，可能会阻碍这些伤口的愈合，并且可能与新的治疗方法的发展有关。
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.