Effective enzymatic debridement of burn wounds depends on the denaturation status of collagen
Effective enzymatic debridement of burn wounds depends on the denaturation status of collagen
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DOI：
10.1111/wrr.12827
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发表时间：
2020-06-22
影响因子：
2.9
通讯作者：
Boekema, Bouke K. H. L.
中科院分区：
文献类型：
--
作者：
Kwa, Kelly A. A.;van Haasterecht, Ludo;Boekema, Bouke K. H. L.
在我们的烧伤中心，通过使用菠萝蛋白酶的酶清创术治疗烧伤伤口已显示出有希望的结果。然而，在少数病例中，由于烧伤的病因是相对低温烧伤，因此清创术不充分。我们假设菠萝蛋白酶在其中胶原蛋白变性（其在大约65摄氏度下发生）尚未发生的烧伤中是无效的。我们的目的是评估胶原蛋白的变性和菠萝蛋白酶对不同温度的急性烧伤创面的清创能力之间是否存在关系。将来自四个不同供体的离体人皮肤切成1 × 1cm样品，并通过在40 ℃、50 ℃、60 ℃、70 ℃和100 ℃的温度下浸入水中20分钟来产生烧伤。用组织学、使用苏木精和伊红（H&E）染色和荧光标记的胶原杂交肽（CHP）以及用二次谐波发生（SHG）显微镜来评估胶原的变性。在应用酶清创术之前和之后，对烧伤样本和一个对照样本（室温）进行称重，以评估酶清创术的有效性。在酶促清创后，在加热至70 ℃和100 ℃的样品中观察到80%的重量减少，而其他样品显示出20%的减少。在加热至60 ℃或更高温度的样品中，观察到胶原蛋白展开、篮状组织排列丧失和坏死。在60 ℃、70 ℃和100 ℃的样品中观察到指示胶原变性的明显CHP荧光。70 ℃和100 ℃组的SHG强度显著降低（P
The treatment of burn wounds by enzymatic debridement using bromelain has shown promising results in our burn center. However, inadequate debridement occurred in a few cases in which the etiology of the burn was attributed to relatively low temperature burns. We hypothesized that bromelain is ineffective in burns in which collagen denaturation, which occurs approximately at 65 degrees C, has not taken place. Our objective was to assess whether there is a relationship between the denaturation of collagen and the ability of bromelain to debride acute scald burn wounds of different temperatures. Ex vivo human skin from four different donors was cut into 1x1 cm samples, and scald burns were produced by immersion in water at temperatures of 40 degrees C, 50 degrees C, 60 degrees C, 70 degrees C, and 100 degrees C for 20 minutes. Denaturation of collagen was assessed with histology, using hematoxylin and eosin (H&E) staining and a fluorescently labeled collagen hybridizing peptide (CHP), and with second harmonic generation (SHG) microscopy. Burned samples and one control sample (room temperature) were weighed before and after application of enzymatic debridement to assess the efficacy of enzymatic debridement. After enzymatic debridement, a weight reduction of 80% was seen in the samples heated to 70 degrees C and 100 degrees C, whereas the other samples showed a reduction of 20%. Unfolding of collagen, loss of basket-weave arrangement, and necrosis was seen in samples heated to 60 degrees C or higher. Evident CHP fluorescence, indicative of collagen denaturation, was seen in samples of 60 degrees C, 70 degrees C and 100 degrees C. SHG intensity, signifying intact collagen, was significantly lower in the 70 degrees C and 100 degrees C group (P