Bonding of articular cartilage using a combination of biochemical degradation and surface cross-linking.

Bonding of articular cartilage using a combination of biochemical degradation and surface cross-linking.
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DOI:
10.1186/ar2202
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发表时间:
2007
影响因子:
4.9
通讯作者:
Hammer J
Hammer J
中科院分区:
医学2区
文献类型:
--
作者:
Englert C;Blunk T;Müller R;von Glasser SS;Baumer J;Fierlbeck J;Heid IM;Nerlich M;Hammer J

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创伤后,关节软骨往往不愈合,由于不完全结合的骨折面。在这项研究中,我们研究了化学交联剂促进关节软骨结合的能力,无论是单独还是与表面降解剂预处理联合使用。从牛小腿股髌骨沟取关节软骨块。预处理后或未经预处理的两个软骨块在定制设计的腔室中部分相对组装并进行交联处理。随后,用粘连强度来测量软骨的粘合,即粘合软骨块破裂时的最大力除以重叠面积。在第一种方法中,仅用交联试剂(戊二醛、1-乙基-3-二氨基丙基-碳二亚胺(EDC)/ n -羟基琥珀酰亚胺(NHS)、吉尼平或转谷氨酰胺酶)处理后研究键合。实验进行了有或没有压缩的对立表面。交联过程中的压缩强烈增强了键合,特别是当应用EDC/NHS和戊二醛时。因此,所有进一步的实验都在压缩条件下进行。与单独使用交联剂相比,四种交联剂中的每一种与降解前处理(胃蛋白酶、胰蛋白酶和胍)的组合在键合方面有明显的改善。使用胃蛋白酶或胍与EDC/NHS的组合以及胍与戊二醛的组合获得了最高的粘合强度。测定了预处理后软骨块的细胞外基质成分,即糖胺聚糖和总胶原蛋白的释放量,但与测定的粘附强度没有直接关系。细胞毒性测定的所有物质,即表面降解剂和交联剂,使用瑞祖脲试验。考虑到胃蛋白酶和EDC/NHS治疗后良好的细胞活力以及胍和戊二醛的细胞毒性作用,胃蛋白酶和EDC/NHS联合治疗似乎是本研究中最有利的治疗方法。总之,关节软骨块的结合是通过使用交联试剂对其表面成分进行化学固定来实现的。压缩力的应用和表面结构的预先调制显著增强了软骨结合。酶治疗联合交联剂可能是当前关节软骨修复技术的一个有希望的补充。
After trauma, articular cartilage often does not heal due to incomplete bonding of the fractured surfaces. In this study we investigated the ability of chemical cross-linkers to facilitate bonding of articular cartilage, either alone or in combination with a pre-treatment with surface-degrading agents. Articular cartilage blocks were harvested from the femoropatellar groove of bovine calves. Two cartilage blocks, either after pre-treatment or without, were assembled in a custom-designed chamber in partial apposition and subjected to cross-linking treatment. Subsequently, bonding of cartilage was measured as adhesive strength, that is, the maximum force at rupture of bonded cartilage blocks divided by the overlap area. In a first approach, bonding was investigated after treatment with cross-linking reagents only, employing glutaraldehyde, 1-ethyl-3-diaminopropyl-carbodiimide (EDC)/N-hydroxysuccinimide (NHS), genipin, or transglutaminase. Experiments were conducted with or without compression of the opposing surfaces. Compression during cross-linking strongly enhanced bonding, especially when applying EDC/NHS and glutaraldehyde. Therefore, all further experiments were performed under compressive conditions. Combinations of each of the four cross-linking agents with the degrading pre-treatments, pepsin, trypsin, and guanidine, led to distinct improvements in bonding compared to the use of cross-linkers alone. The highest values of adhesive strength were achieved employing combinations of pepsin or guanidine with EDC/NHS, and guanidine with glutaraldehyde. The release of extracellular matrix components, that is, glycosaminoglycans and total collagen, from cartilage blocks after pre-treatment was measured, but could not be directly correlated to the determined adhesive strength. Cytotoxicity was determined for all substances employed, that is, surface degrading agents and cross-linkers, using the resazurin assay. Taking the favourable cell vitality after treatment with pepsin and EDC/NHS and the cytotoxic effects of guanidine and glutaraldehyde into account, the combination of pepsin and EDC/NHS appeared to be the most advantageous treatment in this study. In conclusion, bonding of articular cartilage blocks was achieved by chemical fixation of their surface components using cross-linking reagents. Application of compressive forces and prior modulation of surface structures enhanced cartilage bonding significantly. Enzymatic treatment in combination with cross-linkers may represent a promising addition to current techniques for articular cartilage repair.
DOI: 10.1002/art.10627
发表时间: 2002-12-01
影响因子: --
作者:
Chen, AC;Temple, MM;Sah, RL
通讯作者: Sah, RL
DOI: 10.1016/0142-9612(96)81413-x
发表时间: 1996-04-01
期刊: BIOMATERIALS
影响因子: 14
作者:
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通讯作者: Feijen, J
DOI: 10.1002/art.20986
发表时间: 2005-04-01
影响因子: --
作者:
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通讯作者: Sah, RL
DOI: 10.1016/s0736-0266(02)00084-0
发表时间: 2002-11-01
影响因子: 2.8
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通讯作者: Sah, RL
DOI: 10.1016/0304-4165(86)90306-5
发表时间: 1986-09-04
期刊: BIOCHIMICA ET BIOPHYSICA ACTA
影响因子: --
作者:
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通讯作者: BARRETT, AJ