Proteinases secreted by Fasciola hepatica degrade extracellular matrix and basement membrane components
Proteinases secreted by Fasciola hepatica degrade extracellular matrix and basement membrane components
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DOI：
10.2307/3284308
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发表时间：
1997-02-01
影响因子：
1.3
通讯作者：
Carmona, C
中科院分区：
文献类型：
--
作者：
Berasain, P;Goni, F;Carmona, C
寄生性肝片形吸虫的侵入阶段将蛋白酶释放到其所维持的培养基中。在本研究中，我们研究了肝镰刀菌排泄/分泌 (E/S) 产物和从这些产物中纯化的 2 种半胱氨酸蛋白酶（CL1 和 CL2）与细胞外基质和基底膜大分子的相互作用。肝片形吸虫 EIS 产品对纤维状 I 型和 III 型胶原蛋白以及基底膜 IV 型胶原蛋白具有溶胶原活性。 CLI和CL2能够降解酸溶性III型和IV型胶原蛋白，但不能降解不溶性I型胶原蛋白。相比之下，E/S 产品和纯化的 CLI 和 CL2 均未显示出弹性蛋白溶解活性。纤连蛋白和层粘连蛋白被 E/S 产品以及 CL1 和 CL2 降解。纤连蛋白降解产物的序列分析表明，获得的片段对应于完整的生物活性结构域。这些结果表明肝镰刀菌分泌的半胱氨酸蛋白酶可能参与了寄生虫侵入组织的过程。
The invasive stages of the parasitic trematode Fasciola hepatica release proteinases into the medium in which they are mantained. In this study, we investigated the interaction of F. hepatica excretory/secretory (E/S) products and 2 cysteine proteinases (CL1 and CL2) purified from these products with extracellular matrix and basement membrane macromolecules. Fasciola hepatica EIS products contained collagenolytic activity on fibrillar types I and III collagen as well as basement membrane type IV collagen. CLI and CL2 were capable of degrading acid-soluble type III and type IV collagen but not insoluble type I collagen. In contrast, neither the E/S products nor the purified CLI and CL2 showed elastinolytic activity. Fibronectin and laminin were degraded by E/S products and by CL1 and CL2. Sequence analysis of fibronectin degradation products showed that the fragments obtained corresponded to complete biologically active domains. These results indicate that the cysteine proteinases secreted by F. hepatica may be involved in the process of tissue invasion by the parasite.