Fibril-forming collagens in lamprey.
Fibril-forming collagens in lamprey.
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DOI：
10.1016/s0021-9258(19)35449-3
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发表时间：
1988-01
期刊：
影响因子：
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通讯作者：
J. Kelly;Shoichiro Tanaka;T. Hardt;E. Eikenberry;B. Brodsky
中科院分区：
文献类型：
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作者：
J. Kelly;Shoichiro Tanaka;T. Hardt;E. Eikenberry;B. Brodsky
在七鳃鳗组织中发现了五种类型的三螺旋区域长度约为300 nm的胶原蛋白，其显示出特征性的D-周期性胶原蛋白原纤维。这些胶原蛋白是这种原始脊椎动物原纤维形成家族的成员。七鳃鳗胶原蛋白的特征在于相对于溶解度，流动性十二烷基硫酸钠-聚丙烯酰胺凝胶电泳，羧甲基纤维素色谱，肽消化模式，组成，脊椎动物胶原酶的敏感性，热稳定性，和段长间距带型。与纤维形成胶原蛋白在高等脊椎动物（I，II，III，V和XI型）的比较确定了三个七鳃鳗胶原蛋白的II，V和XI型。七鳃鳗真皮和主要体壁胶原蛋白的性质类似于I型，但不是典型的异源三聚体组成。真皮分子只有α 1（I）样链，而体壁分子有α 2（I）样链与类似七鳃鳗II型的链结合。两种胶原蛋白均未表现出III型的链间二硫键或溶解度特性。在II型/XI型组织中的原纤维组织的保护相反，在I型和III型组织中的主要发展后，七鳃鳗和高等脊椎动物的分歧与这些结果是一致的。II型和I型样分子作为主要胶原蛋白和V型和XI型作为次要胶原蛋白的七鳃鳗中的存在，以及这些分子对脊椎动物胶原酶的差异敏感性类似于高等脊椎动物中的发现。
Five types of collagen with triple-helical regions approximately 300 nm in length were found in lamprey tissues which show characteristic D-periodic collagen fibrils. These collagens are members of the fibril forming family of this primitive vertebrate. Lamprey collagens were characterized with respect to solubility, mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, carboxylmethyl-cellulose chromatography, peptide digestion patterns, composition, susceptibility to vertebrate collagenase, thermal stability, and segment long spacing-banding pattern. Comparison with fibril-forming collagens in higher vertebrates (types I, II, III, V, and XI) identified three lamprey collagens as types II, V, and XI. Both lamprey dermis and major body wall collagens had properties similar to type I but not the typical heterotrimer composition. Dermis molecules had only alpha 1(I)-like chains, while body wall molecules had alpha 2(I)-like chains combined with chains resembling lamprey type II. Neither collagen exhibited the interchain disulfide linkages or solubility properties of type III. The conservation of fibril organization in type II/type XI tissues in contrast to the major developments in type I and type III tissues after the divergence of lamprey and higher vertebrates is consistent with these results. The presence of type II and type I-like molecules as major collagens and types V and XI as minor collagens in the lamprey, and the differential susceptibility of these molecules to vertebrate collagenase is analogous to the findings in higher vertebrates.