Characterization of lamprin, an unusual matrix protein from lamprey cartilage. Implications for evolution, structure, and assembly of elastin and other fibrillar proteins.
Characterization of lamprin, an unusual matrix protein from lamprey cartilage. Implications for evolution, structure, and assembly of elastin and other fibrillar proteins.
复制标题
七鳃鳗蛋白的表征，七鳃鳗软骨中一种不寻常的基质蛋白。
DOI：
10.1016/s0021-9258(18)54095-3
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
F. Keeley
中科院分区：
文献类型：
--
作者：
P. Robson;G. Wright;E. Sitarz;A. Maiti;M. Rawat;J. Youson;F. Keeley
七鳃鳗蛋白是一种不溶性非胶原蛋白、非弹性蛋白，是七鳃鳗环状软骨纤维状细胞外基质的主要结缔组织成分。在这里，我们证明灯蛋白的可溶性单体是一个分子质量为 12 和 10 kDa 的高度疏水性自聚集蛋白家族。鉴定出可溶性灯蛋白的两种 mRNA（0.9 和 2 kilobase），主要区别在于其 3'-非翻译尾部的长度。可溶性灯蛋白的变体似乎是作为多个基因的产物和通过交替剪接而出现的。尽管通常与任何其他蛋白质不同源，但可溶性灯蛋白含有串联重复肽序列 (GGLGY)，该序列存在于蚕蛾绒毛膜蛋白和蜘蛛拖丝中。与该重复序列的强同源性也存在于几种哺乳动物和鸟类弹性蛋白中。 VGVAPG（人弹性蛋白中的重复序列）的单克隆抗体也会与灯蛋白发生交叉反应。我们认为这些蛋白质共享一个结构基序，通过β-折叠/β-转角结构中疏水性侧链的交错，促进蛋白质中的自聚集和原纤维形成，该基序在几亿年的进化中以可识别的形式保存下来。
Lamprin, an insoluble non-collagen, non-elastin protein, is the major connective tissue component of the fibrillar extracellular matrix of lamprey annular cartilage. Here we demonstrate that the soluble monomer of lamprin is a family of highly hydrophobic, self-aggregating proteins with molecular masses of 12 and 10 kDa. Two mRNAs for soluble lamprin were identified (0.9and 2 kilobases), differing principally in the length of their 3'-untranslated tails. Variants of soluble lamprin appear to arise both as the products of multiple genes and by alternate splicing. Although not generally homologous to any other protein, soluble lamprins contain a tandemly repeated peptide sequence (GGLGY) which is present in both silkmoth chorion proteins and spider dragline silk. Strong homologies to this repeat sequence are also present in several mammalian and avian elastins. Monoclonal antibodies to VGVAPG, a repeated sequence in human elastin, also cross-react with lamprin. We suggest that these proteins share a structural motif which promotes self-aggregation and fibril formation in proteins through interdigitation of hydrophobic side chains in beta-sheet/beta-turn structures, a motif that has been preserved in recognizable form over several hundred million years of evolution.