Bashir M M, Abrams W R, Rosenbloom J, Kucich U, Bacarra M, Han M D, Brown-Augsberger P, Mecham R, Rosenbloom J
Department of Anatomy and Histology, School of Dental Medicine, University of Pennsylvania, Philadelphia 19104.
Biochemistry. 1994 Jan 18;33(2):593-600. doi: 10.1021/bi00168a026.
Microfibrils having a diameter of 10-12 nm, found either in association with elastin or independently, are an important component of the extracellular matrix of many tissues. Because isolation of native proteins composing the microfibrils has proven difficult, information on structure/function relationships is limited. In order to extend our understanding of the 31-kDa microfibril-associated glycoprotein (MAGP), the bovine gene has been cloned and characterized and the protein has been expressed in a eukaryotic system. The compact coding portion of the gene is contained in 4.5 kbp of genomic DNA and does not appear to share any domain motifs with other known proteins. The size, amino acid composition, and sequence of the amino terminus of the secreted recombinant protein (rMAGP) all agree with values predicted by the nucleotide sequence of the cDNA used in the expression vector. The rMAGP reacts with a monospecific antibody prepared against a defined amino acid sequence of the natural molecule and reacts specifically with recombinantly produced tropoelastin, suggesting that rMAGP will be a useful reagent with which to study its interaction with other extracellular matrix components.
直径为10 - 12纳米的微原纤维，要么与弹性蛋白结合存在，要么独立存在，是许多组织细胞外基质的重要组成部分。由于构成微原纤维的天然蛋白质的分离已被证明很困难，关于结构/功能关系的信息有限。为了扩展我们对31 kDa微原纤维相关糖蛋白（MAGP）的理解，已经克隆并表征了牛基因，并且该蛋白已在真核系统中表达。该基因紧密的编码部分包含在4.5千碱基对的基因组DNA中，并且似乎与其他已知蛋白质没有共享任何结构域基序。分泌的重组蛋白（rMAGP）的大小、氨基酸组成和氨基末端序列均与表达载体中使用的cDNA核苷酸序列预测的值一致。rMAGP与针对天然分子的特定氨基酸序列制备的单特异性抗体发生反应，并与重组产生的原弹性蛋白特异性反应，这表明rMAGP将是研究其与其他细胞外基质成分相互作用的有用试剂。
