Butkowski R J, Shen G Q, Wieslander J, Michael A F, Fish A J
Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis 55455.
J Lab Clin Med. 1990 Mar;115(3):365-73.
Monomeric subunits of the globular domain of type IV collagen from human renal basement membrane were isolated and characterized. The monomers, M24, M26, M28+, and M28 , which have been identified previously in human glomerular basement membrane, were characterized by amino acid analysis, amino-terminal sequencing, and electrophoretic mobility. The results indicate that M24 and M26 are derived from alpha 1(IV) and alpha 2(IV) collagen chains, respectively. Amino-terminal sequencing revealed that M28+, and M28 correspond to the globular domain of novel collagen chains. M28 has been characterized as the principal target antigen in Goodpasture's syndrome and antiglomerular basement membrane (GBM) nephritis, and both M28 species are absent from the GBM in Alport familial nephritis. The cationic charge of M28 appears to be a consequence of a relatively high concentration of basic amino acids when compared with other monomers. Previous studies of bovine GBM have demonstrated chains with amino-terminal sequence homology to M28+ and M28 .
从人肾基底膜中分离并鉴定了IV型胶原蛋白球状结构域的单体亚基。这些单体，即先前在人肾小球基底膜中已鉴定出的M24、M26、M28 +和M28，通过氨基酸分析、氨基末端测序和电泳迁移率进行了表征。结果表明，M24和M26分别源自α1(IV)和α2(IV)胶原链。氨基末端测序显示，M28 +和M28对应于新型胶原链的球状结构域。M28已被确定为Goodpasture综合征和抗肾小球基底膜（GBM）肾炎中的主要靶抗原，而在Alport家族性肾炎的GBM中不存在这两种M28类型。与其他单体相比，M28的阳离子电荷似乎是由于碱性氨基酸浓度相对较高所致。先前对牛GBM的研究已经证明了与M28 +和M28具有氨基末端序列同源性的链。
