过氧化物酶中的古老免疫球蛋白结构域是在IV型胶原蛋白中形成亚磺酰胺交联所必需的。
The Ancient Immunoglobulin Domains of Peroxidasin Are Required to Form Sulfilimine Cross-links in Collagen IV.
作者信息
Ero-Tolliver Isi A, Hudson Billy G, Bhave Gautam
机构信息
From the Division of Nephrology and Hypertension and Department of Medicine, Center for Matrix Biology.
From the Division of Nephrology and Hypertension and Department of Medicine, Center for Matrix Biology, Departments of Biochemistry and Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232.
出版信息
J Biol Chem. 2015 Aug 28;290(35):21741-8. doi: 10.1074/jbc.M115.673996. Epub 2015 Jul 15.
The collagen IV sulfilimine cross-link and its catalyzing enzyme, peroxidasin, represent a dyad critical for tissue development, which is conserved throughout the animal kingdom. Peroxidasin forms novel sulfilimine bonds between opposing methionine and hydroxylysine residues to structurally reinforce the collagen IV scaffold, a function critical for basement membrane and tissue integrity. However, the molecular mechanism underlying cross-link formation remains unclear. In this work, we demonstrate that the catalytic domain of peroxidasin and its immunoglobulin (Ig) domains are required for efficient sulfilimine bond formation. Thus, these molecular features underlie the evolutionarily conserved function of peroxidasin in tissue development and integrity and distinguish peroxidasin from other peroxidases, such as myeloperoxidase (MPO) and eosinophil peroxidase (EPO).
IV型胶原蛋白亚磺酰亚胺交联及其催化酶过氧化物酶，代表了组织发育至关重要的二元组，在整个动物界都保守存在。过氧化物酶在相对的甲硫氨酸和羟赖氨酸残基之间形成新的亚磺酰亚胺键，以在结构上加强IV型胶原蛋白支架，这一功能对基底膜和组织完整性至关重要。然而，交联形成的分子机制仍不清楚。在这项工作中，我们证明过氧化物酶的催化结构域及其免疫球蛋白（Ig）结构域是有效形成亚磺酰亚胺键所必需的。因此，这些分子特征构成了过氧化物酶在组织发育和完整性方面进化保守功能的基础，并将过氧化物酶与其他过氧化物酶，如髓过氧化物酶（MPO）和嗜酸性粒细胞过氧化物酶（EPO）区分开来。
Zotero 插件