Nelson R E, Fessler L I, Takagi Y, Blumberg B, Keene D R, Olson P F, Parker C G, Fessler J H
Molecular Biology Institute, University of California, Los Angeles 90024-1570.
EMBO J. 1994 Aug 1;13(15):3438-47. doi: 10.1002/j.1460-2075.1994.tb06649.x.
Peroxidasin is a novel protein combining peroxidase and extracellular matrix motifs. Hemocytes differentiate early from head mesoderm, make peroxidasin and later phagocytose apoptotic cells. As hemocytes spread throughout the embryo, they synthesize extracellular matrix and peroxidasin, incorporating it into completed basement membranes. Cultured cells secrete peroxidasin; it occurs in larvae and adults. Each 1512 residue chain of the three-armed, disulfide-linked homotrimer combines a peroxidase domain with six leucine-rich regions, four Ig loops, a thrombospondin/procollagen homology and an amphipathic alpha-helix. The peroxidase domain is homologous with human myeloperoxidase and eosinophil peroxidase. This heme protein catalyzes H2O2-driven radioiodinations, oxidations and formation of dityrosine. We propose that peroxidasin functions uniquely in extracellular matrix consolidation, phagocytosis and defense.
过氧化物酶是一种结合了过氧化物酶和细胞外基质基序的新型蛋白质。血细胞早期从头部中胚层分化而来,产生过氧化物酶,随后吞噬凋亡细胞。随着血细胞在胚胎中扩散,它们合成细胞外基质和过氧化物酶,并将其整合到完整的基底膜中。培养细胞分泌过氧化物酶;它存在于幼虫和成虫中。三臂、二硫键连接的同三聚体的每条1512个残基链将一个过氧化物酶结构域与六个富含亮氨酸的区域、四个免疫球蛋白环、一个血小板反应蛋白/前胶原同源物和一个两亲性α螺旋结合在一起。过氧化物酶结构域与人髓过氧化物酶和嗜酸性粒细胞过氧化物酶同源。这种血红素蛋白催化由过氧化氢驱动的放射性碘化、氧化和二酪氨酸的形成。我们认为过氧化物酶在细胞外基质巩固、吞噬作用和防御中具有独特的功能。