Peroxidasin: a novel enzyme-matrix protein of Drosophila development

• Published in: The EMBO journal Vol. 13; no. 15; pp. 3438 - 3447
• Main Authors: Nelson, R.E, Fessler, L.I, Takagi, Y, Blumberg, B, Keene, D.R, Olson, P.F, Parker, C.G, Fessler, J.H
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 01.08.1994
• Subjects: Amino Acid Sequence; amino acid sequences; Analytical, structural and metabolic biochemistry; animal proteins; Animals; Biological and medical sciences; cell differentiation; Cell Line; Chromosome Mapping; complementary DNA; Drosophila; Drosophila - embryology; Drosophila - enzymology; Drosophila - genetics; Drosophila melanogaster; embryogenesis; Enzymes and enzyme inhibitors; extracellular matrix proteins; Extracellular Matrix Proteins - chemistry; Extracellular Matrix Proteins - genetics; Extracellular Matrix Proteins - isolation & purification; Extracellular Matrix Proteins - metabolism; Fundamental and applied biological sciences. Psychology; genbank/u11052; Gene Expression; Genes, Insect - genetics; Hemeproteins - chemistry; Hemeproteins - genetics; Hemeproteins - isolation & purification; Hemeproteins - metabolism; hemocytes; Hemocytes - enzymology; molecular conformation; Molecular Sequence Data; Molecular Weight; nucleotide sequences; Oxidation-Reduction; Oxidoreductases; peroxidase; Peroxidase - chemistry; Peroxidase - genetics; Peroxidase - isolation & purification; Peroxidase - metabolism; Peroxidasin; Protein Conformation; Protein Structure, Tertiary; RNA, Messenger - analysis; Sequence Analysis; Trimer; Enzyme; Insecta; Drosophila; Gene expression; Adhesion; Drosophilidae; Hemocyte; Peroxidases; Enzymatic activity; Domain structure; Arthropoda; Development; Extracellular matrix; Peroxidase; Oxidoreductases; Invertebrata; Diptera; Aminoacid sequence; Structural analysis
• ISSN: 0261-4189; 1460-2075
• 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 a 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.