Cloning of the murine eosinophil peroxidase gene (mEPO): characterization of a conserved subgroup of mammalian hematopoietic peroxidases.
The mouse eosinophil peroxidase (mEPO) gene was cloned by screening a random-primed bone marrow cDNA library at reduced criteria using a hEPO cDNA. An mEPO cDNA was subsequently used to isolate the mEPO gene from a lambda-genomic library. The mEPO gene displays a high degree of conservation with its human homologue: the transcription units are approximately the same size, conserve the relative size and position of the 12 exons associated with each gene, and at a nucleotide level the mouse and human EPO genes are 86% identical in the protein coding regions and 66% identical in the 3'-untranslated trailer regions. This strong conservation extends to the encoded proteins which show approximately 90% amino acid identity. Expression of the mEPO gene is restricted to tissues containing eosinophil progenitor cells (e.g., bone marrow and spleen), a pattern similar to the expression of another murine eosinophil granule protein, major basic protein.
Horton
M A
MA
Department of Biochemistry and Molecular Biology, Mayo Clinic Scottsdale, Arizona, USA.
Larson
K A
KA
Lee
J J
JJ
Lee
N A
NA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001853:Bone Marrow / Q000201:enzymology; D003001:Cloning, Molecular; D017124:Conserved Sequence; D003486:Cyanides / Q000494:pharmacology; D018076:DNA, Complementary / Q000235:genetics; D047209:Eosinophil Peroxidase; D004804:Eosinophils / Q000201:enzymology; D019143:Evolution, Molecular; D005260:Female; D015870:Gene Expression; D006412:Hematopoietic Stem Cells / Q000201:enzymology*; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000096:biosynthesis / Q000235:genetics*; D012045:Regulatory Sequences, Nucleic Acid; D017386:Sequence Homology, Amino Acid
D003486:Cyanides; D018076:DNA, Complementary; D047209:Eosinophil Peroxidase; D010544:Peroxidases