Horton M A, Larson K A, Lee J J, Lee N A
Department of Biochemistry and Molecular Biology, Mayo Clinic Scottsdale, Arizona, USA.
J Leukoc Biol. 1996 Aug;60(2):285-94. doi: 10.1002/jlb.60.2.285.
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.
通过使用人嗜酸性粒细胞过氧化物酶(hEPO)cDNA以降低的标准筛选随机引物骨髓cDNA文库,克隆了小鼠嗜酸性粒细胞过氧化物酶(mEPO)基因。随后使用mEPO cDNA从λ基因组文库中分离出mEPO基因。mEPO基因与其人类同源物显示出高度的保守性:转录单位大小大致相同,保留了与每个基因相关的12个外显子的相对大小和位置,并且在核苷酸水平上,小鼠和人类EPO基因在蛋白质编码区的同一性为86%,在3'-非翻译尾随区的同一性为66%。这种强烈的保守性延伸到编码的蛋白质,它们显示出约90%的氨基酸同一性。mEPO基因的表达仅限于含有嗜酸性粒细胞祖细胞的组织(如骨髓和脾脏),这一模式与另一种小鼠嗜酸性粒细胞颗粒蛋白主要碱性蛋白的表达相似。