Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
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DOI：
10.1111/j.1432-1033.1997.00725.x
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发表时间：
1997-07-15
期刊：
影响因子：
--
通讯作者：
Maines, MD
中科院分区：
文献类型：
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作者：
McCoubrey, WK;Huang, TJ;Maines, MD
迄今为止，已经表征了两种血红素氧酶（HO），HO-1或HSP32和组成型HO-2的同工酶。我们报告发现第三种蛋白质物种，并将其称为HO-3。 HO-3是单个转录本的乘积，该转录物近似于2.4 kb，可以编码大约33 kDa的蛋白质。 HO-3转录本在脾，肝，胸腺，前列腺，心脏，肾脏，脑和睾丸中发现，是单拷贝基因的产物。 HO-3的预测氨基酸结构与HO-1（HSP32）和HO-2都不同，但与HO-2密切相关（大约为90％）。大肠杆菌表达和纯化的HO-3蛋白不会与与大鼠HO-1或HO-2的多克隆抗体交叉反应，是一种较差的血红素催化剂，并且显示出血蛋白光谱特征。预测的蛋白质具有两个血红素调节基序，可能与血红素结合有关。这些基序和HO-3的血蛋白性质表明蛋白质在细胞过程中的潜在调节作用，这是血红素依赖性的。
Two isozymes of heme oxygenase (HO), HO-1 or HSP32 and the constitutive form HO-2, have been characterized to date. We report the discovery of a third protein species and refer to it as HO-3. HO-3 is the product of a single transcript of approximate to 2.4 kb and can encode a protein of approximate to 33 kDa. The HO-3 transcript is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis and is the product of a single-copy gene. The predicted amino acid structure of HO-3 differs from both HO-1 (HSP32) and HO-2 but is closely related to HO-2 (approximate to 90%). Escherichia coli expressed and purified HO-3 protein does not cross react with polyclonal antibodies to either rat HO-1 or HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics. The predicted protein has two heme regulatory motifs that may be involved in heme binding. These motifs and the hemoprotein nature of HO-3 suggest a potential regulatory role for the protein in cellular processes which are heme-dependent.