Inoue M, Kanbe N, Kurosawa M, Kido H
Division of Enzyme Chemistry, Institute for Enzyme Research, University of Tokushima, 3 Kuramoto-cho, Tokushima, 770-8503, Japan.
Biochem Biophys Res Commun. 1998 Nov 18;252(2):307-12. doi: 10.1006/bbrc.1998.9645.
We have cloned a novel serine protease designated as esp-1 from human eosinophils. The amino acid sequence deduced from the cDNA showed that ESP-1 comprises a signal peptide of 18 amino acids, a propeptide of 23 amino acids, an active form sequence of 273 amino acids starting from an Ile-Val-Gly-Gly-Glu motif, the catalytic triad of serine proteases that has been characterized as the essential amino acid residues for the proteolytic activity, and a hydrophobic amino acid stretch in the carboxyl terminus, suggesting this enzyme is a novel membrane-type serine protease. The tissue distributions of esp-1 expression revealed that this protease is not only expressed in human eosinophils, but also widely expressed in mononuclear cells and various tissues other than skeletal muscle and kidney and is most abundant in testis and prostate, and moderately so in lung, spleen and pancreas.
我们从人嗜酸性粒细胞中克隆了一种名为esp-1的新型丝氨酸蛋白酶。从cDNA推导的氨基酸序列表明，ESP-1包含一个18个氨基酸的信号肽、一个23个氨基酸的前肽、一个从Ile-Val-Gly-Gly-Glu基序开始的273个氨基酸的活性形式序列、丝氨酸蛋白酶的催化三联体（已被表征为蛋白水解活性的必需氨基酸残基）以及羧基末端的疏水性氨基酸延伸，表明该酶是一种新型膜型丝氨酸蛋白酶。esp-1表达的组织分布显示，这种蛋白酶不仅在人嗜酸性粒细胞中表达，还在单核细胞以及骨骼肌和肾脏以外的各种组织中广泛表达，在睾丸和前列腺中表达最丰富，在肺、脾和胰腺中表达适中。
