Human Tryptase ε (PRSS22), a New Member of the Chromosome 16p13.3 Family of Human Serine Proteases Expressed in Airway Epithelial Cells*

Human Tryptase ε (PRSS22), a New Member of the Chromosome 16p13.3 Family of Human Serine Proteases Expressed in Airway Epithelial Cells*
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人类类胰蛋白酶 ε (PRSS22),在气道上皮细胞中表达的人类丝氨酸蛋白酶染色体 16p13.3 家族的新成员*

DOI:
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发表时间:
2001
影响因子:
4.8
通讯作者:
R. Stevens
R. Stevens
中科院分区:
生物学2区
文献类型:
--
作者:
G. W. Wong;S. Yasuda;M. Madhusudhan;Lixin Li;Yi Yang;S. Krilis;A. Sali;R. Stevens

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用不同的人类胰蛋白酶cDNA探测GenBank表达序列标签(EST)数据库,鉴定了两个截短的EST,随后发现它们编码一种新的人丝氨酸蛋白酶(命名为类胰蛋白酶ε或蛋白酶,丝氨酸S1家族成员22(PRSS 22))的重叠部分。类胰蛋白酶ε基因位于染色体16p13.3上,在丝氨酸蛋白酶基因的2.5-Mb复合物内。虽然在该复合体中的14个基因中至少有7个编码酶活性蛋白酶,但仅鉴定出一个类胰蛋白酶ε-样基因。在成年人中,发现气管和食管含有最高稳态水平的类胰蛋白酶ε转录物。虽然类胰蛋白酶ε转录本在成人肺中很少,但在胎儿肺中却大量存在。因此,类胰蛋白酶ε基因在气道中以发育调节的方式表达,这与其他人类类胰蛋白酶基因的表达方式不同。在细胞水平上,类胰蛋白酶ε是正常肺上皮细胞以及各种转化上皮细胞系的主要产物。这些细胞也组成性分泌具有酶活性的类胰蛋白酶ε。人类胰蛋白酶ε的氨基酸序列与人类胰蛋白酶α、类胰蛋白酶βI、类胰蛋白酶βII、类胰蛋白酶βIII、跨膜类胰蛋白酶/类胰蛋白酶γ、marapsin和Esp-1/testisin的氨基酸序列具有38-44%的同一性。然而,比较蛋白质结构建模和功能研究使用重组材料显示,类胰蛋白酶ε具有不同于其其他家族成员的底物偏好。这些数据表明,类胰蛋白酶基因的染色体16p13.3复合体的产物进化为在人类中执行各种功能。
Probing of the GenBankTMexpressed sequence tag (EST) data base with varied human tryptase cDNAs identified two truncated ESTs that subsequently were found to encode overlapping portions of a novel human serine protease (designated tryptase ε or protease, serineS1 family member 22 (PRSS22)). The tryptase ε gene resides on chromosome 16p13.3 within a 2.5-Mb complex of serine protease genes. Although at least 7 of the 14 genes in this complex encode enzymatically active proteases, only one tryptase ε-like gene was identified. The trachea and esophagus were found to contain the highest steady-state levels of the tryptase ε transcript in adult humans. Although the tryptase ε transcript was scarce in adult human lung, it was present in abundance in fetal lung. Thus, the tryptase ε gene is expressed in the airways in a developmentally regulated manner that is different from that of other human tryptase genes. At the cellular level, tryptase ε is a major product of normal pulmonary epithelial cells, as well as varied transformed epithelial cell lines. Enzymatically active tryptase ε is also constitutively secreted from these cells. The amino acid sequence of human tryptase ε is 38–44% identical to those of human tryptase α, tryptase βI, tryptase βII, tryptase βIII, transmembrane tryptase/tryptase γ, marapsin, and Esp-1/testisin. Nevertheless, comparative protein structure modeling and functional studies using recombinant material revealed that tryptase ε has a substrate preference distinct from that of its other family members. These data indicate that the products of the chromosome 16p13.3 complex of tryptase genes evolved to carry out varied functions in humans.
DOI: 10.1021/bi991130r
发表时间: 1999-08-24
期刊: BIOCHEMISTRY
影响因子: 2.9
作者:
Peisach, E;Wang, JY;Ringe, D
通讯作者: Ringe, D
DOI: 10.1172/jci114051
发表时间: 1989-05-01
影响因子: 15.9
作者:
SCHWARTZ, LB;YUNGINGER, JW;DULL, D
通讯作者: DULL, D
DOI: 10.1056/nejm198706253162603
发表时间: 1987-06-25
影响因子: 158.5
作者:
SCHWARTZ, LB;METCALFE, DD;SULLIVAN, T
通讯作者: SULLIVAN, T
DOI: --
发表时间: 1991
期刊: The Journal of biological chemistry
影响因子: --
作者:
Reynolds,DS;Gurley,DS;Austen,KF;Serafin,WE
通讯作者: Serafin,WE
DOI: 10.1016/s0021-9258(17)38401-6
发表时间: 1986-06
期刊: The Journal of biological chemistry
影响因子: --
作者:
L. Schwartz;T. Bradford
通讯作者: L. Schwartz;T. Bradford