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1
Multiple domains of endopin 2A for serpin cross-class inhibition of papain.用于丝氨酸蛋白酶抑制剂对木瓜蛋白酶进行交叉类别抑制的内肽酶2A的多个结构域
Arch Biochem Biophys. 2007 May 15;461(2):219-24. doi: 10.1016/j.abb.2007.02.036. Epub 2007 Mar 21.
2
The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition.新型牛丝氨酸蛋白酶抑制剂内多芬2C在交叉类别抑制中，相较于丝氨酸蛋白酶弹性蛋白酶，对半胱氨酸蛋白酶组织蛋白酶L表现出选择性抑制作用。
Biochemistry. 2005 May 31;44(21):7757-67. doi: 10.1021/bi050053z.
3
The novel serpin endopin 2 demonstrates cross-class inhibition of papain and elastase: localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells.新型丝氨酸蛋白酶抑制剂内肽素2对木瓜蛋白酶和弹性蛋白酶具有跨类抑制作用：内肽素2在神经内分泌嗜铬细胞的调节性分泌囊泡中的定位。
Biochemistry. 2002 Aug 20;41(33):10397-405. doi: 10.1021/bi020088o.
4
Novel secretory vesicle serpins, endopin 1 and endopin 2: endogenous protease inhibitors with distinct target protease specificities.新型分泌性囊泡丝氨酸蛋白酶抑制剂，内肽素1和内肽素2：具有不同靶蛋白酶特异性的内源性蛋白酶抑制剂。
Biol Chem. 2002 Jul-Aug;383(7-8):1067-74. doi: 10.1515/BC.2002.115.
5
Expression and mutagenesis of the novel serpin endopin 2 demonstrates a requirement for cysteine-374 for dithiothreitol-sensitive inhibition of elastase.新型丝氨酸蛋白酶抑制剂内多平2的表达与诱变表明，半胱氨酸-374对二硫苏糖醇敏感的弹性蛋白酶抑制作用是必需的。
Biochemistry. 2000 Aug 1;39(30):8944-52. doi: 10.1021/bi9929655.
6
Novel chromaffin granule serpins, endopin 1 and endopin 2: endogenous protease inhibitors with distinct target protease specificities.新型嗜铬粒蛋白丝氨酸蛋白酶抑制剂，内肽素1和内肽素2：具有不同靶蛋白酶特异性的内源性蛋白酶抑制剂。
Ann N Y Acad Sci. 2002 Oct;971:426-44. doi: 10.1111/j.1749-6632.2002.tb04505.x.
7
Simple modifications of the serpin reactive site loop convert SCCA2 into a cysteine proteinase inhibitor: a critical role for the P3' proline in facilitating RSL cleavage.对丝氨酸蛋白酶抑制剂反应位点环进行简单修饰可将SCCA2转化为半胱氨酸蛋白酶抑制剂：P3'脯氨酸在促进反应位点环裂解中起关键作用。
Biochemistry. 2000 Jun 20;39(24):7081-91. doi: 10.1021/bi000050g.
8
Molecular cloning of endopin 1, a novel serpin localized to neurosecretory vesicles of chromaffin cells. Inhibition of basic residue-cleaving proteases by endopin 1.内肽素1的分子克隆，一种定位于嗜铬细胞神经分泌囊泡的新型丝氨酸蛋白酶抑制剂。内肽素1对碱性残基切割蛋白酶的抑制作用。
J Biol Chem. 1999 Nov 26;274(48):34164-73. doi: 10.1074/jbc.274.48.34164.
9
Demonstration of GTG as an alternative initiation codon for the serpin endopin 2B-2.
Biochem Biophys Res Commun. 2005 Feb 18;327(3):837-44. doi: 10.1016/j.bbrc.2004.12.053.
10
The reactive site loop of the serpin SCCA1 is essential for cysteine proteinase inhibition.丝氨酸蛋白酶抑制剂SCCA1的反应位点环对于半胱氨酸蛋白酶抑制至关重要。
Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13465-70. doi: 10.1073/pnas.95.23.13465.

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Parasit Vectors. 2017 Mar 22;10(1):152. doi: 10.1186/s13071-017-2080-1.
2
Bioinformatics and expression analyses of the Ixodes scapularis tick cystatin family.硬蜱属 Ixodes scapularis 组织蛋白酶抑制剂家族的生物信息学和表达分析。
Exp Appl Acarol. 2013 May;60(1):41-53. doi: 10.1007/s10493-012-9613-2. Epub 2012 Oct 10.
3
Endopin serpin protease inhibitors localize with neuropeptides in secretory vesicles and neuroendocrine tissues.内肽酶丝氨酸蛋白酶抑制剂与神经肽共同定位于分泌小泡和神经内分泌组织中。
Neuroendocrinology. 2009;89(2):210-6. doi: 10.1159/000162916. Epub 2008 Oct 8.

本文引用的文献

1
Purification of the skeletal muscle protein Endopin 1B and characterization of the genes encoding Endopin 1A and 1B isoforms.骨骼肌蛋白Endopin 1B的纯化以及编码Endopin 1A和1B亚型的基因的表征。
FEBS Lett. 2006 Jun 12;580(14):3477-84. doi: 10.1016/j.febslet.2006.04.099. Epub 2006 May 15.
2
The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition.新型牛丝氨酸蛋白酶抑制剂内多芬2C在交叉类别抑制中，相较于丝氨酸蛋白酶弹性蛋白酶，对半胱氨酸蛋白酶组织蛋白酶L表现出选择性抑制作用。
Biochemistry. 2005 May 31;44(21):7757-67. doi: 10.1021/bi050053z.
3
Demonstration of GTG as an alternative initiation codon for the serpin endopin 2B-2.
Biochem Biophys Res Commun. 2005 Feb 18;327(3):837-44. doi: 10.1016/j.bbrc.2004.12.053.
4
Muscle endopin 1, a muscle intracellular serpin which strongly inhibits elastase: purification, characterization, cellular localization and tissue distribution.肌肉内源性蛋白酶抑制剂1，一种强烈抑制弹性蛋白酶的肌肉细胞内丝氨酸蛋白酶抑制剂：纯化、特性、细胞定位及组织分布
Biochem J. 2005 May 15;388(Pt 1):273-80. doi: 10.1042/BJ20041921.
5
Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis.Hurpin是溶酶体组织蛋白酶L的选择性抑制剂，可保护角质形成细胞免受紫外线诱导的细胞凋亡。
Biochemistry. 2003 Jun 24;42(24):7381-9. doi: 10.1021/bi027307q.
6
Inhibition of the cysteine proteinases cathepsins K and L by the serpin headpin (SERPINB13): a kinetic analysis.丝氨酸蛋白酶抑制剂头针（SERPINB13）对半胱氨酸蛋白酶组织蛋白酶K和L的抑制作用：动力学分析
Arch Biochem Biophys. 2003 Jan 15;409(2):367-74. doi: 10.1016/s0003-9861(02)00635-5.
7
Serpin structure, mechanism, and function.丝氨酸蛋白酶抑制剂的结构、机制与功能。
Chem Rev. 2002 Dec;102(12):4751-804. doi: 10.1021/cr010170+.
8
The novel serpin endopin 2 demonstrates cross-class inhibition of papain and elastase: localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells.新型丝氨酸蛋白酶抑制剂内肽素2对木瓜蛋白酶和弹性蛋白酶具有跨类抑制作用：内肽素2在神经内分泌嗜铬细胞的调节性分泌囊泡中的定位。
Biochemistry. 2002 Aug 20;41(33):10397-405. doi: 10.1021/bi020088o.
9
Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: engineering alpha(1)-antitrypsin to inhibit cathepsin proteases.丝氨酸蛋白酶抑制剂结构本质上支持木瓜蛋白酶样半胱氨酸蛋白酶抑制作用的证据：工程化α1-抗胰蛋白酶以抑制组织蛋白酶。
Biochemistry. 2002 Apr 16;41(15):4998-5004. doi: 10.1021/bi0159985.
10
The serpin SQN-5 is a dual mechanistic-class inhibitor of serine and cysteine proteinases.丝氨酸蛋白酶抑制剂SQN-5是一种丝氨酸和半胱氨酸蛋白酶的双机制类抑制剂。
Biochemistry. 2002 Mar 5;41(9):3189-99. doi: 10.1021/bi015999x.

用于丝氨酸蛋白酶抑制剂对木瓜蛋白酶进行交叉类别抑制的内肽酶2A的多个结构域

Multiple domains of endopin 2A for serpin cross-class inhibition of papain.

作者信息

Hwang Shin-Rong, Hook Vivian Y H

机构信息

Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA 92093-0744, USA.

出版信息

Arch Biochem Biophys. 2007 May 15;461(2):219-24. doi: 10.1016/j.abb.2007.02.036. Epub 2007 Mar 21.

DOI:10.1016/j.abb.2007.02.036
PMID:17451636
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2745395/
Abstract

The serpin endopin 2A inhibits the cysteine protease papain in cross-class inhibition. This study demonstrates the novel finding that both the non-RSL NH(2)-domain and the RSL domain with P1-P1' residues participate in endopin 2A inhibition. Production of a chimeric mutant of endopin 2A with replacement of its NH(2)-domain with that of endopin 1 resulted in less effective inhibition of papain, indicated by its lower k(ass) association rate constant compared to wild-type endopin 2A. This chimeric mutant formed complexes with papain, but at lower levels compared to that with wild-type endopin 2A. Papain degradation of a portion of the chimeric mutant suggested a role for the NH(2)-domain in regulating relative amounts of endopin 2A that enter the substrate pathway compared to the serpin inhibitory pathway. Furthermore, site-directed mutagenesis demonstrated that the RSL domain with intact P1-P1' residues was necessary for inhibition. These findings indicate that the NH(2)-domain and the RSL region both participate in endopin 2A inhibition of papain.

摘要

丝氨酸蛋白酶抑制剂内肽酶2A在交叉抑制中可抑制半胱氨酸蛋白酶木瓜蛋白酶。本研究证明了一个新发现，即非反应中心环（RSL）的NH₂结构域和具有P1 - P1'残基的RSL结构域均参与内肽酶2A的抑制作用。用内肽酶1的NH₂结构域替换内肽酶2A的NH₂结构域产生的嵌合突变体，对木瓜蛋白酶的抑制效果较差，这表现为与野生型内肽酶2A相比，其较低的k(ass) 缔合速率常数。该嵌合突变体与木瓜蛋白酶形成复合物，但与野生型内肽酶2A相比水平较低。木瓜蛋白酶对部分嵌合突变体的降解表明，NH₂结构域在调节进入底物途径的内肽酶2A与丝氨酸蛋白酶抑制剂抑制途径的相对量方面发挥作用。此外，定点诱变表明具有完整P1 - P1'残基的RSL结构域对于抑制是必需的。这些发现表明，NH₂结构域和RSL区域均参与内肽酶2A对木瓜蛋白酶的抑制作用。