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转谷氨酰胺酶 2：内皮细胞细胞外基质中的一个新的内皮抑素伴侣。

Transglutaminase-2: a new endostatin partner in the extracellular matrix of endothelial cells.

机构信息

Institut de Biologie et Chimie des Protéines, UMR Centre National de la Recherche Scientifique, University Lyon, France.

出版信息

Biochem J. 2010 Apr 14;427(3):467-75. doi: 10.1042/BJ20091594.

DOI:10.1042/BJ20091594
PMID:20156196
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2876729/
Abstract

Endostatin, a C-terminal fragment of collagen XVIII, binds to TG-2 (transglutaminase-2) in a cation-dependent manner. Recombinant human endostatin binds to TG-2 with an affinity in the nanomolar range (Kd=6.8 nM). Enzymatic assays indicated that, in contrast with other extracellular matrix proteins, endostatin is not a glutaminyl substrate of TG-2 and is not cross-linked to itself by the enzyme. Two arginine residues of endostatin, Arg27 and Arg139, are crucial for its binding to TG-2. They are also involved in the binding to heparin [Sasaki, Larsson, Kreuger, Salmivirta, Claesson-Welsh, Lindahl, Hohenester and Timpl (1999) EMBO J. 18, 6240-6248], and to alpha5beta1 and alphavbeta3 integrins [Faye, Moreau, Chautard, Jetne, Fukai, Ruggiero, Humphries, Olsen and Ricard-Blum (2009) J. Biol. Chem. 284, 22029-22040], suggesting that endostatin is not able to interact simultaneously with TG-2 and heparan sulfate, or with TG-2 and integrins. Inhibition experiments support the hypothesis that the GTP-binding site of TG-2 is a potential binding site for endostatin. Endostatin and TG-2 are co-localized in the extracellular matrix secreted by endothelial cells under hypoxia, which stimulates angiogenesis. This interaction, occurring in a cellular context, might participate in the concerted regulation of angiogenesis and tumorigenesis by the two proteins.

摘要

内皮抑素是胶原 XVIII 的 C 端片段，以阳离子依赖的方式与 TG-2（转谷氨酰胺酶-2）结合。重组人内皮抑素与 TG-2 的亲和力在纳摩尔范围内（Kd=6.8 nM）。酶促测定表明，与其他细胞外基质蛋白不同，内皮抑素不是 TG-2 的谷氨酰胺基底物，也不会被该酶自身交联。内皮抑素的两个精氨酸残基 Arg27 和 Arg139 对于其与 TG-2 的结合至关重要。它们也参与与肝素的结合[Sasaki、Larsson、Kreuger、Salmivirta、Claesson-Welsh、Lindahl、Hohenester 和 Timpl（1999）EMBO J. 18, 6240-6248]，以及与α5β1 和 alphavβ3 整合素的结合[Faye、Moreau、Chautard、Jetne、Fukai、Ruggiero、Humphries、Olsen 和 Ricard-Blum（2009）J. Biol. Chem. 284, 22029-22040]，表明内皮抑素不能同时与 TG-2 和肝素硫酸盐，或与 TG-2 和整合素相互作用。抑制实验支持 TG-2 的 GTP 结合位点是内皮抑素潜在结合位点的假设。内皮抑素和 TG-2 在缺氧条件下内皮细胞分泌的细胞外基质中共同定位，这刺激了血管生成。这种发生在细胞环境中的相互作用可能参与了两种蛋白质对血管生成和肿瘤发生的协同调节。

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J Biol Chem. 2009 Aug 14;284(33):22029-22040. doi: 10.1074/jbc.M109.002840. Epub 2009 Jun 5.
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Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2.
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