Role of sialic acid‐containing glycans of matrix metalloproteinase‐9 (MMP‐9) in the interaction between MMP‐9 and staphylococcal superantigen‐like protein 5
Role of sialic acid‐containing glycans of matrix metalloproteinase‐9 (MMP‐9) in the interaction between MMP‐9 and staphylococcal superantigen‐like protein 5
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基质金属蛋白酶 9 (MMP-9) 含唾液酸聚糖在 MMP-9 与葡萄球菌超抗原样蛋白 5 相互作用中的作用
DOI：
10.1111/1348-0421.12573
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发表时间：
2018
影响因子：
2.6
通讯作者：
T. Tsuji
中科院分区：
文献类型：
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作者：
Chisato Kurisaka;T. Oku;S. Itoh;T. Tsuji
葡萄球菌超抗原样蛋白(SSL)没有超抗原活性，但最近被认为是免疫抑制因子。先前报道SSL5与P-选择素糖蛋白配体-1(PSGL-1)和基质金属蛋白酶(MMPs)-9结合，导致抑制白细胞的黏附和侵袭。这些相互作用被认为依赖于含唾液酸多糖的基质金属蛋白酶-9，但唾液酸在SSL5和基质金属蛋白酶-9相互作用中的作用仍然存在争议。在本研究中，我们制备了重组谷胱甘肽S转移酶标记的SSL5(GST-SSL5)，并通过下拉实验分析了其糖基修饰后与基质金属蛋白酶-9的结合能力。我们观察到GST-SSL5与人单核细胞白血病细胞系(THP-1细胞)的MMP-9特异性结合，并以浓度依赖的方式抑制其酶活性。神经氨酸酶处理后，其与GST-SSL5的结合活性明显降低。此外，唾液酸缺失的Lec2突变细胞产生的重组基质金属蛋白酶-9对SSL5的亲和力远低于野生型CHO-K1细胞。用PNGase F处理基质金属蛋白酶-9去除N-糖基后，GST-SSL5/基质金属蛋白酶-9的相互作用没有明显变化。相反，GST-SSL5与培养的THP-1细胞分泌的基质金属蛋白酶-9的结合弱于未经处理的细胞分泌的基质金属蛋白酶-9。这些结果有力地表明了含有唾液酸的基质金属蛋白酶-9的O-糖链在基质金属蛋白酶-9与GST-SSL5相互作用中的重要性。
Staphylococcal superantigen‐like proteins (SSL) show no superantigenic activity but have recently been considered to act as immune suppressors. It was previously reported that SSL5 bound to P‐selectin glycoprotein ligand‐1 (PSGL‐1) and matrix metalloproteinase (MMP)‐9, leading to inhibition of leukocyte adhesion and invasion. These interactions were suggested to depend on sialic acid‐containing glycans of MMP‐9, but the roles of sialic acids in the interaction between SSL5 and MMP‐9 are still controversial. In the present study, we prepared recombinant glutathione S‐transferase‐tagged SSL5 (GST‐SSL5) and analyzed its binding capacity to MMP‐9 by pull‐down assay after various modifications of its carbohydrate moieties. We observed that GST‐SSL5 specifically bound to MMP‐9 from a human monocytic leukemia cell line (THP‐1 cells) and inhibited its enzymatic activity in a concentration‐dependent manner. After MMP‐9 was treated with neuraminidase, its binding activity towards GST‐SSL5 was markedly decreased. Furthermore, recombinant MMP‐9 produced by sialic acid‐deficient Lec2 mutant cells showed much lower affinity for SSL5 than that produced by wild‐type CHO‐K1 cells. Treatment of MMP‐9 with PNGase F to remove N‐glycan resulted in no significant change in the GST‐SSL5/MMP‐9 interaction. In contrast, the binding of GST‐SSL5 to MMP‐9 secreted from THP‐1 cells cultured in the presence of an inhibitor for the biosynthesis of O‐glycan (benzyl‐GalNAc) was weaker than the binding of GST‐SSL5 to MMP‐9 secreted from untreated cells. These results strongly suggest the importance of the sialic acid‐containing O‐glycans of MMP‐9 for the interaction of MMP‐9 with GST‐SSL5.
DOI：
10.1016/s0021-9258(18)32554-7
发表时间：
1983-04
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
S. Tollefsen;R. Kornfeld
通讯作者：
S. Tollefsen;R. Kornfeld
明胶酶 B/基质金属蛋白酶-9 的环状三聚体构成了一组独特的功能酶分子，受金属蛋白酶-1 组织抑制剂的差异调节。
DOI：
10.1042/bj20140418
发表时间：
2015
期刊：
The Biochemical journal
影响因子：
--
作者：
Vandooren,Jennifer;Born,Benjamin;Solomonov,Inna;Zajac,Ewa;Saldova,Radka;Senske,Michael;Ugarte-Berzal,Estefanía;Martens,Erik;VandenSteen,PhilippeE;VanDamme,Jo;Garcia-Pardo,Angeles;Froeyen,Matheus;Deryugina,ElenaI;Quigley,Jam
通讯作者：
Quigley,Jam