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本文引用的文献

1
Stroma-derived matrix metalloproteinase (MMP)-2 promotes membrane type 1-MMP-dependent tumor growth in mice.基质衍生的基质金属蛋白酶（MMP）-2促进小鼠中膜型1-MMP依赖性肿瘤生长。
Cancer Res. 2007 May 1;67(9):4311-9. doi: 10.1158/0008-5472.CAN-06-4761.
2
Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP.细胞表面胶原分解需要膜结合型胶原酶MT1-MMP的同二聚化。
Mol Biol Cell. 2006 Dec;17(12):5390-9. doi: 10.1091/mbc.e06-08-0740. Epub 2006 Oct 18.
3
TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains.膜型2（MT2）-基质金属蛋白酶（MMP）-2激活对金属蛋白酶组织抑制因子（TIMP）的独立性由MT2-MMP催化结构域和血红素结合蛋白C结构域共同作用决定。
J Biol Chem. 2006 Sep 8;281(36):26528-39. doi: 10.1074/jbc.M603331200. Epub 2006 Jul 6.
4
A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1.二聚体受体酪氨酸激酶DDR1的激活需要一个跨膜亮氨酸拉链。
J Biol Chem. 2006 Aug 11;281(32):22744-51. doi: 10.1074/jbc.M603233200. Epub 2006 Jun 14.
5
MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells.基质金属蛋白酶-1引导血管平滑肌细胞侵袭动脉壁并形成新生内膜。
J Exp Med. 2005 Sep 5;202(5):663-71. doi: 10.1084/jem.20050607.
6
Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration.半胱氨酸574位点的棕榈酰化对于MT1-MMP促进细胞迁移至关重要。
FASEB J. 2005 Aug;19(10):1326-8. doi: 10.1096/fj.04-3651fje. Epub 2005 Jun 9.
7
MT1-MMP: a potent modifier of pericellular microenvironment.基质金属蛋白酶-1：细胞周围微环境的强效调节剂。
J Cell Physiol. 2006 Jan;206(1):1-8. doi: 10.1002/jcp.20431.
8
An MT1-MMP-PDGF receptor-beta axis regulates mural cell investment of the microvasculature.MT1-MMP-血小板衍生生长因子受体-β轴调节微血管的壁细胞包绕。
Genes Dev. 2005 Apr 15;19(8):979-91. doi: 10.1101/gad.1294605. Epub 2005 Apr 1.
9
Membrane-type 1 matrix metalloproteinase is required for normal alveolar development.正常肺泡发育需要膜型1基质金属蛋白酶。
Dev Dyn. 2005 Apr;232(4):1079-90. doi: 10.1002/dvdy.20267.
10
Distinctive functions of membrane type 1 matrix-metalloprotease (MT1-MMP or MMP-14) in lung and submandibular gland development are independent of its role in pro-MMP-2 activation.膜型1基质金属蛋白酶（MT1-MMP或MMP-14）在肺和下颌下腺发育中的独特功能独立于其在原MMP-2激活中的作用。
Dev Biol. 2005 Jan 1;277(1):255-69. doi: 10.1016/j.ydbio.2004.09.033.

MT1-MMP的第二个二聚体界面，即跨膜结构域，对于细胞表面的ProMMP-2激活至关重要。

The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface.

作者信息

Itoh Yoshifumi, Ito Noriko, Nagase Hideaki, Seiki Motoharu

机构信息

Department of Matrix Biology, Imperial College London, Hammersmith, London W6 8LH, UK.

出版信息

J Biol Chem. 2008 May 9;283(19):13053-62. doi: 10.1074/jbc.M709327200. Epub 2008 Mar 12.

DOI:10.1074/jbc.M709327200
PMID:18337248
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2442350/
Abstract

Activation of proMMP-2 and cell surface collagenolysis are important activities of membrane-type 1 matrix metalloproteinase (MT1-MMP) to promote cell migration in tissue, and these activities are regulated by homodimerization of MT1-MMP on the cell surface. In this study, we have identified the transmembrane domain as a second dimer interface of MT1-MMP in addition to the previously identified hemopexin domain. Our analyses indicate that these two modes of dimerization have different roles; transmembrane-dependent dimerization is critical for proMMP-2 activation, whereas hemopexin-dependent dimerization is important for degradation of collagen on the cell surface. Our finding provides new insight into the potential molecular arrangement of MT1-MMP contributing to its function on the cell surface.

摘要

前基质金属蛋白酶-2（proMMP-2）的激活和细胞表面胶原溶解是膜型1基质金属蛋白酶（MT1-MMP）促进组织中细胞迁移的重要活性，并且这些活性受MT1-MMP在细胞表面的同源二聚化调节。在本研究中，我们除了先前确定的血红素结合蛋白结构域外，还确定了跨膜结构域是MT1-MMP的第二个二聚体界面。我们的分析表明这两种二聚化模式具有不同的作用；跨膜依赖性二聚化对proMMP-2的激活至关重要，而血红素结合蛋白依赖性二聚化对细胞表面胶原的降解很重要。我们的发现为MT1-MMP在细胞表面发挥功能的潜在分子排列提供了新的见解。