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基质金属蛋白酶2在动脉瘤和正常主动脉壁内的定位。

Localization of matrix metalloproteinase 2 within the aneurysmal and normal aortic wall.

作者信息

Crowther M, Goodall S, Jones J L, Bell P R, Thompson M M

机构信息

Departments of Surgery and Pathology, Clinical Sciences Building, Leicester Royal Infirmary, Leicester LE2 7LX, UK.

出版信息

Br J Surg. 2000 Oct;87(10):1391-400. doi: 10.1046/j.1365-2168.2000.01554.x.

Abstract

BACKGROUND

Current research has shed new light on the role of matrix metalloproteinase (MMP) 2 in the development of abdominal aortic aneurysms (AAAs). MMP-2 is a major protease in the wall of small aneurysms and is produced at increased levels by smooth muscle cells derived from AAAs compared with normal controls. In vivo, MMP-2 is produced as an inactive proenzyme that is activated predominantly by the cell membrane-bound enzyme, membrane type 1 matrix metalloproteinase (MT1-MMP). This study investigated the production of the MMP-2-MT1-MMP-tissue inhibitor of metalloproteinases (TIMP) 2 system within the wall of aortic aneurysms and in age-matched control arterial tissue.

METHODS

Arterial tissue from four patients with aortic aneurysms and four age-matched aortic samples was examined for the production and expression of MMP-2, TIMP-2 and MT1-MMP protein using immunohistochemistry, in situ hybridization and in situ zymography.

RESULTS

All components of the MMP-2-TIMP-2-MT1-MMP enzyme system were detected in the arterial wall of both aneurysm and control samples, specifically in the medial tissue. The enzymes co-localized with medial smooth muscle cells. Gelatinolytic activity was localized to elastin fibres in normal and aneurysmal aorta.

CONCLUSION

The presence of MT1-MMP within the media of arterial tissue suggests a powerful pathway for the activation of MMP-2. The localization of the MMP-2-TIMP-2-MT1-MMP enzyme system to the medial layer of the arterial wall gives support to the concept that this system may play an aetiological role in the pathogenesis of AAAs.

摘要

背景

目前的研究为基质金属蛋白酶(MMP)2在腹主动脉瘤(AAA)发展中的作用带来了新的认识。MMP-2是小动脉瘤壁中的主要蛋白酶,与正常对照相比,源自AAA的平滑肌细胞产生的MMP-2水平升高。在体内,MMP-2以无活性的酶原形式产生,主要由细胞膜结合酶膜型1基质金属蛋白酶(MT1-MMP)激活。本研究调查了主动脉瘤壁和年龄匹配的对照动脉组织中MMP-2-MT1-金属蛋白酶组织抑制剂(TIMP)2系统的产生情况。

方法

使用免疫组织化学、原位杂交和原位酶谱法,对4例主动脉瘤患者的动脉组织和4个年龄匹配的主动脉样本进行MMP-2、TIMP-2和MT1-MMP蛋白的产生和表达检测。

结果

在动脉瘤和对照样本的动脉壁中均检测到MMP-2-TIMP-2-MT1-MMP酶系统的所有成分,特别是在内膜组织中。这些酶与内膜平滑肌细胞共定位。明胶酶活性定位于正常和动脉瘤主动脉的弹性纤维。

结论

动脉组织中膜内存在MT1-MMP提示了一条激活MMP-2的强大途径。MMP-2-TIMP-2-MT1-MMP酶系统定位于动脉壁的中层,支持了该系统可能在AAA发病机制中起病因学作用的观点。

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