引用本文:夏莉莉(综述),黄华艺(审校).血清可溶性基质金属蛋白酶与肿瘤关系的研究进展[J].中国临床新医学,2014,7(5):469-474.
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血清可溶性基质金属蛋白酶与肿瘤关系的研究进展
夏莉莉(综述),黄华艺(审校)
530021 南宁,广西壮族自治区人民医院检验科
摘要:
[摘要] 基质金属蛋白酶(MMPs)是一组含锌的细胞内蛋白酶家族,它们享有一些共同的结构域,但有不同的底物特异性、细胞来源和诱导性。MMPs的主要功能是降解和重塑细胞外基质的各个组分。目前已经发现的MMPs已达20多种,按它们的底物亲和性不同可把它们分为白明胶酶类(MMP-2和MMP-9)、间质胶原酶类(MMP-1、MMP-8和MMP-13)、广谱特异性间质溶解素(MMP-7和MMP-13)和其他类。MMPs活性与各种细胞的增殖、迁移和分化有关。MMPs降解细胞外基质,使肿瘤细胞向周围组织侵犯然后向远处转移。多种肿瘤组织中出现MMPs的过表达,血清中的MMPs浓度与组织中的表达呈平行关系并与患者的病程、预后和化疗药物敏感性有关。因此,测定血清/血浆中的MMPs含量具有方便、创伤小和花费低等优点,因而具有重要的临床意义。
关键词:  血清  基质金属蛋白酶  细胞外基质  肿瘤  转移
DOI:10.3969/j.issn.1674-3806.2014.05.30
分类号:R 730.4
基金项目:
Serum soluble matrix metalloproteinase and cancer
XIA Li-li, Huang Hua-yi
Department of Clinical Laboratories, the People′s Hospital of Guangxi Zhuang Autonomous Region, Nanning 530021, China
Abstract:
[Abstract] Matrix metalloproteinases(MMPs) are a group of zinc dependent extracellular protease family. MMPs share a common domain structure with different substrate specificity, different cellular origin and inducibility. The major function of MMPs is to degrade and remodel the extracellular components. There are more than 20 MMPs members have been confirmed so far. The MMPs can be categorized into gelatinase(MMP-2 and MMP-9), interstitial collagenase(MMP-1, MMP-8, and MMP-13), and other types based on their substrate specificity. Studies have demonstrated that the activity of MMPs is associated with cancer cell proliferation, migration, and differentiation. The degradation of extracellular matrix by MMPs results in the invasion, migration, and metastasis of cancer cells. Over expression of MMPs have been found in various types of tumors. Studies also showed that serum MMPs level is correlated with their tissue expression and associated with cancer progression, prognosis, and response to chemotherapy. Serum or plasma MMPs analysis is a simple, fast with low cost method, thus, it is very helpful in cancer diagnosis and prognosis prediction.
Key words:  Serum  Matrix metalloproteinase(MMPs)  Extra cellular matrix  Cancer  Metastasis