• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文学位 >Matrix metalloproteinase activation and induction in keratinocytes by a purified thiol-proteinase from Porphyromonas gingivalis.
【24h】

Matrix metalloproteinase activation and induction in keratinocytes by a purified thiol-proteinase from Porphyromonas gingivalis.

机译：牙龈卟啉单胞菌中纯化的巯基蛋白酶在角质形成细胞中激活基质金属蛋白酶。

获取原文
获取原文并翻译 | 示例
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Connective tissue remodelling is, currently, a poorly understood process that occurs during growth and development as well as in the chronic inflammatory diseases (the arthritides and periodontitis) and tumor metastasis. In the past decade a family of vertebrate enzymes called matrix metalloproteinases (MMPs) were found to be associated with these remodelling processes. The MMPs are a family of nine or more zinc-metalloproteinases secreted as zymogens and when activated can, collectively, degrade most or all the known extracellular matrix (ECM) proteins.; Periodontitis is a unique model for ECM remodelling because degradation of the hard and soft tissues supporting the teeth results from a chronic bacterial infection. During the disease process, tooth-supporting collagen fibers close to the bacterial infection are degraded while the epithelium surrounding the tooth migrates into the space left by the dissolved collagen, ultimately resulting in loss of the tooth. The source of the enzymes responsible for this ECM degradation is not known. We have previously shown that live epithelial cells (keratinocytes) growing on type I collagen fibers can be stimulated to degrade the collagen substrate by the addition of bacterial culture fluid from Porphyromonas gingivalis, a microorganism highly associated with the incidence and severity of periodontitis in adults. The factor within the P. gingivalis culture medium responsible for this stimulating effect was identified as a thiol-proteinase and characterized as an aggregate of peptides all derived from internal hydrolysis of a 140 kDa precursor proteinase. The P. gingivalis proteinase demonstrated the ability to activate MMPs, including collagenase, and when applied to live keratinocytes in culture stimulated the induction of MMP mRNA levels resulting in highly localized collagen-substrate degradation by the keratinocytes. These results are some of the first to define the potential relationship between proteinase activity released by P. gingivalis and epithelial cells with regard to matrix remodelling. Given the close proximity that the bacteria, the epithelium, and the collagenous attachment apparatus share in periodontitis, these data suggest that activation and induction of MMPs in the epithelial cells by pathogenic bacteria such as P. gingivalis may promote the accelerated tissue destruction in periodontitis.
机译：目前，结缔组织重塑是一个鲜为人知的过程，其发生在生长和发育以及慢性炎性疾病（关节炎和牙周炎）和肿瘤转移过程中。在过去的十年中，发现一种被称为基质金属蛋白酶（MMP）的脊椎动物酶家族与这些重塑过程有关。 MMP是一类九种或多种锌-金属蛋白酶，以酶原的形式分泌，被激活后可以共同降解大多数或所有已知的细胞外基质（ECM）蛋白。牙周炎是ECM重塑的独特模型，因为支持牙齿的硬组织和软组织的降解是由慢性细菌感染引起的。在疾病过程中，靠近细菌感染的支持牙齿的胶原纤维降解，而牙齿周围的上皮迁移到溶解的胶原所留下的空间中，最终导致牙齿脱落。导致这种ECM降解的酶的来源尚不清楚。我们以前已经表明，通过添加来自牙龈卟啉单胞菌的细菌培养液可以刺激在I型胶原纤维上生长的活上皮细胞（角质形成细胞）降解胶原蛋白底物，该细菌培养液与成人牙周炎的发生和严重程度高度相关。牙龈卟啉单胞菌培养基中负责该刺激作用的因子被鉴定为硫醇蛋白酶，并表征为全部源自140kDa前体蛋白酶的内部水解的肽的聚集体。牙龈卟啉单胞菌蛋白酶具有激活包括胶原酶在内的MMP的能力，当应用于培养的角质形成细胞时，可刺激MMP mRNA水平的诱导，导致角质形成细胞高度定位的胶原底物降解。这些结果是首次确定牙龈卟啉单胞菌释放的蛋白酶活性与上皮细胞在基质重塑之间的潜在关系的一些结果。鉴于细菌，上皮细胞和胶原附着装置在牙周炎中的共享程度非常接近，这些数据表明，致病菌（如牙龈卟啉单胞菌）对上皮细胞中MMP的激活和诱导可能促进牙周炎中组织的加速破坏。

著录项

  • 作者

    DeCarlo, Arthur Anthony, Jr.;

  • 作者单位

    The University of Alabama at Birmingham.;

  • 授予单位 The University of Alabama at Birmingham.;
  • 学科 Biology Microbiology.; Chemistry Biochemistry.; Health Sciences Dentistry.
  • 学位 Ph.D.
  • 年度 1994
  • 页码 130 p.
  • 总页数 130
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 微生物学;生物化学;口腔科学;
  • 关键词

  • 入库时间 2022-08-17 11:49:44

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号