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Binding of type II collagen fragments to the surface of human articular chondrocytes.

机译：II型胶原蛋白片段与人关节软骨细胞表面的结合。

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摘要

Type II collagen binds to chondrocytes through integrins and Annexin V. While the potential integrin binding sites have been identified, it is unclear which domains bind to Annexin V. Proteolytic fragments of collagen are known to modulate cell signaling pathways resulting in degradation of articular cartilage; it is unknown whether Annexin V binds the fragments. One of the goals of this study was to determine the binding of type II collagen and its fragments to chondrocytes using flow cytometry and fluorescence microscopy. Our data suggest that the binding of the N-telopeptide of type II collagen is through Annexin V, while binding of the C-telopeptide and the triple helical peptide to the surface of chondrocytes are potentially facilitated through other collagen receptors, such as integrins and cell-associated matrix proteins.; One of the characteristics of Annexin V is that it is a calcium ion receptor. Most physiological processes utilize intracellular and/or extracellular calcium ions. Calcium ions within the cytosol act as a key intracellular second messenger and as an enzymatic cofactor. Therefore, intracellular calcium flux was measured upon N-telopeptide binding to Annexin V. Flow cytometry data demonstrated that upon N-telopeptide binding to the cell surface, calcium is rapidly released from intracellular stores. Calcium release was also observed with C-telopeptide and helical peptide, but to a lesser extent. In addition, chondrocyte cytosolic baseline calcium levels decreased after prolonged exposure to all three peptides. Further investigation with bradykinin, a known inflammatory agent, demonstrated a rapid release of stored calcium. The cells pre-treated with all three peptides seem to be more sensative to bradykinin than the cells treated with type II collagen. It may be hypothesized that in the diseased tissue cells that are exposed to fragments of type II collagen may have increased sensitivity to inflammatory stimuli that may be present in the matrix such as various cytokines.
机译：II型胶原蛋白通过整联蛋白和膜联蛋白V与软骨细胞结合。虽然已经确定了潜在的整联蛋白结合位点，但尚不清楚哪个结构域与膜联蛋白V结合。已知胶原蛋白水解蛋白片段可调节细胞信号传导途径，从而导致关节软骨降解。膜联蛋白V是否结合片段尚不清楚。这项研究的目标之一是使用流式细胞仪和荧光显微镜确定II型胶原及其片段与软骨细胞的结合。我们的数据表明，II型胶原蛋白的N-端肽的结合是通过膜联蛋白V进行的，而C-端肽和三螺旋肽与软骨细胞表面的结合可能通过其他胶原蛋白受体（例如整合素和细胞）来促进-相关的基质蛋白。膜联蛋白V的特征之一是它是钙离子受体。大多数生理过程利用细胞内和/或细胞外钙离子。胞质溶胶中的钙离子充当关键的细胞内第二信使和酶促辅因子。因此，在N-端肽与膜联蛋白V结合后测量细胞内钙通量。流式细胞仪数据表明，在N-端肽与细胞表面结合后，钙迅速从细胞内贮存中释放出来。 C-端肽和螺旋肽也观察到钙释放，但程度较小。此外，长时间暴露于所有三种肽后，软骨细胞胞质基线钙水平降低。缓激肽（一种已知的炎症剂）的进一步研究证明了所储存钙的快速释放。用所有三种肽预处理的细胞似乎比用II型胶原处理的细胞对缓激肽更敏感。可以假设，在患病组织中，暴露于II型胶原蛋白片段的细胞可能对基质中可能存在的炎性刺激（例如各种细胞因子）具有更高的敏感性。

著录项

  • 作者

    Lucic, Danijela.;

  • 作者单位

    Rush University.;

  • 授予单位 Rush University.;
  • 学科 Biology Cell.; Chemistry Biochemistry.
  • 学位 Ph.D.
  • 年度 2003
  • 页码 121 p.
  • 总页数 121
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 细胞生物学;生物化学;
  • 关键词

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