Shakibaei M, Merker H J
Institut für Anatomie, Freie Universität Berlin, Königin-Luise-Strasse 15, D-14195 Berlin, Germany.
Cell Tissue Res. 1999 Jun;296(3):565-73. doi: 10.1007/s004410051318.
Integrins are cell-surface receptors that mediate cell attachment to extracellular matrix components. The pericellular matrix in cartilage not only is a mechanical framework, but is also important for chondrocyte differentiation and stabilization of the phenotype. The interaction between chondrocytes and pericellular matrix is mediated, in part, by integrin receptors. We have previously demonstrated the presence of beta1-integrins in the cartilage matrix of organoid culture of limb buds from 12-day-old mouse embryos by immunohistological methods. In order to corroborate these findings, we have further investigated the distribution of integrins in the cartilage matrix by immunoelectron microscopy and by immunoprecipitation methods. Cartilage tissue of limb buds of 17-day-old mouse embryos was treated with collagenase and the cell-free and cellular protein-free supernatant was removed and used for immunoprecipitation experiments. Immunoprecipitation with antibodies against beta1-, alpha1-, alpha3-, and alpha5beta1-integrins and collagen type II, followed by immunoblotting with the same antibodies, demonstrated the presence of these integrins and collagen type II in the supernatant. The integrins found in the cartilage matrix could have been either secreted or shed by the cells. The question as to whether they have a function in the cartilage matrix, such as interlinking, in the matrix organization or in the stabilization of matrix components remains to be elucidated.
整合素是介导细胞与细胞外基质成分附着的细胞表面受体。软骨中的细胞周围基质不仅是一个机械框架,对于软骨细胞分化和表型稳定也很重要。软骨细胞与细胞周围基质之间的相互作用部分是由整合素受体介导的。我们之前通过免疫组织学方法在12日龄小鼠胚胎肢芽类器官培养的软骨基质中证实了β1整合素的存在。为了证实这些发现,我们通过免疫电子显微镜和免疫沉淀方法进一步研究了整合素在软骨基质中的分布。用胶原酶处理17日龄小鼠胚胎肢芽的软骨组织,去除无细胞和无细胞蛋白的上清液并用于免疫沉淀实验。用抗β1、α1、α3和α5β1整合素以及II型胶原的抗体进行免疫沉淀,然后用相同抗体进行免疫印迹,证实上清液中存在这些整合素和II型胶原。在软骨基质中发现的整合素可能是细胞分泌的或脱落的。它们在软骨基质中是否具有诸如交联、基质组织或基质成分稳定等功能的问题仍有待阐明。