Ruggiero F, Pfäffle M, von der Mark K, Garrone R
Histologie Expérimentale, UA CNRS 244, Université Claude Bernard, Villeurbanne, France.
Cell Tissue Res. 1988 Jun;252(3):619-24. doi: 10.1007/BF00216649.
An antibody reacting with the C-propeptide of chick type-II procollagen was used in an attempt to localize this terminal extension of the procollagen molecule (by immunogold labelling) during early collagen fibrillogenesis in chondrocyte cultures. After 2 days in culture the chondrocytes were surrounded by pericellular type-II collagen, as demonstrated by an indirect immunofluorescence labelling technique. An electron microscopy study of these cultures showed that the collagen fibrils were thin (approximately 15 nm diameter), with a poorly visible cross striation, sometimes enhanced by slight thickenings. The antibody against the C-propeptide of type-II procollagen labelled most of the collagen fibrils, according to a very regular pattern constituting a 60 nm periodicity. After 3 days the label was still present on the pericellular collagen fibrils but disappeared from the collagen fibrils of the extracellular matrix. Our results indicate that the C-propeptide of type-II procollagen is retained in the newly formed fibrils.
一种与鸡Ⅱ型前胶原C-前肽发生反应的抗体,被用于通过免疫金标记在软骨细胞培养物早期胶原纤维形成过程中定位前胶原分子的这个末端延伸部分。培养2天后,软骨细胞被细胞周Ⅱ型胶原所包围,这通过间接免疫荧光标记技术得以证明。对这些培养物的电子显微镜研究表明,胶原纤维很细(直径约15纳米),横纹不太明显,有时会因轻微增粗而更清晰。抗Ⅱ型前胶原C-前肽的抗体按照构成60纳米周期的非常规则的模式标记了大部分胶原纤维。3天后,标记仍存在于细胞周胶原纤维上,但从细胞外基质的胶原纤维上消失了。我们的结果表明,Ⅱ型前胶原的C-前肽保留在新形成的纤维中。