The C5 domain of Col6A3 is cleaved off from the Col6 fibrils immediately after secretion
The C5 domain of Col6A3 is cleaved off from the Col6 fibrils immediately after secretion
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DOI：
10.1006/bbrc.2001.6227
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发表时间：
2002-01-18
影响因子：
3.1
通讯作者：
Pöschl, E
中科院分区：
文献类型：
--
作者：
Aigner, T;Hambach, L;Pöschl, E
在关节软骨中，VI型胶原主要集中在细胞周围的基质中。在蛋白质的合成和加工过程中，至少α3链经历了显著的翻译后修饰和切割。在本研究中，我们研究了VI型胶原在关节软骨中的加工过程。用针对Alpha3(VI)C5结构域的特异性多克隆抗血清免疫染色显示，几乎所有关节软骨细胞都有很强的细胞染色。激光共聚焦扫描显微镜和免疫电子显微镜允许这种染色主要定位于细胞质和直接的细胞周围基质。双标记实验表明，C5结构域和细胞周围成熟的VI型胶原蛋白有很小的重叠。我们的结果表明，至少在成人关节软骨中，α3(VI)胶原的C5结构域被合成并最初结合到新形成的VI型胶原纤维中，但在分泌被切断后立即消失，不存在于关节软骨成熟的VI型细胞周围基质中。(C)2002年爱思唯尔科学公司。
In articular cartilage, type VI collagen is concentrated in the pericellular matrix compartment. During protein synthesis and processing at least the alpha3 chain undergoes significant posttranslational modification and cleavage. In this study, we investigated the processing of type VI collagen in articular cartilage. Immunostaining with a specific polyclonal antiserum against the C5 domain of alpha3(VI) showed strong cellular staining seen in nearly all chondrocytes of articular cartilage. Confocal laser-scanning microscopy and immunoelectron microscopy allowed localization of this staining mainly to the cytoplasm and the immediate pericellular matrix. Double-labeling experiments showed a narrow overlap of the C5 domain and the pericellular mature type VI collagen. Our results suggest that at least in human adult articular cartilage the C5 domain of alpha3(VI) collagen is synthesized and initially incorporated into the newly formed type VI collagen fibrils, but immediately after secretion is cut off and is not present in the mature pericellular type VI matrix of articular cartilage. (C) 2002 Elsevier Science.