Wellcome Trust Centre for Cell-Matrix Research, The University of Manchester, Manchester, United Kingdom.
PLoS One. 2011;6(12):e29422. doi: 10.1371/journal.pone.0029422. Epub 2011 Dec 19.
In order to characterise the function of the novel fibrillar type XXVII collagen, a series of mice expressing mutant forms of the collagen were investigated. Mice harboring a glycine to cysteine substitution in the collagenous domain were phenotypically normal when heterozygote and displayed a mild disruption of growth plate architecture in the homozygous state. Mice expressing an 87 amino acid deletion in the collagenous domain of collagen XXVII were phenotypically normal as heterozygotes whereas homozygotes exhibited a severe chondrodysplasia and died perinatally from a lung defect. Animals expressing the 87 amino acid deletion targeted specifically to cartilage were viable but severely dwarfed. The pericellular matrix of proliferative chondrocytes was disrupted and the proliferative cells exhibited a decreased tendency to flatten and form vertical columns. Collagen XXVII plays an important structural role in the pericellular extracellular matrix of the growth plate and is required for the organisation of the proliferative zone.
为了研究新型纤维状 XXVII 型胶原的功能，研究了一系列表达突变型胶原的小鼠。杂合子状态下，胶原纤维结构域中甘氨酸突变为半胱氨酸的小鼠表型正常，但纯合子状态下生长板结构轻度破坏。在 XXVII 型胶原的胶原纤维结构域中表达 87 个氨基酸缺失的小鼠杂合子时表型正常，而纯合子时表现出严重的软骨发育不良，并因肺缺陷而在围产期死亡。特异性表达于软骨的 87 个氨基酸缺失的动物是有活力的，但严重矮小。增殖性软骨细胞的细胞周基质被破坏，增殖细胞的扁平并形成垂直柱的趋势减少。VII 型胶原在生长板的细胞周细胞外基质中起着重要的结构作用，对于增殖区的组织是必需的。
