Keene D R, Ridgway C C, Iozzo R V
Shriners Hospital for Children, Portland, Oregon 97201, USA.
J Histochem Cytochem. 1998 Feb;46(2):215-20. doi: 10.1177/002215549804600210.
Immunolocalization studies demonstrate that Type VI collagen forms a flexible network that interweaves among collagen fibrils in the dermis of skin as well as in other loose connective tissues. Although binding of Type VI collagen with other matrix components has been suggested, no structural evidence supporting these studies has been reported. In this study, we demonstrate that Type VI microfilaments consistently crossbanded collagen fibrils near the "d" band, indicating that the interaction of Type VI collagen with banded fibrils is not passive. This "d" band is also the location of the binding domain of decorin to banded fibrils, suggesting that decorin mediates the interaction of Type VI microfilaments with banded fibers. Examination of the architecture of the Type VI network in a decorin nullizygous mouse demonstrates a continuance of this specific interaction, indicating that the association is not entirely dependent on the presence of decorin. At least one other component, whose identity is uncertain, persists near the "d" band, which may also serve to mediate the attachment of Type VI collagen to collagen fibrils.
免疫定位研究表明,VI型胶原蛋白形成一个灵活的网络,该网络在皮肤真皮层以及其他疏松结缔组织中的胶原纤维之间相互交织。尽管有人提出VI型胶原蛋白与其他基质成分存在结合,但尚未有支持这些研究的结构证据报道。在本研究中,我们证明VI型微丝在“d”带附近始终与胶原纤维交叉带化,表明VI型胶原蛋白与带状纤维的相互作用并非被动的。这个“d”带也是核心蛋白聚糖与带状纤维结合域的位置,这表明核心蛋白聚糖介导了VI型微丝与带状纤维的相互作用。对核心蛋白聚糖基因敲除小鼠中VI型网络结构的检查表明这种特定相互作用持续存在,这表明这种关联并不完全依赖于核心蛋白聚糖的存在。至少还有一种身份不明的其他成分在“d”带附近持续存在,它也可能有助于介导VI型胶原蛋白与胶原纤维的附着。