Type V collagen: molecular structure and fibrillar organization of the chicken alpha 1(V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis.

摘要: Previous work from our laboratories has demonstrated that: (a) the striated collagen fibrils of corneal stroma are heterotypic structures composed type V molecules coassembled along with those I collagen, (b) high content within is one factor responsible for small, uniform fibrillar diameter (25 nm) characteristic this tissue, (c) completely processed form found tissues retains a large noncollagenous region, termed NH2-terminal domain, at amino end its alpha 1 chain, and (d) domain may contain least some information observed regulation fibril diameters. In present investigation we have employed polyclonal antibodies against retained 1(V) chain immunohistochemical studies embryonic avian corneas immunoscreening chicken cDNA library. When combined sequencing molecular rotary shadowing, these approaches provide on structure as well how might function in structure. immunofluorescence immunoelectron microscopy analyses, react mature stroma. Thus, epitopes portion exposed surface. This marked contrast to mAbs which previously characterized being directed located major triple helical molecule. The recognized by antigenically masked that been assembled into fibrils. Sequencing isolated clones provided conceptual acid sequence entire procollagen chain. shows location what appear be potential propeptidase cleavage sites. One these, if preferentially used during processing molecule, can an explanation retention data also suggest consists several regions, providing fits molecule visualized shadowing.