Publications by authors named "Rex Oxford"
Article Synopsis
- Fibrillar collagens, mainly types V and XI, are crucial for the structure of connective tissues, with type XI playing a key regulatory role in collagen fibril assembly.
- A unique amino-terminal propeptide domain in these collagens has not yet been structurally determined, but modeling efforts based on related structures have suggested potential interactions with glycosaminoglycans and calcium.
- The study of existing collagen genes reveals that many contain a similar domain, which could enhance our understanding of the extracellular matrix and the effects of collagen XI deficiencies on skeletal growth disorders.
Type XI collagen is a quantitatively minor yet essential constituent of the cartilage extracellular matrix. The amino propeptide of the alpha1 chain remains attached to the rest of the molecule for a longer period of time after synthesis than the other amino propeptides of type XI collagen and has been localized to the surface of thin collagen fibrils. Yeast two-hybrid system was used to demonstrate that a homodimer of alpha1(XI) amino propeptide (alpha1(XI)Npp) could form in vivo.
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