Interaction Between Amino Propeptides of Type XI Procollagen 1 Chains
نویسندگان
چکیده
منابع مشابه
Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen.
A key question relating to procollagen biosynthesis is the way in which closely related procollagen chains discriminate between each other to assemble in a type-specific manner. Intracellular assembly of procollagen occurs via an initial interaction between the C-propeptides followed by vectorial propagation of the triple-helical domain in the C to N direction. Recognition signals within the C-...
متن کاملCharacterization of type III procollagen from chick embryo blood vessels.
The precursors of collagen types I and III were extracted from radioactively labeled chick embryo blood vessels. Procollagen III was found to consist of three identical proa III chains, each containing a large amino and a large carboxyl propeptide. Interchain disulfide bridges occur at three locations: between the amino propeptides, the carboxyl propeptides, and within the vertebrate collagenas...
متن کاملAssembly and processing of procollagen type III in chick embryo blood vessels.
The processing of [3H]proline-labeled procollagen III in excised chick embryo blood vessels was found to differ significantly from that of procollagen I in the same tissue. While first the amino propeptides and then the carboxyl propeptides were fairly rapidly cleaved from procollagen I, only the carboxyl propeptides were split off procollagen III, leaving pN-collagen III. This intermediate, wh...
متن کاملProcollagen propeptide release by procollagen peptidases and bacterial collagenase.
Amino and carboxyl procollagen peptidases cleaved chick procollagen I to yield the intact amino propeptides and the disulfide-linked carboxyl propeptides, which were identified and partly characterized. The same products were released by these enzymes from the two separated fragments of procollagen produced by vertebrate collagenase, and this supports the concept that cleavage of amino and carb...
متن کاملIdentification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity.
Bone morphogenetic protein (BMP)-1, which belongs to the tolloid subgroup of astacin-like zinc metalloproteinases, cleaves the C-propeptides of procollagen at the physiologic site and is, therefore, a procollagen C-proteinase (PCP). Cleavage occurs between a specific alanine or glycine residue (depending on the procollagen chain) and an invariant aspartic acid residue in each of the three chain...
متن کامل