Covalent crosslinking between molecules of type I and type III collagen. The involvement of the N-terminal, nonhelical regions of the alpha 1 (I) and alpha 1 (III) chains in the formation of intermolecular crosslinks.

摘要: Several peptides containing intermolecular crosslinks were isolated from tryptic digests of the insoluble matrix human leiomyoma and calf aorta. From type III collagen, two crosslinked isolated. The peptide [TN(III)]2, is a dimer which contains 73 amino-terminal residues two, zero-D staggered, α1(III) chains (D being distance by molecules or are staggered relative to each other). After de-blocking with pyroglutamate aminopeptidase, its amino acid sequence was determined be < Glu-Tyr-Asp-Ser-Tyr-Asp-Val-Xaa-Ser-Gly-Val-Ala-Val-Gly-Gly-Leu-Ala-Gly-Tyr-Hyp-Gly-. involvement [TN(III)]2 in formation 4D-staggered bonds demonstrated analysis [TN(III)2]×T(III). For this three-chained peptide, double corresponded TN(III) T(III), nine-residue carboxy-terminal helical crosslinking site found. Crosslinks between I collagens identified isolating TN(III)×TN(I) leiomyoma. This characterized, first digesting it collagenase giving rise ColN(III)×ColN(I) then chymotrypsin C(III) C(I). C(I) characteristic for collagens, respectively. Further, three-component crosslink-containing peptides, both aorta ColN(III)× ColN(I)× T(III) Col×N(III) T(I) regions 0D-staggered molecules, joined either an adjacent molecule. Crosslinked involving only collagen also [colN(III)]2 [CoIN(III)2]×T(III)]. As intramolecular can excluded isolation these that present within same fibrit OD stagger, bound crosslinks. significance findings respect proposed models fibres physiological properties extracellular matrix, discussed.