Characterization and interactions of a fragment of the core protein of the small proteoglycan (PGII) from bovine tendon
- 29 October 1987
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 148 (2), 658-663
- https://doi.org/10.1016/0006-291x(87)90927-2
Abstract
Sequence analysis showed that Staphylococcus aureus V8 protease cleaved the core protein of the small dermatan sulfate proteoglycan of bovine tendon (PGII) on the carboxy side of a glutamic acid residue located 17 amino acids from the N-terminus of the intact molecule. The remaining 40 kDa core protein fragment inhibited collagen fibrillogenesis in an in vitro assay. V8 protease readily generated this fragment in tendon tissue, but it was not released from the tissue during treatment. These results indicate that neither the 17-amino acid N-terminal peptide nor the glycosaminoglycan chain attached to this peptide is required for maintaining the interaction of this proteoglycan with a collagen matrix.Keywords
This publication has 6 references indexed in Scilit:
- The Effect of Proteoglycans on the Morphology of Collagen Fibrils Formed In VitroCollagen and Related Research, 1987
- A role for disulphide bridges in the protein core in the interaction of proteodermatan sulphate and collagenBiochemical and Biophysical Research Communications, 1986
- The core proteins of large and small interstitial proteoglycans from various connective tissues form distinct subgroupsBiochemical Journal, 1985
- Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendonBiochemical Journal, 1984
- [43] Analysis of phenylthiohydantoins by ultrasensitive gradient high-performance liquid chromatographyMethods in enzymology, 1983
- Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap regionBiochemical Journal, 1981