Proteoglycan-degrading activity of human stromelysin-1 and leukocyte elastase in rabbit joints. Quantitation of proteoglycan and a stromelysin-induced HABR fragment of aggrecan in synovial fluid and cartilage.

Autor: Olszewski JM; Department of Pharmacology, Merck Research Laboratories, Rahway, New Jersey 07065, USA., Moore VL, McDonnell J, Williams H, Saphos CA, Green BG, Knight WB, Chapman KT, Hagmann WK, Dorn CP, Hale JJ, Mumford RA
Jazyk: angličtina
Zdroj: Connective tissue research [Connect Tissue Res] 1996; Vol. 33 (4), pp. 291-9.
DOI: 10.3109/03008209609028887
Abstrakt: The objective of this study was to compare the specificity and potency of recombinant human SLN-1 (rhSLN) and human leukocyte elastase (HLE) as proteoglycan (PG)-degrading enzymes after intraarticular injection into rabbits. Another objective was to evaluate the elicitation of a rhSLN-induced hyaluronan-binding region (HABR) fragment from rabbit aggrecan in joints using a polyclonal antiserum (anti-FVDIPEN) against the synthetic peptide, Phe-Val-Asp-Ile-Pro-Glu-Asn (FVDIPEN). The intraarticular injection of either activated rhSLN or HLE resulted in enzyme-specific quantitative release of PG fragments into synovial fluid. Based on the criteria used herein, HLE appears to be a more potent PG-degrading enzyme than SLN. Intraarticular injection of rhSLN also resulted in time- and dose-dependent release of a new HABR fragment of aggrecan (HABR-FMDIPEN) into both articular cartilage and synovial fluid. HABR-FVDIPEN is likely to be a good marker of matrix metalloproteinase (MMP)-induced degradation of aggrecan.
Databáze: MEDLINE