Matrix metalloproteinase-13 influences ERK signalling in articular rabbit chondrocytes

Osteoarthritis and Cartilage
L J RaggattN C Partridge

Abstract

Matrix metalloproteinase-13 (MMP-13) is an extracellular MMP that cleaves type II collagen, the major protein component of cartilage, with high specificity and has been implicated in the pathology of osteoarthritis. The present study aimed to characterize the binding and internalization kinetics of MMP-13 in normal rabbit chondrocytes and whether MMP-13 affected cell signalling. Rabbit chondrocytes were used in [125I]-MMP-13 binding assays to investigate the MMP-13 binding kinetics and Western analysis allowed for the assessment of intracellular signalling cascades. Rabbit chondrocytes were found to express the cartilage-specific genes aggrecan and type II collagen throughout their in vitro culture period. Appreciable specific cell-association of [125I]-MMP-13 was detected after 10 min of exposure to the ligand and equilibrium was obtained after 2 h. Binding of [125I]-MMP-13 to chondrocytes was specific and approached saturation at 75 nM. Internalization of MMP-13 was evident after 20 min, reached a maximum at 30 min and had returned to baseline by 90 min. Addition of receptor-associated protein (RAP) inhibited the internalization of MMP-13 indicating a likely role for low-density lipoprotein receptor-related protein-1 (LRP1) i...Continue Reading

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Citations

Sep 4, 2010·Critical Reviews in Biochemistry and Molecular Biology·Bénédicte Cauwe, Ghislain Opdenakker
Jun 19, 2008·Matrix Biology : Journal of the International Society for Matrix Biology·Eleonora MarsichSergio Paoletti
Apr 5, 2016·The Journal of Clinical Investigation·Jing FuSuzanne Lentzsch
Feb 21, 2019·American Journal of Physiology. Lung Cellular and Molecular Physiology·Sandra CabreraAnnie Pardo

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