Hard Single Diffraction in pbarp Collisions at root-s = 630 and 1800 GeV

Using the D0 detector, we have studied events produced in proton-antiproton collisions that contain large forward regions with very little energy deposition (``rapidity gaps'') and concurrent jet production at center-of-mass energies of root-s = 630 and 1800 Gev. The fractions of forward and central jet events associated with such rapidity gaps are measured and compared to predictions from Monte Carlo models. For hard diffractive candidate events, we use the calorimeter to extract the fractional momentum loss of the scattered protons.Comment: 11 pages 4 figures. submitted to PR

Matrix metalloproteinase-13 influences ERK signalling in articular rabbit chondrocytes

Summary Objective 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. Methods 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. Results 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) in this process. Interestingly the presence of MMP-13 induced phosphorylation of the extracellular signal-regulated kinase 1/2 (ERK1/2) protein showing that there is initiation of a signalling process in response to MMP-13 being bound and internalized by rabbit chondrocytes. However, this activation does not involve the MMP-13 internalization receptor LRP1. Conclusion These studies demonstrate and characterize the MMP-13 binding and internalization system in rabbit chondrocytes and indicate that MMP-13 may regulate the phenotype of the chondrocytes through this receptor syste