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Träfflista för sökning "WFRF:(Singer W.) srt2:(1995-1999)"

Search: WFRF:(Singer W.) > (1995-1999)

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  • Harvey, P, et al. (author)
  • The electric field instrument on the Polar satellite
  • 1995
  • In: Space Science Reviews. - 0038-6308 .- 1572-9672. ; 71, s. 583-596
  • Journal article (peer-reviewed)abstract
    • The Polar satellite carries a system of four wire booms in the spacecraft spin plane and two rigid booms along the spin axis. Each of the booms has a spherical sensor at its tip along with nearby guard and stub surfaces whose potentials relative to that of their sphere are controlled by associated electronics. The potential differences between opposite sphere pairs are measured to yield the three components of the DC to >1 MHz electric field. Spheres can also be operated in a mode in which their collected current is measured to give information on the plasma density and its fluctuations. The scientific studies to be performed by this experiment as well as the mechanical and electrical properties of the detector system are described.
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  • Lark, Michael W., et al. (author)
  • Aggrecan degradation in human cartilage : Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints
  • 1997
  • In: Journal of Clinical Investigation. - 0021-9738. ; 100:1, s. 93-106
  • Journal article (peer-reviewed)abstract
    • To examine the activity of matrix metalloproteinases (MMPs) and aggrecanase in control and diseased human articular cartilage, metabolic fragments of aggrecan were detected with monospecific antipeptide antibodies. The distribution and quantity of MMP-generated aggrecan G1 fragments terminating in VDIPEN341 were compared with the distribution of aggrecanase-generated G1 fragments terminating in NITEGE373. Both types of G1 fragments were isolated from osteoarthritic cartilage. The sizes were consistent with a single enzymatic cleavage in the interglobular domain region, with no further proteolytic processing of these fragments. Both neoepitopes were also detected by immunohistochemistry in articular cartilage from patients undergoing joint replacement for osteoarthritis (OA), rheumatoid arthritis (RA), and in cartilage from adults with no known joint disease. In control specimens, the staining intensity for both G1 fragments increased with age, with little staining in cartilage from 22-wk-old fetal samples. There was also an increase with age in the extracted amount of MMP- generated neoepitope in relation to both aggrecan and collagen content, confirming the immunohistochemical results. After the age of 20-30 yr this relationship remained at a steady state. The staining for the MMP-generated epitope was most marked in control cartilage exhibiting histological signs of damage, whereas intense staining for the aggrecanase-generated fragment was often noted in adult cartilage lacking overt histological damage. Intense staining for both neoepitopes appeared in the more severely fibrillated, superficial region of the tissue. Intense immunostaining for both VDIPEN- and NITEGE-neoepitopes was also detected in joint cartilage from patients with OA or RA. Cartilage in these specimens was significantly more degraded and high levels of staining for both epitopes was always seen in areas with extensive cartilage damage. The levels of extracted VDIPEN neoepitope relative to collagen or aggrecan in both OA and RA samples were similar to those seen in age-matched control specimens. Immunostaining for both types of aggrecan fragments was seen surrounding the cells but also further removed in the interterritorial matrix. In some regions of the tissue, both neoepitopes were found while in others only one was detected. Thus, generation and/or turnover of these specific catabolic aggrecan fragments is not necessarily coordinated. Our results are consistent with the presence in both normal and arthritic joint cartilage of proteolytic activity against aggrecan based on both classical MMPs and 'aggrecanase'.
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