Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 68.65  (1)
  • Key words: Macrophage metalloelastase — Activation — Cartilage degradation  (1)
  • 1
    ISSN: 1420-908X
    Keywords: Key words: Macrophage metalloelastase — Activation — Cartilage degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. Objective and Design: Identify and characterize the matrix metalloproteinase responsible for cartilage proteoglycan degradation mediated by a macrophage cell line in a cell culture model that resembles some aspects of rheumatoid pannus.¶Materials or Subjects: Supernatants from the transformed mouse macrophage cell line J774A.1 were used to purify the proteoglycan degrading activity.¶Methods: J774A.1 macrophage culture supernatants were purified by sequential column chromatography and proteins were identified by zymography, western blotting and amino acid sequence analysis. Cartilage degradation was measured using 35S labeled bovine nasal cartilage.¶Results: The cartilage degrading proteolytic activity in the mouse macrophage supernatants proved to be due to two major proteins with approximate molecular masses of 48 kDa and 22 kDa that were identified as macrophage metalloelastase (MME). Incubation of purified MME at 37°C for up to 16 h resulted in the processing of the 48 kDa protein to several novel bands including a previously undescribed protein of ∼25 kDa without accumulation of fully processed 22 kDa protein. A number of proteinases increased the rate of this processing. J774A.1 macrophage metalloelastase degraded cartilage proteoglycan with an efficiency approximately equal to human macrophage metalloelastase (MMP-12) and matrilysin (MMP-7) and twice that of stromelysin-1 (MMP-3).¶Conclusions: These data identify the cartilage proteoglycan degrading metalloproteinase secreted by J774A.1 macrophages in this cell culture model as MME, and describes mechanisms of activation and processing of this enzyme that may play an important role in cartilage degradation.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 93 (1994), S. 277-297 
    ISSN: 1434-6036
    Keywords: 75.30.K ; 68.65 ; 25.40.F
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Stage-2 CoCl2-GIC approximates a two-dimensional easy-plane (XY) ferromagnet on a triangular lattice. It has been found in prior work to order in two steps, with the intermediate phase showing long-ranged ferromagnetic correlations within the intercalate plane, but no correlations between neighboring planes. We have probed the wave vector and temperature dependence of the static and dynamic spin correlations in detail, including measurements of the critical scattering, the quasielastic scattering from vortex diffusion and the spin wave excitations with and without an external magnetic field. Some of the predictions for a Kosterlitz-Thouless type transition are met in this compound, at least qualitatively, including an apparent jump in the spin stiffness at the critical point and the existence of a diffusive central peak in the scattering function possibly originating from vortex autocorrelations. However, there are some inconsistencies between our observations and recent analytical studies as well as Monte Carlo-molecular dynamics simulations of the vortex dynamics that prevent unambigous assignment of the upper critical temperature as a vortex-binding transition.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...