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Digitale Medien

Cartilage proteoglycan degradation by a mouse transformed macrophage cell line is mediated by macrophage metalloelastase (1999)

Janusz, M. J. ; Hare, M. ; Durham, S. L. ; [weitere]

Springer

Inflammation research 48 (1999), S. 280-288

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ISSN: 1420-908X

Schlagwort(e): Key words: Macrophage metalloelastase — Activation — Cartilage degradation

Quelle: Springer Online Journal Archives 1860-2000

Thema: Medizin

Notizen: 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/s000110050460

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Digitale Medien

Two dimensional XY type magnetism in intercalated graphite: an elastic and inelastic neutron scattering study (1994)

Wiesler, D. G. ; Zabel, H. ; Shapiro, S. M.

Springer

The European physical journal 93 (1994), S. 277-297

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ISSN: 1434-6036

Schlagwort(e): 75.30.K ; 68.65 ; 25.40.F

Quelle: Springer Online Journal Archives 1860-2000

Thema: Physik

Notizen: 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01312698

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