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  • 1
    Electronic Resource
    Electronic Resource
    Regulation of interleukin-1β and tumor necrosis factor secretion by the human monocytic leukemia cell line, THP-1 (1989)
    Springer
    Inflammation research 27 (1989), S. 271-273 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Activated macrophages synthesize and release the potent polypeptides, interleukin-1 (IL-1) and tumor necrosis factor (TNF). In an effort to identify the cellular signals which control cytokine production by activated macrophages, we have developed anin vitro model employing the human THP-1 cell line. In the present study, THP-1 cells “primed” by 1.6 μM phorbol 12-myristate-13-acetate (TPA) for 4 hr demonstrated a dose-and time-dependent release of IL-1β and TNF upon activation by 20 μg/ml LPS. BSA/anti-BSA-coated latex beads were also a potent stimulus for IL-1β secretion. Moreover, the combination of a suboptimal concentration of LPS (200 ng/ml) plus interferon-γ (0.03–333 U/ml) greatly enhanced IL-1β production. Resting THP-1 monocytes not “primed” by TPA did not secrete IL-1β or TNF. These distinct patterns of cytokine production may be related to the developmental stages of macrophage activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01972794
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Cytokine production in whole bloodex vivo (1991)
    Springer
    Inflammation research 34 (1991), S. 49-52 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Interleukin-1β (IL-1β) and tumor necrosis factor-α (TNF-α) have been reported to contribute to the pathogenesis of many inflammatory diseases, e.g., rheumatoid arthritis. As monocytes are believed to be the primary source of these cytokines in peripheral blood, the present study was conducted to establish ranges and patterns of IL-1β and TNF-α secretion. Using heparinized unseparated whole blood obtained from normal human volunteers, peripheral blood monocytes were stimulated withSal. minnesota LPS or BSA/anti-BSA immune complex-coated beads (BSA-beads). ELISAs for IL-1β and TNF-α were employed to quantitate cytokine levels in blood plasma without performing arduous and time-consuming extraction procedures. Over the course of a 6 hr incubation, LPS elicited a dose-dependent increase in TNF-α and IL-1β production. Preincubation of whole blood with interferon-γ prior to the addition of a suboptimal dose of LPS or BSA-beads resulted in a synergistic potentiation of IL-1β/TNF-α production. Dexamethasone, utilized in the treatment of rheumatoid arthritis, proved to be a potent inhibitor of cytokine biosynthesis in whole bloodex vivo. The measurement of cytokine biosynthesis in a relevant physiologic environment not only avoids non-specific monocyte activation, but also may increase our ability to predict clinical outcomes in rheumatoid arthritis and/or other inflammatory diseases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01993235
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a tight-binding MMP-3 inhibitor using improved fluorescence spectroscopy techniques (1993)
    Springer
    Inflammation research 39 (1993), S. C189 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Accurate kinetic characterization of stromelysin (MMP-3) inhibitors is critical in the design of potent inhibitors of this enzyme. We have successfully modified a previously described assay [1] which used an internally quenched peptide substrate (Dnp-PYAYWMR) that, upon cleavage by MMP-3, produces the products, Dnp-PYA (quiet) and YWMR (a fluorophore at 360 nm). This improved assay uses purified human MMP-3 in the presence of either 5% methanol or 5% DMSO. Fluorescence intensities associated with total hydrolysis of substrate by enzyme have been successfully mimicked using a combination of the product peptides as a standard. We have determined aK m of 39.2 μM andK cat/K m of 4.6 μM/h for MMP-3 (in 5% MeOH) using this peptide substrate. This assay was used successfully to characterize Ro 31-4724 ((N-[(N-[2-[(N-hydroxycarbamoyl)methyl]-4-methyl-valeryl]-L-leucyl]-L-alanine ethyl ester) as a reversible, tightly binding, inhibitor with aK i of 26 nm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01972762
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Peptides based on the conserved prodomain sequence of matrix metalloproteinases inhibit human stromelysin and collagenase (1993)
    Springer
    Inflammation research 39 (1993), S. C148 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Prostromelysin, a member of the family of matrix metalloproteinases, is secreted as a zymogen which is activated after cleavage of the His81−Phe82 bond. The 82 amino acid propeptide that is removed during activation contains 12 amino acids, MRKPRC75GVPDVG, that are highly conserved in all MMPs. We evaluated a series of peptides that span this region for their ability to inhibit stromelysin. The hexapeptide, Ac-RCGVPD, and the pentapeptide, Ac-RCGVP had IC50 values of approx. 10 μM. The tetrapeptide, Ac-RCGV, was somewhat less potent with an IC50 of 60 μM. Smaller peptides, e. g. Ac-RCG, were significantly less potent as inhibitors. Substitutions of Cys75 with Ser resulted in a complete loss of inhibitory activity. The peptides in this series also inhibited human fibroblast collagenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01972749
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    Paper (German National Licenses)
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