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  • 1990-1994  (2)
  • Cytokines  (1)
  • procaine isothiocyanate  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Leukaemia inhibitory factor stimulates proteoglycan resorption in porcine articular cartilage (1993)
    Springer
    Rheumatology international 13 (1993), S. 5-8 
    Details
    ISSN: 1437-160X
    Keywords: Arthritis ; Cytokines ; Chondrocytes ; Growth factors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Leukaemia inhibitory factor (LIF) is a secretory glycoprotein produced by tumour, mesenchymal and haemopoietic cells. LIF has been found to have pleiotropic actions that include the capacity to regulate cell differentiation, promote acute-phase protein synthesis and stimulate calcium release in bone explants. In view of its similarity to other cytokines that affect cartilage metabolism, the effects of LIF on proteoglycan resorption were examined in pig cartilage explants. Endotoxinfree recombinant mouse LIF was found to produce a dose-dependent increase in sulphated glycosaminoglycan (S-GAG) release (ED50=123 U/ml, approx. 25–50 pM). Statistically significant stimulation was observed with doses of 100 U/ml or greater. When pig cartilage was stimulated with maximum concentrations of LIF and either interleukin 1α (IL-1α), interleukin 1β (IL-1β) or tumour necrosis factor α (TNFα), in each case a significantly greater release of S-GAGs was observed than with the respective cytokines alone (P〈0.05). Comparison of the areas under the curves showed that the action of LIF was additive, and not synergistic with other catabolic cytokines. Dose-response studies showed that transforming growth factor β (TGFβ) produced a partial inhibition of LIF-stimulated release of S-GAGs (ED50=4.5 U/ml). Statistically significant inhibition was observed with doses of 2U/ml or greater. These results showed that LIF stimulated proteoglycan resorption in vitro and that this effect was modulated by other cytokines. Whether LIF contributes to the progressive destruction of cartilage in septic or chronic inflammatory arthritis remains to be determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290327
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Procaine isothiocyanate: An irreversible inhibitor of the specific binding of [3H]batrachotoxinin-A benzoate to sodium channels (1990)
    Springer
    Neurochemical research 15 (1990), S. 441-448 
    Details
    ISSN: 1573-6903
    Keywords: Local anesthetic ; procaine ; procaine isothiocyanate ; sodium channel ; batrachotoxin ; synaptoneurosome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract [3H]Batrachotoxinin-A benzoate ([3H]BTX-B) binds with high affinity to sites on voltage sensitive sodium channels in synaptoneurosomes from guinea pig cerebral cortex. Local anesthetics competitively antagonize the binding of [3H]BTX-B. An irreversible local anesthetic, procaine isothiocyanate (PRIT) and a tritiated derivative ([3H]PRIT) have been prepared. PRIT inhibits the binding of [3H]BTX-B in a noncompetitive, irreversible manner (apparent Ki=13 μM) whereas the parent compound, procaine, inhibits in a competitive, reversible manner (Ki=40 μM). The dissociation rate of [3H]BTX-B from sites on the sodium channel is greatly accelerated in a concentration dependent manner in the presence of PRIT. A 50% increase in the dissociation rate of [3H]BTX-B is achieved in the presence of 0.98 μM PRIT. [3H]PRIT binds irreversibly to three proteins in synaptoneurosomes with apparent molecular weights of 20, 42, and 68 kDa. Protection studies with procaine and other local anesthetics suggest that only the 68 kDa species was related to local anesthetic binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00969931
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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