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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European journal of clinical pharmacology 3 (1971), S. 102-105 
    ISSN: 1432-1041
    Keywords: Indomethacin ; cortisol ; protein-binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Simultaneous determinations of free and protein bound plasma cortisol and of the concentrations of cortisol in skin biopsies were performed after treatment with indomethacin. Neither after a single dose nor in patients on continuous treatment, were any consistent changes found in the protein binding of plasma cortisol. However, in patients treated for more than 3 weeks a significantly greater number of skin biopsies were observed with very low concentrations of cortisol. No relation between the free fraction of plasma cortisol and the tissue cortisol could be demonstrated.In vitro experiments showed no alteration of the protein binding of cortisol after the addition of indomethacin to plasma. It is concluded that indomethacin does not have antirheumatic activity because of displacement of the protein bound plasma cortisol as proposed by other workers. However, long term treatment with indomethacin does seem to influence the tissue distribution of cortisol. The possible relationship of this observation is discussed in view of reported fatalities after long continued indomethacin treatment.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European journal of clinical pharmacology 4 (1972), S. 119-124 
    ISSN: 1432-1041
    Keywords: Indomethacin ; protein-binding ; salicylic acid ; plasma kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The fluorometric method of Holt & Hawkins (1965) has been modified to permit determination of 50 ng indomethacin in 0.5 ml plasma, by measuring its fluorescence in a phosphate buffer at pH 11.6 instead of sodium hydroxide. The method has also been adapted to show the presence of salicylic acid and a column chromatographic method has been devised for its removal. The protein binding of indomethacin in human plasma was calculated to be about 90% from an association constant of 0.86×103 M−1 (M=molarity). The number of binding sites on albumin is about 15. The plasma levels of indomethacin in patients receiving continuous treatment with Indocid® were between 0.5 and 3 µg/ml during the 4–5 h immediately after the last dose of 25 mg. The disappearance of indomethacin from plasma appears to consist of a fast primary phase at plasma concentrations greater than 1 µg/ml (T 1/2 about 90 min.), and a slower secondary phase.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0021-9304
    Keywords: surface topography ; plasma etching ; cellular orientation ; focal adhesion point ; in vitro ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: During this study, microtechnology and plasma etching were used to produce gratings 1.0 (TiD01), 2.0 (TiD02), 5.0 (TiD05), and 10.0 μm wide (TiD10) into commercially pure titanium wafers. After incubation of rat dermal fibroblast (RDFs) on these surfaces for 3 days, the cells were observed with scanning electron (SEM), transmission electron (TEM), and confocal laser scanning microscopy (CLSM). Results showed that the RDFs as a whole and their stress fibers oriented strictly parallel to the surface pattern on the TiD01 and TiD02 surfaces. On the TiD05 and TiD10 surfaces, this orientation was not observed. In addition, TEM and CLSM demonstrated that the focal adhesion points (FAP) were located mainly on the surface pattern ridges. TEM revealed that FAP were wrapped occasionally around the edges of the ridges. Only the RDFs on both the TiD05 and TiD10 surfaces protruded into the grooves and possessed FAP on the walls of the grooves. Attachment to the groove floor was observed only on the TiD10 textures. Comparison of these results with earlier observations on microtextured silicone rubber substrata suggests that material-specific properties do not influence the orientational effect of the surface texture on the observed RDF cellular behavior. The proliferation rate of the RDFs, however, seems to be much higher on titanium than on silicone rubber substrata. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 40, 425-433, 1998.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0021-9304
    Keywords: surface topography ; actin ; vinculin ; fibronectin ; vitronectin ; grooves ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The microfilaments and vinculin-containing attachment complexes of rat dermal fibroblasts (RDF) incubated on microtextured surfaces were investigated with confocal laser scanning microscopy (CLSM) and digital image analysis (DIA). In addition, depositions of bovine and endogenous fibronectin and vitronectin were studied. Smooth and microtextured silicone substrata were produced that possessed parallel surface grooves with a groove and ridge width of 2.0, 5.0, and 10.0 μm. The groove depth was approximately 0.5 μm. CLSM and DIA make it possible to visualize and analyze intracellular and extracellular proteins and the underlying surface simultaneously. It was observed that the microfilaments and vinculin aggregates of the RDFs on the 2.0 μm grooved substrata were oriented along the surface grooves after 1, 3, 5, and 7 days of incubation while these proteins were significantly less oriented on the 5.0 and 10.0 μm grooved surfaces. Vinculin was located mainly on the surface ridges on all textured surfaces. In contrast, bovine and endogenous fibronectin and vitronectin were oriented along the surface grooves on all textured surfaces. These proteins did not seem to be hindered by the surface grooves since many groove-spanning filaments were found on all the microgrooved surfaces. In conclusion, it can be said that microtextured surfaces influence the orientation of intracellular and extracellular proteins. Although results corroborate three earlier published hypotheses, they do not justify a specific choice of any one of these hypotheses. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 40, 291-300, 1998.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
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