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J Zündorf

Publications and source records attributed to J Zündorf.

5 recordsLinked to original sources

Effect of melanin and carotenoids of Exophiala (Wangiella) dermatitidis on phagocytosis, oxidative burst, and killing by human neutrophils.

The black yeast Exophiala (Wangiella) dermatitidis is an increasingly recognized pathogen and a leading cause of severe pheohyphomycosis. Melanin is thought to contribute to the virulence of E. dermatitidis. Whereas the synthesis and the redox properties of melanin have been studied intensively, the influence of melanin and carotenoids on the phagocytosis, the oxidative burst, and the killing of E. dermatitidis by human neutrophils has not been studied. To study their effects on these phenomena, we applied a combination of flow cytometry and a colony-count-dependent method. Using E. dermatitidis wild-type strain 8565 and several melanin-deficient mutants that have been described previously, we demonstrate that melanin prevents this pathogen from being killed in the phagolysosome of the neutrophils. Melanin did not influence the phagocytosis or the oxidative burst of the neutrophils involved. The carotenoids torulene and torularhodine were not found to contribute to the prevention of killing. The ability of E. dermatitidis to block the effects of the neutrophil oxidative burst may critically impair the potential of the host to sufficiently eliminate this fungal pathogen and thus may play an important role in the pathogenesis of phaeohyphomycosis.

Adult↗

Monitoring of redox-state of respiratory enzymes and myoglobin oxygenation in the working rat heart in normoxia and oxygen deficiency.

The cellular oxygen supply in the isolated, hemoglobin-free perfused, working rat heart can be determined by measurements of myoglobin oxygenation. However, for a precise analysis of mitochondrial hypoxia and anoxia (pO2 < 0.01 Torr) redox-state of respiratory enzymes must be known. By use of the EMPHO (Frank et al. 1989) it is possible to perform a high speed spectrometry within very small tissue volumes. Because of the characteristic absorption spectra of oxygenated and deoxygenated myoglobin and of the oxidized and reduced cytochrome aa3 within the wavelength interval from 500 to 630 nm it is possible to isolate these two pigments from the remission spectra and to determine the oxygenation state of myoglobin and the redox-state of cytochrom aa3.

Animals↗