1,720,976 research outputs found
Antimorphogenic effects of 2-deoxy-d-glucose in Candida albicans.
No full textAbstract 2-Deoxy-d-glucose (dGlc) is able to inhibit both N-acetyl-hexosamine-induced chlamydosporogenesis and N-acetyl-glucosamine- or proline-induced germ-tube formation in Candida albicans. This inhibition is exerted also at dGlc concentrations which do not affect growth in the yeast form and do not reduce either the uptake or the incorporation of N-acetyl-d-glucosamine (GlcNAc) into yeast or hyphal cell material. Inhibition of germtube formation by dGlc does not occur in serum and is fully reversed by glucose. It is suggested that dGlc acts as a potent antimorphogenic effector in C. albicans
Nutrition-dependent modulations of proteins synthesis in Candida albicans during germ-tube formation or maintenance of the yeast form in N-acetyl-d-glucosamine media.
No full textAbstract Stationary phase, yeast-form cells of Candida albicans grown in glucose-yeast extract medium were shifted to N-acetylglucosamine (GlcNAc) and/or glucose medium, and the pattern of protein synthesized under conditions of a progressive decrease in the rate of total protein synthesis was analyzed by SDS-PAGE and autoradiography.
Marked temporal modulations in the rate of synthesis of some cytoplasmic proteins were detected both in cells forming germ-tubes (at 37°C) and in yeast cells (at 28°C). The major modulated components showed molecular weights of 63, 53, 48 and 34 kDa. These products could not be qualified as heat-shock or heat-stroke proteins, because analogous modulations were observed on shifting cells from 28°C to 37°C or from 28°C to 28°C. However, no marked modulations in the synthesis of specific proteins were detected when amino acids were added to the medium fostering germ-tube formation under conditions of unimpaired overall rate of protein synthesis.
It is suggested that the modulations observed in cells incubated in GlcNAc-glucose medium could represent a response to a nutritional stress
Analysis of cell wall proteins and their role in morphogenesis and cell differentiation in Candida albicans.
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Modulations of proteins synthesis associated with temperature shift in the pathogenic fungs Candida albicans.
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Possible participation of polymorphonuclear cells stimulated by microbial immunomodulators in the dysregulated cytokine patterns of AIDS patients
No full textProtein synthesis and aminoacid pool during yeast- mycelial transition induced by N-acetyl-d-glucosamine in Candida albicans.
No full textProtein synthesis at different stages of yeast-mycelial transition induced by N-aCetyl-Dglucosamine
in Candida albicans was evaluated by following incorporation of radioactive amino
acids into the acid-insoluble cellular material. In passing from the early germ-tube formation
(60-90 min) to the mature hyphal cell (240-270 min) there was a marked decrease in the capacity
for protein synthesis. Apparently, this decrease was not due to a decreased amino acid uptake
into the soluble cellular pool or to exhaustion of carbonlenergy source in the inducing medium
with consequent arrest of growth. Protein synthesis, however, did not decay when amino acids
at high concentration were added to the medium fostering the yeast-mycelial transition and this
effect was potentiated by glucose.
Analysis of the intracellular amino acid pool showed that both germ-tubes and hyphal cells
were relatively depleted of several amino acids as compared to the yeast-form cells, whereas in
the hyphae there was a higher concentration of glutamic acid/glutamine, the latter being the predominant
component. These modulations in amino acid pool composition were not seen when
yeasts were converted to hyphae in an amino acid-rich induction medium. This study
emphasizes that yeast-form cells of C. albicans may efficiently convert to the mycelial form even
under a progressively lowered rate of protein synthesis, and suggests that initiation of hyphal
morphogenesis in the presence of N-acetyl-D-glucosamine is somehow separated from cellular
growth
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