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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have isolated a Candida albicans gene, coding for a putative peroxisomal carnitine acetyl transferase (CTN) protein, which is up-regulated during macrophage infection. In the present study, we describe the disruption of CTN3 gene (previously called CAT3) to gain insight into its potential role during infection. The ability of disrupted Candida mutants to filament was affected by several solid media. Northern blot analysis revealed that CTN3 gene may be involved not only in conditions of cell starvation but also during the process of germination. In agreement with the putative peroxisomal localization of the corresponding protein, we observed a strong glucose repression of CTN3 gene and, on the contrary, high level of transcription by carbon sources that induce the formation of peroxisomal proteins. Furthermore, we showed the existence of two additional C. albicans CTN encoding sequences, which are also induced during macrophage infection.
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PMID:Candida albicans CTN gene family is induced during macrophage infection: homology, disruption and phenotypic analysis of CTN3 gene. 1521 62

Periods of carbohydrate deprivation are commonly encountered by plant cells. Plants respond to this nutrient stress by the mobilization of stored carbohydrates and the reallocation of other cellular macromolecules to degradative pathways. Previously we identified a number of metabolic genes that are upregulated in Arabidopsis thaliana cells during sucrose starvation. One of the genes identified encodes acyl-CoA oxidase-4 (ACX4, EC 1.3.3.6), a peroxisomal acyl-CoA oxidase that is unique to plants and involved in beta-oxidation of short-chain fatty acids. Here we demonstrate that ACX4 activity increases during sucrose starvation, indicating a shift to a catabolic breakdown of fatty acids as a source of available carbon. This suggests a role for degradation of short-chain fatty acids in the response to sucrose starvation, leading in turn to the production of toxic H2O2. Catalase-3 (CAT3, EC 1.11.1.6) activity also increases during starvation as a direct response to the increase in oxidative stress caused by the rapid activation of alternative catabolic pathways, including a specific increase in ACX4 activity. Any disruption in ACX4 expression or in beta-oxidation of fatty acids in general prevents this increase in catalase activity and expression. We hypothesize that CAT3 activity increases to remove the H2O2 produced by alternative catabolic processes induced during the carbohydrate shortages caused by extended periods of low-light conditions.
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PMID:Increase in catalase-3 activity as a response to use of alternative catabolic substrates during sucrose starvation. 2013 75