Molecular cloning, sequencing and expression of cDNA encoding human trehalase

Ishihara, Reiko; Taketani, Shigeru; Sasai-Takedatsu, Misa; Kino, Motoki; Tokunaga, Rikio; Kobayashi, Yohnosuke

doi:10.1016/s0378-1119(97)00455-1

Cited by 63 publications

(40 citation statements)

References 27 publications

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“…1), as observed in the membrane-bound trehalases in silkworm B. mori (trehalase-2), 7) brine shrimp A. franciscana, 19) rabbit, 22) and human 34) ( Fig. 3).…”

Section: Homologs Of the Trehalasementioning

confidence: 74%

Molecular Cloning of cDNA for Trehalase from the European Honeybee,Apis melliferaL., and Its Heterologous Expression inPichia pastoris

Lee

Saito

Mori

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…1), as observed in the membrane-bound trehalases in silkworm B. mori (trehalase-2), 7) brine shrimp A. franciscana, 19) rabbit, 22) and human 34) ( Fig. 3).…”

Section: Homologs Of the Trehalasementioning

confidence: 74%

Molecular Cloning of cDNA for Trehalase from the European Honeybee,Apis melliferaL., and Its Heterologous Expression inPichia pastoris

Lee

Saito

Mori

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…Enzymes involved in trehalose metabolism must be considered as a potential target in the search for new antifungal compounds (31,32), since the sugar is absent from mammal cells, whereas trehalase is located in the brush border membranes of epithelial cells and in the kidney proximal tube (59). Previous work showed that in C. albicans, TPS1 and TPS2 genes are factors of virulence (30 -32).…”

Section: Discussionmentioning

confidence: 99%

The ATC1 Gene Encodes a Cell Wall-linked Acid Trehalase Required for Growth on Trehalose in Candida albicans

Pedreño

Maicas

Argüelles

et al. 2004

Journal of Biological Chemistry

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After screening a Candida albicans genome data base, the product of an open reading frame (IPF 19760/ CA2574) with 41% identity to Saccharomyces cerevisiae vacuolar acid trehalase (Ath1p) was identified and named Atc1p. The deduced amino acid sequence shows that Atc1p contains an N-terminal hydrophobic signal peptide and 20 potential sites for N-glycosylation. C. albicans homozygous mutants that lack acid trehalase activity were constructed by gene disruption at the two ATC chromosomal alleles. Analysis of these null mutants shows that Atc1p is localized in the cell wall and is required for growth on trehalose as a carbon source. An Atc1p endowed with acid trehalase activity was obtained by an in vtro transcription-translation coupled system. These results strongly suggest that ATC1 is the structural gene encoding cell wall acid trehalase in C. albicans. Determinations of ATC1 mRNA expression as well as acid trehalase activity in the presence and absence of glucose point out that ATC1 gene is regulated by glucose repression.

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“…Many organisms use trehalose as a go-between between carbohydrate storage as glycogen and the cellular availability of glucose for energy needs (besides the other cellular roles trehalose plays in the cells' economy as an anti-stress factor): Why is this the case? Vertebrates have foregone altogether the use of trehalose, but still possess unique trehalose-degrading enzymes (trehalases; for example, human trehalase, used to digest trehalose from the diet and garner the glucose moieties within [37]). What advantages do trehalose imparts that has assured its selection in many diverse organisms (bacteria, algae, plants, fungi, invertebrates including insects), yet its loss in the vertebrate lineage?…”

Section: Why Trehalose? Physicochemical Properties Of Trehalosementioning

confidence: 99%