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Human trehalase is a stress responsive protein in Saccharomyces cerevisiae.
Biochem Biophys Res Commun 2009; 379(2):621-5BB

Abstract

Three trehalases ATH1, NTH1, and NTH2 have been identified in Saccharomyces cerevisiae. ATH1, and NTH1 hydrolyze trehalose to glucose to provide energy and assist in recovery from stress. Human trehalase (TREH) is expressed in the intestine and kidney and probably hydrolyzes ingested trehalose in the intestine and acts as marker of renal tubular damage in kidney. Since trehalose is not present in circulation or kidney tubules, its renal effect suggests it has other yet unidentified actions. Here we examined the function of human trehalase in budding yeast. We constructed three yeast trehalase mutants (NTH1Delta, NTH2Delta, and ATH1Delta) and then transformed TREH into these mutants. NTH1Delta did not grow on media containing trehalose as the carbon source, and TREH did not rectify NTH1Delta dysfunction and also did not grow on trehalose medium, suggesting that TREH is not responsible for utilization of exogenous trehalose in yeast. In experiments involving exposure to heat, osmotic and oxidative stresses, NTH1Delta showed no recovery. Interestingly, ATH1Delta-TREH showed high sensitivity to all three stressors. ATH1Delta and NTH2Delta showed very low neutral trehalase activity and NTH1Delta did not show any neutral trehalase activity, and trehalose concentrations were higher. Increased neutral trehalase activity (equivalent to the wild type), reduction of trehalose content and brisk sensitivity to stressors were noted in TREH-ATH1Delta strain, but not in TREH-NTH1Delta or -NTH2Delta. Our results suggest that TREH acts as a stress-response protein in the kidney rather than involved in utilization of exogenous trehalose.

Authors+Show Affiliations

Department of Biochemistry 2, University of Yamanashi, Faculty of Medicine, 1110, Shimokato, Chuo, Yamanashi 409-3898, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

19126402

Citation

Ouyang, Yuhui, et al. "Human Trehalase Is a Stress Responsive Protein in Saccharomyces Cerevisiae." Biochemical and Biophysical Research Communications, vol. 379, no. 2, 2009, pp. 621-5.
Ouyang Y, Xu Q, Mitsui K, et al. Human trehalase is a stress responsive protein in Saccharomyces cerevisiae. Biochem Biophys Res Commun. 2009;379(2):621-5.
Ouyang, Y., Xu, Q., Mitsui, K., Motizuki, M., & Xu, Z. (2009). Human trehalase is a stress responsive protein in Saccharomyces cerevisiae. Biochemical and Biophysical Research Communications, 379(2), pp. 621-5. doi:10.1016/j.bbrc.2008.12.134.
Ouyang Y, et al. Human Trehalase Is a Stress Responsive Protein in Saccharomyces Cerevisiae. Biochem Biophys Res Commun. 2009 Feb 6;379(2):621-5. PubMed PMID: 19126402.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Human trehalase is a stress responsive protein in Saccharomyces cerevisiae. AU - Ouyang,Yuhui, AU - Xu,Qinghong, AU - Mitsui,Kazuhiro, AU - Motizuki,Mitsuyoshi, AU - Xu,Zhaojun, Y1 - 2009/01/04/ PY - 2008/12/16/received PY - 2008/12/20/accepted PY - 2009/1/8/entrez PY - 2009/1/8/pubmed PY - 2009/2/14/medline SP - 621 EP - 5 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 379 IS - 2 N2 - Three trehalases ATH1, NTH1, and NTH2 have been identified in Saccharomyces cerevisiae. ATH1, and NTH1 hydrolyze trehalose to glucose to provide energy and assist in recovery from stress. Human trehalase (TREH) is expressed in the intestine and kidney and probably hydrolyzes ingested trehalose in the intestine and acts as marker of renal tubular damage in kidney. Since trehalose is not present in circulation or kidney tubules, its renal effect suggests it has other yet unidentified actions. Here we examined the function of human trehalase in budding yeast. We constructed three yeast trehalase mutants (NTH1Delta, NTH2Delta, and ATH1Delta) and then transformed TREH into these mutants. NTH1Delta did not grow on media containing trehalose as the carbon source, and TREH did not rectify NTH1Delta dysfunction and also did not grow on trehalose medium, suggesting that TREH is not responsible for utilization of exogenous trehalose in yeast. In experiments involving exposure to heat, osmotic and oxidative stresses, NTH1Delta showed no recovery. Interestingly, ATH1Delta-TREH showed high sensitivity to all three stressors. ATH1Delta and NTH2Delta showed very low neutral trehalase activity and NTH1Delta did not show any neutral trehalase activity, and trehalose concentrations were higher. Increased neutral trehalase activity (equivalent to the wild type), reduction of trehalose content and brisk sensitivity to stressors were noted in TREH-ATH1Delta strain, but not in TREH-NTH1Delta or -NTH2Delta. Our results suggest that TREH acts as a stress-response protein in the kidney rather than involved in utilization of exogenous trehalose. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/19126402/Human_trehalase_is_a_stress_responsive_protein_in_Saccharomyces_cerevisiae_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(08)02558-8 DB - PRIME DP - Unbound Medicine ER -