@article { ISI:000302335800008,
	title = {Trehalose as an indicator of desiccation stress in Drosophila melanogaster larvae: a potential marker of anhydrobiosis},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {419},
	number = {4},
	year = {2012},
	month = {MAR},
	pages = {638-642},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>In the current scenario of global climate change, desiccation is considered as one of the major environmental stressors for the biota exposed to altered levels of ambient temperature and humidity. Drosophila melanogaster, a cosmopolitan terrestrial insect has been chosen as a humidity-sensitive bioindicator model for the present study since its habitat undergoes frequent stochastic and/or seasonally aggravated dehydration regimes. We report here for the first time the occurrence of anhydrobiosis in D. melanogaster larvae by subjecting them to desiccation stress under laboratory conditions. Larvae desiccated for ten hours at \&lt;5\% relative humidity could enter anhydrobiosis and could revive upon rehydration followed by resumption of active metabolism. As revealed by FIR and HPLC analyzes, our findings strongly indicated the synthesis and accumulation of trehalose in the desiccating larvae. Biochemical measurements pointed out the desiccation-responsive trehalose metabolic pathway that was found to be coordinated in concert with the enzymes trehalose 6-phosphate synthase and trehalase. Further, an inhibitor-based experimental approach using deoxynojirimycin, a specific trehalase inhibitor, demonstrated the pivotal role of trehalose in larval anhydrobiosis of D. melanogaster. We therefore propose trehalose as a potential marker for the assessment of anhydrobiosis in Drosophila. The present findings thus add to the growing list of novel biochemical markers in specific bioindicator organisms for fulfilling the urgent need of environmental biomonitoring of climate change. (C) 2012 Elsevier Inc. All rights reserved.</p>},
	keywords = {Anhydrobiosis, biomarker, Deoxynojirimycin, Desiccation, Drosophila melanogaster, trehalose},
	issn = {0006-291X},
	doi = {10.1016/j.bbrc.2012.02.065},
	author = {Thorat, Leena J. and Gaikwad, Sushama M. and Nath, Bimalendu B.}
}
@article { ISI:000353901700002,
	title = {Insect trehalase: physiological significance and potential applications},
	journal = {Glycobiology},
	volume = {25},
	number = {4},
	year = {2015},
	month = {APR},
	pages = {357-367},
	publisher = {OXFORD UNIV PRESS INC},
	address = {JOURNALS DEPT, 2001 EVANS RD, CARY, NC 27513 USA},
	abstract = {<p>Trehalose, a non-reducing disaccharide, is widespread throughout the biological world. It is the major blood sugar in insects playing a crucial role as an instant source of energy and in dealing with abiotic stresses. The hydrolysis of trehalose is under the enzymatic control of trehalase. The enzyme trehalase is gaining interest in insect physiology as it regulates energy metabolism and glucose generation via trehalose catabolism. The two forms of insect trehalase namely, Tre-1 and Tre-2, are important in energy supply, growth, metamorphosis, stress recovery, chitin synthesis and insect flight. Insect trehalase has not been reviewed in depth and the information available is quite scattered. The present mini review discusses our recent understanding of the regulation, mechanism and biochemical characterization of insect trehalase with respect to its physiological role in vital life functions. We also highlight the molecular and biochemical properties of insect trehalase that makes it amenable to competitive inhibition by most glycosidase inhibitors. Due to its crucial role in carbon metabolism in insects, application of inhibitors against trehalose can form a promising area towards formulating strategies for insect pest control.</p>},
	keywords = {carbohydrate metabolism, glycosidase inhibitor, glycoside hydrolase, trehalase, trehalose},
	issn = {0959-6658},
	doi = {10.1093/glycob/cwu125},
	author = {Shukla, Ekta and Thorat, Leena J. and Nath, Bimalendu B. and Gaikwad, Sushama M.}
}
