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Late embryogenesis abundant proteins protect human hepatoma cells during acute desiccation.(APPLIED BIOLOGICAL SCIENCES)(Report)(Author abstract)

Expression of late embryogenesis abundant (LEA) proteins is highly correlated with desiccation tolerance in anhydrobiotic animals, selected land plants, and bacteria. Genes encoding two LEA proteins, one localized to the cytoplasm/nucleus (AfrLEA2) and one targeted to mitochondria (AfrLEA3m), were s... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States Dec 18, 2012, Vol.109(51), p.20859(6)
Main Author: Li, Shumin
Other Authors: Chakraborty, Nilay , Borcar, Apurva , Menze, Michael A. , Toner, Mehmet , Hand, Steven C.
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424
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recordid: gale_ofa314347484
title: Late embryogenesis abundant proteins protect human hepatoma cells during acute desiccation.(APPLIED BIOLOGICAL SCIENCES)(Report)(Author abstract)
format: Article
creator:
  • Li, Shumin
  • Chakraborty, Nilay
  • Borcar, Apurva
  • Menze, Michael A.
  • Toner, Mehmet
  • Hand, Steven C.
subjects:
  • Embryonic Development -- Physiological Aspects
  • Embryonic Development -- Health Aspects
  • Proteins -- Health Aspects
  • Proteins -- Physiological Aspects
  • Hepatocellular Carcinoma -- Physiological Aspects
  • Hepatocellular Carcinoma -- Development And Progression
  • Cancer Cells -- Physiological Aspects
  • Cancer Cells -- Health Aspects
ispartof: Proceedings of the National Academy of Sciences of the United States, Dec 18, 2012, Vol.109(51), p.20859(6)
description: Expression of late embryogenesis abundant (LEA) proteins is highly correlated with desiccation tolerance in anhydrobiotic animals, selected land plants, and bacteria. Genes encoding two LEA proteins, one localized to the cytoplasm/nucleus (AfrLEA2) and one targeted to mitochondria (AfrLEA3m), were stably transfected into human HepG2 cells. A trehalose transporter was used for intracellular loading of this disaccharide. Cells were rapidly and uniformly desiccated to low water content (
language: English
source:
identifier: ISSN: 0027-8424
fulltext: fulltext
issn:
  • 0027-8424
  • 00278424
url: Link


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titleLate embryogenesis abundant proteins protect human hepatoma cells during acute desiccation.(APPLIED BIOLOGICAL SCIENCES)(Report)(Author abstract)
creatorLi, Shumin ; Chakraborty, Nilay ; Borcar, Apurva ; Menze, Michael A. ; Toner, Mehmet ; Hand, Steven C.
ispartofProceedings of the National Academy of Sciences of the United States, Dec 18, 2012, Vol.109(51), p.20859(6)
identifierISSN: 0027-8424
subjectEmbryonic Development -- Physiological Aspects ; Embryonic Development -- Health Aspects ; Proteins -- Health Aspects ; Proteins -- Physiological Aspects ; Hepatocellular Carcinoma -- Physiological Aspects ; Hepatocellular Carcinoma -- Development And Progression ; Cancer Cells -- Physiological Aspects ; Cancer Cells -- Health Aspects
descriptionExpression of late embryogenesis abundant (LEA) proteins is highly correlated with desiccation tolerance in anhydrobiotic animals, selected land plants, and bacteria. Genes encoding two LEA proteins, one localized to the cytoplasm/nucleus (AfrLEA2) and one targeted to mitochondria (AfrLEA3m), were stably transfected into human HepG2 cells. A trehalose transporter was used for intracellular loading of this disaccharide. Cells were rapidly and uniformly desiccated to low water content (<0.12 g [H.sub.2]0/g dry weight) with a recently developed spin-drying technique. Immediately on rehydration, control cells without LEA proteins or trehalose exhibited 0% membrane integrity, compared with 98% in cells loaded with trehalose and expressing AfrLEA2 or AfrLEA3m; surprisingly, AfrLEA3m without trehalose conferred 94% protection. Cell proliferation across 7 d showed an 18-fold increase for cells dried with AfrLEA3m and trehalose, compared with 27-fold for nondried controls. LEA proteins dramatically enhance desiccation tolerance in mammalian cells and offer the opportunity for engineering biostability in the dried state. water stress | biopreservation | intrinsically disordered proteins | osmolyte | Artemia franciscana www.pnas.org/cgi/doi/ 10.1073/pnas.1214893109
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titleLate embryogenesis abundant proteins protect human hepatoma cells during acute desiccation.(APPLIED BIOLOGICAL SCIENCES)(Report)(Author abstract)
descriptionExpression of late embryogenesis abundant (LEA) proteins is highly correlated with desiccation tolerance in anhydrobiotic animals, selected land plants, and bacteria. Genes encoding two LEA proteins, one localized to the cytoplasm/nucleus (AfrLEA2) and one targeted to mitochondria (AfrLEA3m), were stably transfected into human HepG2 cells. A trehalose transporter was used for intracellular loading of this disaccharide. Cells were rapidly and uniformly desiccated to low water content (<0.12 g [H.sub.2]0/g dry weight) with a recently developed spin-drying technique. Immediately on rehydration, control cells without LEA proteins or trehalose exhibited 0% membrane integrity, compared with 98% in cells loaded with trehalose and expressing AfrLEA2 or AfrLEA3m; surprisingly, AfrLEA3m without trehalose conferred 94% protection. Cell proliferation across 7 d showed an 18-fold increase for cells dried with AfrLEA3m and trehalose, compared with 27-fold for nondried controls. LEA proteins dramatically enhance desiccation tolerance in mammalian cells and offer the opportunity for engineering biostability in the dried state. water stress | biopreservation | intrinsically disordered proteins | osmolyte | Artemia franciscana www.pnas.org/cgi/doi/ 10.1073/pnas.1214893109
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abstractExpression of late embryogenesis abundant (LEA) proteins is highly correlated with desiccation tolerance in anhydrobiotic animals, selected land plants, and bacteria. Genes encoding two LEA proteins, one localized to the cytoplasm/nucleus (AfrLEA2) and one targeted to mitochondria (AfrLEA3m), were stably transfected into human HepG2 cells. A trehalose transporter was used for intracellular loading of this disaccharide. Cells were rapidly and uniformly desiccated to low water content (<0.12 g [H.sub.2]0/g dry weight) with a recently developed spin-drying technique. Immediately on rehydration, control cells without LEA proteins or trehalose exhibited 0% membrane integrity, compared with 98% in cells loaded with trehalose and expressing AfrLEA2 or AfrLEA3m; surprisingly, AfrLEA3m without trehalose conferred 94% protection. Cell proliferation across 7 d showed an 18-fold increase for cells dried with AfrLEA3m and trehalose, compared with 27-fold for nondried controls. LEA proteins dramatically enhance desiccation tolerance in mammalian cells and offer the opportunity for engineering biostability in the dried state. water stress | biopreservation | intrinsically disordered proteins | osmolyte | Artemia franciscana www.pnas.org/cgi/doi/ 10.1073/pnas.1214893109
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date2012-12-18