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Elimination of damaged proteins during differentiation of embryonic stem cells

Hernebring, M ; Brolén, Gabriella LU ; Aguilaniu, H ; Semb, Henrik LU and Nystrom, T (2006) In Proceedings of the National Academy of Sciences 103(20). p.7700-7705
Abstract
During mammalian aging, cellular proteins become increasingly damaged: for example, by carbonylation and formation of advanced glycation end products (AGEs). The means to ensure that offspring are born without such damage are unknown. Unexpectedly, we found that undifferentiated mouse ES cells contain high levels of both carbonyls and AGEs. The damaged proteins, identified as chaperones and proteins of the cytoskeleton, are the main targets for protein oxidation in aged tissues. However, the mouse ES cells rid themselves of such damage upon differentiation in vitro. This elimination of damaged proteins coincides with a considerably elevated activity of the 20S proteasome. Moreover, damaged proteins were primarily observed in the inner cell... (More)
During mammalian aging, cellular proteins become increasingly damaged: for example, by carbonylation and formation of advanced glycation end products (AGEs). The means to ensure that offspring are born without such damage are unknown. Unexpectedly, we found that undifferentiated mouse ES cells contain high levels of both carbonyls and AGEs. The damaged proteins, identified as chaperones and proteins of the cytoskeleton, are the main targets for protein oxidation in aged tissues. However, the mouse ES cells rid themselves of such damage upon differentiation in vitro. This elimination of damaged proteins coincides with a considerably elevated activity of the 20S proteasome. Moreover, damaged proteins were primarily observed in the inner cell mass of blastocysts, whereas the cells that had embarked on differentiation into the trophectoderm displayed drastically reduced levels of protein damage. Thus, the elimination of protein damage occurs also during normal embryonic development in vivo. This clear-out of damaged proteins may be a part of a previously unknown rejuvenation process at the protein level that occurs at a distinct stage during early embryonic development. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
protein carbonylation, proteasome, embryogenesis, advanced glycation end products, aging
in
Proceedings of the National Academy of Sciences
volume
103
issue
20
pages
7700 - 7705
publisher
National Acad Sciences
external identifiers
  • pmid:16672370
  • wos:000237835900032
  • scopus:33646744719
ISSN
1091-6490
DOI
10.1073/pnas.0510944103
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Stem Cell and Pancreas Developmental Biology (013212044)
id
ddf2491f-6a58-47ae-b14a-fc1a020c446f (old id 407533)
date added to LUP
2016-04-01 12:33:22
date last changed
2021-06-30 01:31:49
@article{ddf2491f-6a58-47ae-b14a-fc1a020c446f,
  abstract     = {During mammalian aging, cellular proteins become increasingly damaged: for example, by carbonylation and formation of advanced glycation end products (AGEs). The means to ensure that offspring are born without such damage are unknown. Unexpectedly, we found that undifferentiated mouse ES cells contain high levels of both carbonyls and AGEs. The damaged proteins, identified as chaperones and proteins of the cytoskeleton, are the main targets for protein oxidation in aged tissues. However, the mouse ES cells rid themselves of such damage upon differentiation in vitro. This elimination of damaged proteins coincides with a considerably elevated activity of the 20S proteasome. Moreover, damaged proteins were primarily observed in the inner cell mass of blastocysts, whereas the cells that had embarked on differentiation into the trophectoderm displayed drastically reduced levels of protein damage. Thus, the elimination of protein damage occurs also during normal embryonic development in vivo. This clear-out of damaged proteins may be a part of a previously unknown rejuvenation process at the protein level that occurs at a distinct stage during early embryonic development.},
  author       = {Hernebring, M and Brolén, Gabriella and Aguilaniu, H and Semb, Henrik and Nystrom, T},
  issn         = {1091-6490},
  language     = {eng},
  number       = {20},
  pages        = {7700--7705},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {Elimination of damaged proteins during differentiation of embryonic stem cells},
  url          = {http://dx.doi.org/10.1073/pnas.0510944103},
  doi          = {10.1073/pnas.0510944103},
  volume       = {103},
  year         = {2006},
}