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Heat-shock inhibits protein synthesis and eIF-2 activity in cultured cortical neurons

Hu, Bing Ren ; Ou Yang, Yi Bing and Wieloch, Tadeusz LU (1993) In Neurochemical Research 18(9). p.1003-1007
Abstract

Stress, such as heat-shock, hypoxia and hypoglycemia, inhibits the initiation of protein synthesis. The effects of heat-shock on protein synthesis, eucaryotic initiation factor 2 (eIF-2) activity, protein kinase C (PKC), and casein kinase II (CKII) activities were studied in primary cortical neuronal cultures. In neurons exposed to heat-shock at 44°C for 20 min, protein synthesis is inhibited by more than 80%, and is accompanied by a 60% decrease in eIF-2 activity. Steady state PKC and CK II activities were not affected by heat-shock. Vanadate (200 μM), a protein phosphotyrosine phosphatase inhibitor, partially prevented the depression of eIF-2 activity during heat-shock, and increased CKII activity by 90%. In contrast, staurosporine... (More)

Stress, such as heat-shock, hypoxia and hypoglycemia, inhibits the initiation of protein synthesis. The effects of heat-shock on protein synthesis, eucaryotic initiation factor 2 (eIF-2) activity, protein kinase C (PKC), and casein kinase II (CKII) activities were studied in primary cortical neuronal cultures. In neurons exposed to heat-shock at 44°C for 20 min, protein synthesis is inhibited by more than 80%, and is accompanied by a 60% decrease in eIF-2 activity. Steady state PKC and CK II activities were not affected by heat-shock. Vanadate (200 μM), a protein phosphotyrosine phosphatase inhibitor, partially prevented the depression of eIF-2 activity during heat-shock, and increased CKII activity by 90%. In contrast, staurosporine (62nM), a protein kinase C inhibitor, did not affect eIF-2 activity. We conclude that heat-shock causes a change in the phosphorylation/ dephosphorylation of regulatory proteins leading to a depressed eIF-2 activity and protein synthesis in neurons.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Brain, casein kinase II, heat-shock, initiation factor 2, protein phosphorylation, protein synthesis, tyrosine kinase
in
Neurochemical Research
volume
18
issue
9
pages
5 pages
publisher
Springer
external identifiers
  • scopus:0027328409
  • pmid:8232716
ISSN
0364-3190
DOI
10.1007/BF00966760
language
English
LU publication?
yes
id
c109093e-b4c0-420d-83ce-97fc51010a18
date added to LUP
2019-06-13 16:15:01
date last changed
2024-01-01 10:15:08
@article{c109093e-b4c0-420d-83ce-97fc51010a18,
  abstract     = {{<p>Stress, such as heat-shock, hypoxia and hypoglycemia, inhibits the initiation of protein synthesis. The effects of heat-shock on protein synthesis, eucaryotic initiation factor 2 (eIF-2) activity, protein kinase C (PKC), and casein kinase II (CKII) activities were studied in primary cortical neuronal cultures. In neurons exposed to heat-shock at 44°C for 20 min, protein synthesis is inhibited by more than 80%, and is accompanied by a 60% decrease in eIF-2 activity. Steady state PKC and CK II activities were not affected by heat-shock. Vanadate (200 μM), a protein phosphotyrosine phosphatase inhibitor, partially prevented the depression of eIF-2 activity during heat-shock, and increased CKII activity by 90%. In contrast, staurosporine (62nM), a protein kinase C inhibitor, did not affect eIF-2 activity. We conclude that heat-shock causes a change in the phosphorylation/ dephosphorylation of regulatory proteins leading to a depressed eIF-2 activity and protein synthesis in neurons.</p>}},
  author       = {{Hu, Bing Ren and Ou Yang, Yi Bing and Wieloch, Tadeusz}},
  issn         = {{0364-3190}},
  keywords     = {{Brain; casein kinase II; heat-shock; initiation factor 2; protein phosphorylation; protein synthesis; tyrosine kinase}},
  language     = {{eng}},
  month        = {{09}},
  number       = {{9}},
  pages        = {{1003--1007}},
  publisher    = {{Springer}},
  series       = {{Neurochemical Research}},
  title        = {{Heat-shock inhibits protein synthesis and eIF-2 activity in cultured cortical neurons}},
  url          = {{http://dx.doi.org/10.1007/BF00966760}},
  doi          = {{10.1007/BF00966760}},
  volume       = {{18}},
  year         = {{1993}},
}