Heat-shock inhibits protein synthesis and eIF-2 activity in cultured cortical neurons
(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
- Hu, Bing Ren ; Ou Yang, Yi Bing and Wieloch, Tadeusz LU
- organization
- publishing date
- 1993-09-01
- 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
-
- pmid:8232716
- scopus:0027328409
- 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}}, }