Vanadate Activated Akt and Promoted S Phase Entry

Details

• Personal Author:
  Gao N ; He H ; Huang C ; Luo J ; Shi X ; Zhang Z
• Description:
  Protein kinase B (PKB)/Akt and its upstream signal transducer, phosphatidylinosito-3 kinase (PI3K) play an essential role in control of transcription and translation, which impact cell growth, survival, and metabolism. Transcription factor E2F is a component of the downstream proliferative machinery regulated by Akt. Hyperphosphorylation of retinoblastoma protein (pRb), a pocket protein, leads to release of E2F1, resulting in transition from G1 to S phase. The present study shows that in normal C141 cells, vanadate treatment increased the percentage of cells at S phase and elevated cyclin E and cyclin A expression. Vanadate treatment triggered phosphorylation of pRb and release of E2F1. Furthermore, vanadate increased Akt kinase activity and caused its phosphorylation at Ser473 and Thr308. Inhibition of Akt by either inhibitors or transfected cells with dominant negative kinase mutant or dominant negative phosphorylation mutant decreased the percentage of the cells at the S phase induced by vanadate, and reduced both cyclin E and E2F1 expression and phosphorylation of pRb. The present study indicates that Akt plays an essential role in vanadate-induced increase in cell number at S phase and transition from G1 to S phase through E2F-pRb pathway. [Description provided by NIOSH]
• Subjects:
  Cells, Cultured Energy Metabolism Enzymes Occupational Health Safety
• Keywords:
  Akt Author Keywords: Vanadate Cell-cultures Cell-function Cell-growth Cell-metabolism Cell Cycle Regulation Cellular-function Cellular-reactions E2F1 Enzyme-activity Metabolism PI3K PRb Proteins

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• ISSN:
  0300-8177
• Document Type:
  Text
• Genre:
  Journal Article
• Place as Subject:
  New York ; OSHA Region 2 ; OSHA Region 3 ; West Virginia
• CIO:
  National Institute for Occupational Safety and Health (NIOSH)
• Division:
  HELD - Health Effects Laboratory Division
• Topic:
  Workplace Safety & Health
• Location:
  North America
• Pages in Document:
  227-237
• Volume:
  255
• Issue:
  1
• NIOSHTIC Number:
  nn:20025982
• Citation:
  Mol Cell Biochem 2004 Jan; 255(1-2):227-237
• Contact Point Address:
  X. Shi, Pathology and Physiology Research Branch, National Institute for Occupational Safety and Health, 1095 Willowdale Road, Morgantown, WV 26505
• Email:
  xshi@cdc.gov
• Federal Fiscal Year:
  2004
• Peer Reviewed:
  True
• Source Full Name:
  Molecular and Cellular Biochemistry
• Collection(s):
  National Institute for Occupational Safety and Health
• Main Document Checksum:
  urn:sha-512:19ccdb0a64c71cec7cd769ed48ac34b597741421bafe3076c05c30087ef304f95034d44e888ce3c835eb550de1d38ffd3682d44389b9b48ef6a5ccfa22e78342
• Download URL:
  https://stacks.cdc.gov/view/cdc/197133/cdc_197133_DS1.pdf
• File Type:
  [PDF - 249.03 KB ]