Mitogen-activated protein (MAP) kinases are serine/threonine protein kinases that are activated rapidly in cells stimulated by various extracellular signals. With stimulation of quiescent cells by growth factors, activated p42/p44 MAP kinases rapidly translocate to the nucleus, where they induce imm
Cytosolic phospholipase A2 activity during the ongoing cell cycle
β Scribed by Gerda S.A.T. van Rossum; Angela S. Vlug; Henk van den Bosch; Arie J. Verkleij; Johannes Boonstra
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 168 KB
- Volume
- 188
- Category
- Article
- ISSN
- 0021-9541
- DOI
- 10.1002/jcp.1123
No coin nor oath required. For personal study only.
β¦ Synopsis
Cytosolic phospholipase A(2) (cPLA(2)) is of special interest because it selectively releases arachidonic acid from membrane phospholipids. Arachidonic acid has been implicated to play an important role in various cellular responses. Recently arachidonic acid release and prostaglandin synthesis have been shown to be cell cycle dependent and therefore the activity of cPLA(2) during the ongoing cell cycle was investigated, using the mitotic shake off method for cell synchronisation. cPLA(2) activity was high in mitotic cells and decreased rapidly in the early G1 phase. A strong increase in activity was measured following the G1/S transition in both neuroblastoma and Chinese hamster ovary cells. The changes in activity were not due to a difference in cPLA(2) expression but due to phosphorylation of cPLA(2). Phosphorylation of cPLA(2) occurs through MAPK since the use of a specific MAPK kinase inhibitor and serum depletion of synchronised cells inhibited cPLA(2) activity.
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