Histone H1 dephosphorylation is not a general feature in early apoptosis.
Histone H1 is a family of nucleosomal proteins that exist in a number of subtypes. These subtypes can be modified after translation in various ways, above all by phosphorylation. Increasing levels of H1 phosphorylation has been correlated with cell cycle progression, while both phosphorylation and dephosphorylation of histone H1 have been linked to the apoptotic process. Such conflicting results may depend on which various apoptosis-inducing agents cause apoptosis via different apoptotic pathways and often interfere with cell proliferation. Therefore, we investigated the relation between apoptosis and H1 phosphorylation in Jurkat cells after apoptosis induction via both the extrinsic and intrinsic pathways and by taking cell cycle effects into account. After apoptosis induction by anti-Fas, no significant dephosphorylation, as measured by capillary electrophoresis, or cell cycle-specific effects were detected. In contrast, H1 subtypes were rapidly dephosphorylated when apoptosis was induced by camptothecin. We conclude that histone H1 dephosphorylation is not connected to apoptosis in general but may be coupled to apoptosis by the intrinsic pathway or to concomitant growth inhibitory signaling.
Division of Cell Biology, Department of Clinical and Experimental Medicine, Linkoping University, SE-58185 Linkoping, Sweden.
Anna
A
Gréen
Bettina
B
Sarg
Elisavet
E
Koutzamani
Ulrika
U
Genheden
Herbert H
HH
Lindner
Ingemar
I
Rundquist
D017304:Annexin A5 / Q000378:metabolism; D017209:Apoptosis / Q000187:drug effects / Q000502:physiology*; D002166:Camptothecin / Q000494:pharmacology; D020169:Caspases / Q000378:metabolism; D002453:Cell Cycle; D006657:Histones / Q000378:metabolism*; D006801:Humans; D019169:Jurkat Cells; D007700:Kinetics; D010766:Phosphorylation
D017304:Annexin A5; D006657:Histones; D020169:Caspases; D002166:Camptothecin