AMP-activated Protein Kinase Contributes to UV- and H2O2-induced Apoptosis in Human Skin Keratinocytes

The question of how Bax is activated during apoptosis to perform its role in permeabilization of mitochondrial membranes is intriguing for investigators in the wide field of cell death research. In their paper published in the Biochemical Journal in 2006, Capano and Crompton presented their discovery that simulated ischaemia causes rapid activation of AMPK (AMP-activated protein kinase) which phosphorylates and activates p38 MAPK (mitogen-activated protein kinase) leading to Bax activation and translocation to mitochondria in isolated cardiac myocytes. This was the first report on the molecular mechanism of Bax activation and migration during ischaemia-induced apoptosis in cardiomyocytes.

Download Full-text

Involvement of AMP-activated protein kinase in mediating pyrrolo-1,5-benzoxazepine–induced apoptosis in neuroblastoma cells

Investigational New Drugs ◽

10.1007/s10637-016-0366-3 ◽

2016 ◽

Vol 34 (5) ◽

pp. 663-676 ◽

Cited By ~ 3

Author(s):

Jennifer C. Lennon ◽

Stefania Butini ◽

Giuseppe Campiani ◽

Anne O’Meara ◽

D. Clive Williams ◽

...

Keyword(s):

Protein Kinase ◽

Neuroblastoma Cells ◽

Induced Apoptosis ◽

Amp Activated Protein Kinase

Download Full-text

Niacin protects against UVB radiation-induced apoptosis in cultured human skin keratinocytes

International Journal of Molecular Medicine ◽

10.3892/ijmm.2012.886 ◽

2012 ◽

Vol 29 (4) ◽

pp. 593-600 ◽

Cited By ~ 11

Author(s):

FUQUAN LIN ◽

WEN XU ◽

CUIPING GUAN ◽

MIAONI ZHOU ◽

WEISONG HONG ◽

...

Keyword(s):

Human Skin ◽

Uvb Radiation ◽

Skin Keratinocytes ◽

Radiation Induced ◽

Induced Apoptosis

Download Full-text

5-Aminoimidazole-4-carboxamide riboside induces apoptosis in Jurkat cells, but the AMP-activated protein kinase is not involved

Biochemical Journal ◽

10.1042/bj20021053 ◽

2003 ◽

Vol 370 (3) ◽

pp. 1027-1032 ◽

Cited By ~ 52

Author(s):

José M. LÓPEZ ◽

Antonio F. SANTIDRIÁN ◽

Clara CAMPÀS ◽

Joan GIL

Keyword(s):

Protein Kinase ◽

Cell Types ◽

Jurkat Cells ◽

Nucleoside Transport ◽

Cytochrome C Release ◽

Nucleotide Biosynthesis ◽

Apoptotic Effect ◽

Nucleoside Transport Inhibitor ◽

Induced Apoptosis ◽

Amp Activated Protein Kinase

5-Aminoimidazole-4-carboxamide (AICA) riboside, a precursor of purine nucleotide biosynthesis, induces apoptosis in Jurkat cells. Incorporation of AICAriboside into the cells is necessary for this effect since addition of nitrobenzylthioinosine, a nucleoside-transport inhibitor, completely protects Jurkat cells from apoptosis. Adenosine, but not other nucleosides, also protects Jurkat cells from AICAriboside-induced apoptosis. The apoptotic effect is caspase-dependent since caspases 9 and 3 are activated and the caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD.fmk) blocks apoptosis. Furthermore, AICAriboside induces mitochondrial cytochrome c release. AICAriboside, when phosphorylated to AICAribotide (ZMP), is a specific activator of the AMP-activated protein kinase (AMPK) in certain cell types. However, AICAriboside does not activate AMPK in Jurkat cells. Moreover, 5-iodotubercidin, an inhibitor of AICAriboside phosphorylation, does not inhibit apoptosis in Jurkat cells. These results indicate that AICAriboside induces apoptosis independently of ZMP synthesis and AMPK activation in Jurkat cells.

Download Full-text