Transcript TNF-a
Presented By:
Deepanjan Paul
M.Sc. (F), MHG.
The term “PCD” was used in 1965 to describe developmental cell
deaths in insect systems by Lockshin & Williams.
Apoptosis (Apo: Away; Ptosis: Falling off) was coined by John
F. Kerr, Andrew H. Wyllie & A. R. Currie in 1972.
Cell shrinkage, karyorrhexis, blebbing, apoptotic bodies formation,
phagocytosis by macrophages.
Autophagy- Portions of cytoplasm or organelles are sequestered
into a double-membrane autophagosome and delivered to the
lysosomes and autolysosomes for breakdown and recycling.
www.nature.com/reviews/molcellbio
APOPTOSIS TIMELINE
Cell Death and Differentiation (2002) 9, 349-354
Pleiotropic cytokine.
Role in immune and inflammatory responses.
Induction of apoptosis.
TNF-a
Apoptosis
TNF R1 TNF R2 Mitochondrial
dysfunction
Extrinsic
pathway Intrinsic pathway
Mediator
of TNF-a associated cellular response.
Group of dimeric transcription factor.
NF-kB/Rel family (p50, p52, p65, Rel-B & c-Rel).
NF-kB pathway
Canonical
Noncanonical
p50 & p65
p52 & Rel-B
IkB
NF-kB
IKK Kinases
IkB
Proteosomal degradation
Activated NF-kB
Nucleus
Binds to kB sequence
Target genes
NF-kB
NF-kB
c-FLIP,Bcl-2,Bcl-XL
cIAP2,A1/Bfl-2.
p53,Fas,Fas ligand
death receptor 4,death
receptor 5.
Protection from apoptosis.
Promotes apoptosis
p53- DEPENDENT
g-radiation
Drugs
p53
PUMA activation
p53- INDEPENDENT
Serum starvation,kinase inhibitors,
glucocorticoids, ER stress,
ischemia/reperfusion.
PUMA activation
PUMA is essential for damage-induced & p53-dependent apoptosis.
Phosphorylation of CREB-binding protein (CBP) by IKKa suppresses p53mediated gene expression by switching the binding preference of CBP from p53
to NF-kB.
NF-kB can promote thymocyte and T-cell apoptosis, which is critical for shaping
the T-cell repertoire during thymocyte ontogeny.
Glucocorticoid dexamethasone induces PUMA dependent apoptosis in mouse
thymocytes.
PUMA can complement the function of Bim in controlling T-cell apoptosis in the
termination of immune response.
Mechanism & function of p53-independent PUMA induction
remain unclear.
PUMA is involved in ischemia/reperfusion-induced
intestinal injury, inducing inflammatory response ,
so, it may be regulated by inflammatory cytokines.
Cell culture and drug treatment.
Transfection and reporter assays.
Western blotting and antibodies.
RT-PCR and CHIP.
Analysis of apoptosis.
Animal experiments.
TUNEL and Immunostaining.
Bioinformatics and statistical analyses.
TNF-a (20ng/ml)
HCT116 colon cancer cells
PUMA mRNA and protein were induced my TNF-a within several hours.
Induction of PUMA mRNA and protein was unaffected in p53-KO or BS-KO.
Induction of PUMA by TNF-a was also independent of FOXO3a.
Bad, Bim and Noxa but not Bid were induced by TNF-a.
Potential binding sites of several TF (NF-kB, ATF,IRF & CREB families)
known to mediate TNF-a response were identified .
Only transfection of p65 subunit of NF-kB increased PUMA expression in
wild-type (WT), p53-KO, and BS-KO HCT116 cells.
p53-independent
induction of PUMA by p65
BAY 11-7082
(inhibitor of IKK Kinases)
IkBa superrepressor mutant
(Non-degradable)
Suppression of PUMA induction & P65 nuclear
translocation.
p65 si-RNA
PUMA induction
abrogated.
PUMA induction by TNF-a in mouse embryonic fibroblast (MEF) cells was also
found to be p65 dependent, but p53 independent.
p65
is necessary for PUMA induction by TNF-a
A luciferase reporter construct containing the putative kB site in the PUMA
promoter was constructed.
TNF-a treatment or co-transfection with p65 markedly activated the PUMA
reporter.
BAY 11-7082, IkBa superrepressor mutant & introducing mutations into the kB
site abolished the responsiveness of the reporter.
CHIP showed that recruitment of p65 to the PUMA promoter region containing
the kB site was enhanced following TNF-a treatment for 6 hrs.
p65
directly binds to the PUMA promoter to activate
PUMA transcription in response to TNF-a
Knockdown of Bcl-XL (but not cIAP1 or Mcl-1) by siRNA, led to a significant
increase in TNF-a-induced apoptosis but apoptosis induction was much reduced
in PUMA-KO HCT116 cells.
Caspase 3,8,9 activation, Bid cleavage & cytochrome-c release were also
suppressed in PUMA-KO cells.
Dominant-negative (DN) FADD mutant slightly lowered TNF-a-induced
apoptosis, but did not affect PUMA-dependent apoptosis following Bcl-XL
knockdown.
So, NF-kB-mediated PUMA induction is a novel mechanism
mediating TNF-a-induced apoptosis.
PUMA-dependent apoptosis induced by TNF-a in
colon cancer cells
TNF-a was injected intravenously at several doses (2, 4, and 10 mg) in WT and
PUMA-KO mice.
PUMA, Bcl-XL & Bim were induced by TNF-a in the small intestine.
TNF-a-induced apoptosis was blocked to a large extent (60–90%) in the crypts
and villus epithelium in PUMA-KO mice compared to the WT.
Caspase-3 activation was blocked in PUMA-KO mice.
PUMA is necessary for TNF-a-induced apoptosis in
the intestinal epithelium
PUMA (but not other BH3-only proteins) was increased in the liver of WT mice
following TNF-a treatment for 8 hr.
TNF-a-induced apoptosis was blocked by 50–70% in the PUMA-KO mice.
Caspase 3 activation induced by TNF-a at different doses was abrogated in the
hepatocytes of PUMA-KO mice.
So, PUMA mediates TNF-a-induced hepatocyte apoptosis.
PUMA mediates TNF-a-induced hepatocyte apoptosis
TUNEL staining revealed more than two fold reduction in apoptosis in PUMAKO thymocytes compared to WT ones.
Primary thymocytes from WT showed spontaneous apoptosis in culture but
TNF-a treatment had little effect on PUMA-KO primary thymocytes.
So, TNF-a-induced apoptosis in thymocytes is PUMA
dependent.
TNF-a-induced and PUMA-dependent apoptosis in
thymocytes
1st case of direct regulation of a BH-3 only Bcl-2 family by NF-kB in the TNF-a
response.
A completely p53 independent PUMA activation, inspite of the well-established
cross talk between p53 & NF-kB in regulating gene expression, is quite
unexpected.
Phosphorylation of CBP & hence its preferential binding to NF-kB might be
directing p65, instead of p53, to the PUMA promoter in response to TNF-a.
TNF-a-induced apoptosis often rely on using transcription or translation
inhibitors, which nonspecifically inhibit gene expression and often complicate
data interpretation.
p53 & p65 can cooperatively induce apoptosis in some circumstances, resulting
from coordinated induction of PUMA by p53 & p65.
PUMA functions as a novel link between the extrinsic & intrinsic apoptotic
pathways & hence necessary for TNF-a-induced apoptosis.
In vivo analysis of PUMA induction by TNF-a needs to be further
examined using more physiological systems including genetic
models.
PUMA was required for TNF-a-induced apoptosis in villus
epithelial cells but not in villus-inside cells.
Inhibition of NF-kB has been explored as an attractive approach
for anticancer therapies.
Again, NF-kB inhibition can compromise PUMA induction by
inflammatory cytokines, which may be involved in tumor
suppression and be beneficial for anticancer therapies.
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