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Table 5 A list of differentially expressed proteins in the cerebellum with fundamental roles in the regulation of cell death

From: Proteome profiling of different rat brain regions reveals the modulatory effect of prolonged maternal separation on proteins involved in cell death-related processes

Protein ID Gene name Protein name Y S/C M S/C F S/C C M/F S M/F Protein function
Pdk2 [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial ↓ (0.41) p53 activation decreases Pdk2 transcription [92]
P97570 Pla2g6 85/88 kDa calcium independent phospholipase A2 S N M M tBID and Bax augments Pla2g6 (iPLA2) activity via ROS production leading to changes in the MOM [93]
Overexpression of iPLA2 increased the rate of apoptosis, iPLA2 is cleaved by caspase-3 [94]
β-cell apoptosis is attributable to the modulation of 5′SS selection in Bcl-X pre-mRNA by bioactive lipids modulated by iPLA2 [95]
Q9JKL8 Adnp Activity-dependent neuroprotector homeobox protein C M Down-regulation of Adnp up-regulates p53 [144]
NAP sequence of Adnp reduces activity of caspase-3 [145]
Dysregulation of Adnp expression increases Bcl-2 expression in hippocampus [146]
Apc Adenomatosis polyposis coli C N M N APC can regulate apoptosis by governing the level of caspase-3 [134]
P23928 Cryab Alpha-crystallin B chain S ↓ (0.50) Cryab prevents apoptosis; it binds to caspase-3 [134], Bax and Bcl-XS [135] and p53 [136]
Cryab gene is a targer of p53 and p53-dependent apoptosis is affected by Cryab expression [136]
Bcl2l1 Bcl-2-like protein 1 N M M Bcl2l1 (Bcl-X) gene generates two protein products by alternative pre-mRNA splicing: Bcl-XL is anti-apoptotic, while Bcl-XS is pro-apoptotic; deletion of Bcl-X in mice results in neuronal death in the brain during late embryonic development; Bcl-XL overexpression attenuates brain injury in neonatal rodents [77]
Q91XJ1 Becn1 Beclin-1 N N M M Beclin-1-induced autophagy is inversely correlated with apoptosis [13]
Rcan2 Calcipressin-2 S N M M Calcineurin regulation [138]
Capn1 Calpain-1 catalytic subunit N S N N M Calpain is a Ca2+-dependent protease, which cleaves Bid, Bcl-2, Bcl-XL [17] and Bax [80]
It cleaves caspase-3, -8 and -12, p53 and NMDA receptors [81]
Capn5 Calpain-5 S N N M Ca2+-dependent protease
P55213 Casp3 Caspase-3 N S N F Cleavage and activation of caspase-3 initiates apoptosis; essential for neuronal cell death [100]
Caspase-3 expression is regulated with age [21]
a regulatory calpain/caspase-3 cross-talk [101]
Q1HL14 Cers1 Ceramide synthase 1 S N S N F Inhibition of de novo ceramide synthesis inhibited caspase 3/7 activation and apoptosis [102]
Overexpression of CerS1 and increased level of C18 ceramide resulted in activation of ER stress and inhibition of cell viability, independent of Bax [103]
Creb1 Cyclic AMP-responsive element-binding protein 1 C C N Enhanced Creb activity leads to increased Bcl-2 promoter activity and cell survival [147]
Ephb2 Eph receptor B2 - S F Ephb2 can prevent against Fas-triggered apotosis by inhibition of caspase-8 and caspase-3 [140]
Q8R2E7 Fadd FAS-associated death domain protein C F Pro-apoptotic adapter protein involved in extrinsic pathway of apoptosis [100]
Overexpression of FADD promotes apoptosis [103]
Grid2 Glutamate ionotropic receptor, delta-2 ↑ (3.12) Gain-to-function mutation of Grid2 induces neuronal death [105]; this mutation is associated with increased expression of Bax, Bcl-XS, caspase-3 and -8 [106]
TNF-α has a role in regulation of Grid2 gene expression, which can be a suppressor in TNF-induced neurodegeneration [107]
Grik2 Glutamate ionotropic receptor, kainate 2 S F Grik2 (GluR6) promotes Bax translocation and increase in caspase-3 activation [108]
Grin1 Glutamate ionotropic receptor, NMDA 1 C F Up-regulation of Grin1 (NR1 subunit) is associated with increased expression of Bax and decreased expression of Bcl-XL [148]
Grin2a Glutamate ionotropic receptor, NMDA 2A S S N N M NMDARs containing Grin2a (NR2A subunit) promotes neuronal survival [149]; down-regulation of Creb was exaggerated in neurons over-expressing Grin2A [83]
Grin2b Glutamate ionotropic receptor, NMDA 2B C S N N M NMDARs containing Gin2b (NR2B subunit) promotes neuronal death [149]; down-regulation of Creb was exaggerated in neurons over-expressing Grin2b [83]
Grin2c Glutamate ionotropic receptor, NMDA 2C S S S N NR2C expression supports neuronal survival [150]
O35821 Mybbp1a Myb-binding protein 1A C M Mybbp1a can increase Bax expression via p53 acetylation [151]
Mybbp1a down-regulation induces apoptosis via caspase-3 activation [152]
P06907 Mpz Myelin protein P0 C ↓ (0.34) ↑ (4.08) ↑ (7.98) Mpz knockdown induced apoptosis [114]
P2rx7 P2X purinoceptor 7 S P2rx7s mediate caspase-8 and caspase-3 dependent apoptosis [115]
Its activation is associated with Ca2 + responses and TNF-α production [116,117,118]
Mpv17 Protein Mpv17 N ↑ (3.97) F F The increase of Mpv17 expression can be accompanied by the enhanced expression of p53, Bax, cyt c and active caspase-3 and decreased expression of Bcl-2 in the pathological proces [119]
P70600 Ptk2b Protein-tyrosine kinase2-beta C C C ↑ (5.55) N Overexpression of Ptk2b can induce apoptosis [143]
D4ADQ1 Rrm2b Ribonucleotide reductase M2 B (TP53 inducible) N N C F N Loss of Rrm2b can increase apoptosis [123]
Rrm2b expression is induced by stress [124]
Rrm2b cleavage is mediated by caspase-8 and -3) [125]
Rbm10 RNA-binding protein 10 S F Rbm10 knock-down can decrease caspase activation [126]
Rbm10 regulates alternative splicing of Fas and Bcl-X genes [127]
Rbm10 expression is associated with increased apoptosis [128]
D4A280 Pak7 Serine/threonine-protein kinase PAK 5 S C F M Pak7 expression can prevent apoptosis by phosphorylating of Bad on Ser112 and inhibition of caspase-3 and PARP cleavage [153]
Tnfaip8 TNF-α induced protein 8 C C C N Tnfaip8 can suppress TNF-mediated apoptosis by inhibiting TNF-induced caspase-8 activity [69]
  1. C protein detected only in samples of the cerebellum from control rats, S protein detected only in samples of the cerebellum from maternally separated rats, M protein detected only in samples of the cerebellum from adult male rats, F protein detected only in samples of the cerebellum from adult female rats, N protein not detected in the samples, –, unchanged protein expression between the samples; ↓, protein down-regulated in samples of the cerebellum from maternally separated rats; ↑, protein up-regulated in samples of the cerebellum from maternally separated rats