Archives

  • 2018-07
  • 2019-04
  • 2019-05
  • 2019-06
  • 2019-07
  • 2019-08
  • 2019-09
  • 2019-10
  • 2019-11
  • 2019-12
  • 2020-01
  • 2020-02
  • 2020-03
  • 2020-04
  • 2020-05
  • 2020-06
  • 2020-07
  • 2020-08
  • 2020-09
  • 2020-10
  • 2020-11
  • 2020-12
  • 2021-01
  • 2021-02
  • 2021-03
  • 2021-04
  • 2021-05
  • 2021-06
  • 2021-07
  • 2021-08
  • 2021-09
  • 2021-10
  • 2021-11
  • 2021-12
  • 2022-01
  • 2022-02
  • 2022-03
  • 2022-04
  • 2022-05
  • 2022-06
  • 2022-07
  • 2022-08
  • 2022-09
  • 2022-10
  • 2022-11
  • 2022-12
  • 2023-01
  • 2023-02
  • 2023-03
  • 2023-04
  • 2023-05
  • 2023-06
  • 2023-08
  • 2023-09
  • 2023-10
  • 2023-11
  • 2023-12
  • 2024-01
  • 2024-02
  • 2024-03
  • Kuo et al Have shown that DAPK

    2019-09-25

    Kuo et al. (2006) Have shown that DAPK1 function in inhibiting microtubule (MT) assembly is through the activation of microtubule affinity-regulating kinases (MARK)/PAR-1 family kinases MARK1/2, which destabilize MT by phosphorylating tau and related MAP2/4. This relation with DAPK1 has demonstrated the function of DAPK1 in the modulation of MT assembly and neuronal differentiation. It also provides a molecular link between DAPK1 and tau phosphorylation, an event associated with Alzheimer’s Disease (AD) pathology (Wu et al., 2011). DAPK1 was recently shown to have apoptosis-independent effects on the cytoskeletons (Kuo et al., 2006) and its association with stress fibers to induce inhibition of integrins by the cytoskeletal-binding domain of DAPK1 (Bialik et al., 2004). DAPK1 has also been linked to neurite outgrowth regulation in mice peptide yy kinase (Fujita et al., 2008). DAPK1 interacts with neogenin, which is a receptor for repulsive guidance molecule (RGM) that has diverse functions in the central nervous system development (Fujita et al., 2008). The same study showed the cytochrome c release from the mitochondria induced by neogenin is dependent on DAPK1. It has also demonstrated that DAPK1 is required for neogenin-induced cell death in the developing chick neural tube. Furthermore, neogenin induced cell death is abolished in the presence of RGM by blocking DAPK1. Moreover, following NGF-induced differentiation of rat PC12 cells, DAPK1 catalytic activity and protein levels increased drastically. These and other neuronal recovery results indicate that DAPK1 may have a previously unexplored role in neuronal development or regeneration following injury (Schumacher et al., 2002). It has been shown that DAPK1 is critical for the induction of neuronal cell apoptosis in response to various stimuli such as seizure, ischemia and ceramide in cell culture and animal models (Li et al., 2006; Liu et al., 2012; Mitoma et al., 1998). Two studies have observed the implication of DAPK1 in the molecular pathways of cell death during seizure-induced peptide yy kinase neuronal death model (Henshall et al., 2003). DAPK1 expression was induced in a rat seizure model in regions of the brain that were not undergoing apoptosis (Henshall et al., 2003). Augustinack et al. (2002) Showed DAPK1 protein expression was elevated in temporal lobe of epilepetic animals. It has been publicized from different distinct studies that the induction of seizures following kainic acid administration was accompanied by significant increase in DAPK1 in the CA3 region of the rat hippocampus and more interestingly the same trends was seen concerning p53, which suggest the interaction between the two proteins and their involvement in cell death in this models of neurodegeneration (Araki et al., 2004; Henshall et al., 2003). Middle cerebral artery occlusion (MCAO) is a model used to study neuronal death. It has been shown in line with previous studies that the induction of ischemia was associated with an elevation in DAPK1 expression (Schumacher et al., 2002; Shamloo et al., 2005). DAPK1-deficient mice showed a decrease in cell death following administration of glutamate or after knockout of DAPK1 that protects retinal ganglion cells from glutamate toxicity (Schori et al., 2002). It is well known that Aβ peptide is a neurotoxin and it is broadly used to mimic Alzherheimer’s disease (AD), condition to explore the mechanisms behind neuronal death in such diseases. In an in vitro study, Cheung et al. (2011) showed that the exposure of cultured neurons to Aβ results in cell death which is accompanied by activation of DAPK1. AD brain cells express an increasing number of apoptosis related proteins such as ZIP (Zipper interacting protein) kinase, Bim/BOD (Bcl-2 interacting mediator of cell death/Bcl-2 related ovarian death gene) and p21 AD frontal cortex. This increase has been suggested to be regulated by DAPK1 expression (Engidawork et al., 2001). Interestingly, aberrant methylation of DAPK1 has been implicated in tumourigenesis of neurofibromas or neurofibrosarcomas (Alonso et al., 2003; Gonzalez-Gomez et al., 2003a,b).