Deletion of the kinase domain in death-associated protein kinase attenuates renal tubular cell apoptosis in chronic obstructive uropathy

Yukawa, Kazunori; Hoshino, Katsuaki; Kishino, Masanori; Mune, Masatoshi; Shirasawa, Nobuyuki; Kimura, Akihiko; Tsubota, Yuji; Owada-Makabe, Kyoko; Tanaka, Tetsuji; Ichinose, Masakazu; Maeda, Masanobu; Takeda, Kiyoshi; Akira, Shizuo

doi:10.3892/ijmm.13.4.515

Cited by 12 publications

(19 citation statements)

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“…DAPK is known to modulate apoptosis induced by several cytokines, Fas, ceramide, and cellular detachment from the extracellular matrix (4-7). Studies using knockout mice revealed crucial roles of DAPK in apoptotic cell death induced in vitro and in vivo (5,(8)(9)(10)(11). Thus, many studies, including ours, showed that DAPK was linked to apoptosis, by disclosing its pro-apoptotic role.…”

Section: Introductionmentioning

confidence: 65%

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Deletion of the kinase domain from death-associated protein kinase enhances spatial memory in mice

Yukawa

Tanaka²,

Bai³

et al. 2006

Int J Mol Med

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Abstract. Death-associated protein kinase (DAPK) is a Ca 2+ /calmodulin-dependent serine/threonine kinase that is thought to mediate apoptosis. DAPK is highly expressed in hippocampal neurons which are essential elements for memory formation. To examine if DAPK is implicated in spatial learning and memory, both wild-type and DAPK-mutant mice were subjected to Morris water maze tests. DAPKmutant mice were generated by deleting 74 amino acids from the catalytic kinase domain of DAPK, and were used to investigate roles of the DAPK kinase domain in regulating spatial memory. Both mutant and wild-type mice were able to learn the water maze tasks to locate a hidden escape platform. In the first probe test, mutant mice showed a more precise memory for platform position compared to wild-type mice. In the reversal training in which the platform was located opposite from the original position, DAPK-mutant mice exhibited superior spatial learning compared to wildtype mice. DAPK-mutant mice also showed a more precise memory than their wild-type littermates in the probe trial of reversal test. Thus, the present results revealed crucial implications of DAPK in regulating spatial memory in mice.

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Section: Introductionmentioning

confidence: 65%

“…Mice expressing a mutant form of DAPK lacking a portion of the kinase domain (amino acids 22-95), were generated by gene targeting in E14.1 embryonic stem (ES) cells (8)(9)(10)(11). Briefly, targeting vectors were designed to replace the exon encoding amino acids 22-95 of mature DAPK with a neomycin-resistance gene.…”

Section: Dapk-mutant Micementioning

confidence: 99%

Deletion of the kinase domain from death-associated protein kinase enhances spatial memory in mice

Yukawa

Tanaka²,

Bai³

et al. 2006

Int J Mol Med

Self Cite

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show abstract

“…DAPK-mutant mice expressing a mutant form of DAPK lacking the kinase domain (amino acids 22-95) were generated as described previously (16)(17)(18)(19). The mutant mice had a C57BL/6 genetic background, and wild-type littermates were used as controls.…”

Section: Methodsmentioning

confidence: 99%

“…The mutant mice had a C57BL/6 genetic background, and wild-type littermates were used as controls. The mice were maintained on a 12-h light/12-h dark cycle with free access to food and water in the animal facility of Wakayama Medical University and genotyped by polymerase chain reaction (PCR) analysis of tail DNA (16). All the animal experiments were approved by the Animal Ethics Review Committee of Wakayama Medical University.…”

Section: Methodsmentioning

confidence: 99%

“…Both the kinase domain and death domain are critical for its death-mediating functions (8,14,15). Using DAPK-mutant mice lacking the 74-amino acid catalytic kinase domain of DAPK, we have revealed that DAPK plays a pro-apoptotic role in renal tubular cell apoptosis in chronic obstructive uropathy and renal ischemiareperfusion injuries (16)(17)(18). Furthermore, DAPK is involved in modulating spatial memory in mice (19).…”

Section: Introductionmentioning

confidence: 99%

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Irinotecan-induced ovarian follicular apoptosis is attenuated by deleting the kinase domain of death-associated protein kinase

Tanaka²,

Yukawa³

et al. 2009

Int J Oncol

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Abstract. Although death-associated protein kinase (DAPK) is a Ca2+ /calmodulin-regulated serine/threonine kinase that plays important roles in various types of apoptotic cell death, there have been no reports of its tissue distributions and functions in female reproductive organs. By comparing C57BL/6 wild-type mice with DAPK-mutant mice lacking the 74-amino acid catalytic kinase domain of DAPK, the cellular distributions and biological functions of DAPK in murine ovaries were investigated. In situ hybridization analyses with sense and antisense riboprobes revealed that DAPK mRNA was selectively and highly expressed in granulosa cells in the ovaries of both types of mice. There were no significant differences in the body weights, ovarian weights and unstimulated ovarian follicular numbers between the wild-type and DAPK-mutant mice. Intraperitoneal injection of CPT-11, an anticancer topoisomerase I inhibitor that causes granulosa cell-specific apoptosis partly through Fas-Fas ligand (FasL) interactions in MCH mice, induced follicular apoptosis in both the wild-type and DAPK-mutant mice. However, the numbers of apoptotic follicles were significantly reduced in the DAPK-mutant mice. The Fas and FasL expression levels in the CPT-11-injected mice did not differ significantly between the wild-type and DAPK-mutant mice. These results indicate that DAPK positively regulates intracellular signaling pathways for CPT-11-induced granulosa cell apoptosis.

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Role of DAPK1 in neuronal cell death, survival and diseases in the nervous system

Alsaadi

2019

Intl J of Devlp Neuroscience

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DAPK (death‐associated protein kinase) is a calcium/calmodulin (Ca2+/CaM) regulated serine/threonine kinase. Structurally, it assumes a multi‐domain structure and participates in various apoptotic systems which imply that it may interact with a wide range of intracellular components to exert its action. DAPK plays vital roles in pro‐apoptotic, apoptotic and autophagic pathways. In addition, it plays important roles in many diseases such as cancer, Alzheimer's disease, cerebral ischemia and epilepsy. Although a novel protein, DAPK's various cellular signal transduction pathways proves that it can be a target for a potential future therapeutic effects. Specific role of DAPK in the development and maintenance of the nervous system needs to be further investigated as it is involved in neurodegeneration, traumatic brain injury and neuronal development or recovery from injury. This review summarizes DAPK signaling pathways in autophagy, apoptosis, and stresses the important role it might play in the nervous system.

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Deletion of the kinase domain in death-associated protein kinase attenuates renal tubular cell apoptosis in chronic obstructive uropathy

Cited by 12 publications

References 0 publications

Deletion of the kinase domain from death-associated protein kinase enhances spatial memory in mice

Deletion of the kinase domain from death-associated protein kinase enhances spatial memory in mice

Irinotecan-induced ovarian follicular apoptosis is attenuated by deleting the kinase domain of death-associated protein kinase

Role of DAPK1 in neuronal cell death, survival and diseases in the nervous system

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