DAPK Reverse PCR Primer (200bp position)
- Known as:
- DAPK Reverse PCR test kit Primer (200bp position)
- Catalog number:
- MP1134
- Product Quantity:
- ea
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- DAPK Reverse PCR Primer (200bp position)
Related genes to: DAPK Reverse PCR Primer (200bp position)
- Gene:
- DAPK1 NIH gene
- Name:
- death associated protein kinase 1
- Previous symbol:
- -
- Synonyms:
- DAPK, ROCO3
- Chromosome:
- 9q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 1995-04-27
- Date modifiied:
- 2017-04-06
Related products to: DAPK Reverse PCR Primer (200bp position)
Related articles to: DAPK Reverse PCR Primer (200bp position)
- Metastasis and associated therapy resistance remain the principal drivers of cancer related death, and there is a pressing need for a deeper mechanistic understanding and anti-metastatic therapies. For patients that suffer from hepatocellular carcinomas (HCCs), which are the most common primary liver cancers, frequent systemic metastasis results in bleak 5-year survival prognoses of only 4%. To metastasize, carcinoma cells must acquire an invasive phenotype, which typically requires switching from an epithelial-like apical-basal polarity to the front-rear polarity of mesenchymal-like cells. Signaling cues that originate in the tumor microenvironment can activate cellular morphogenic programs that drive polarity switching, like the epithelial-mesenchymal transition (EMT). Protein kinases control most cell signaling pathways and are highly actionable drug targets; however, systematic studies determining the kinases that underly the epithelial-mesenchymal polarity switch (EMPS) are lacking. We developed an assay platform that integrates mass spectrometry (MS)-based kinome profiling, broadly capturing kinase network activity, with chemical genetic screening using selective kinase inhibitors and quantitative phase imaging (QPI), serving as the phenotypic readout. Applying this approach that we dubbed morphokin-MS, to epithelial-like HCC cell lines that we induced to undergo EMPS identified a conserved network of 12 kinases that contributed to HCC cell polarity switching and directed cell migration; MS-based kinome profiling of 17 HCC patient tumors showed that these kinase are frequently upregulated in human tumors. morphokin-MS also revealed that death-associated protein kinase 3 (DAPK3) is one of the principal drivers of the EMPS and directed HCC cell migration. Thus, our mechanistic studies revealed that DAPK3 forms a complex with DAPK1 and filamin-A inter-acting protein 1-like (FILIP1L), which act as scaffold proteins that recruit DAPK3 to the centrosome. Pharmaco-logical and genetic inhibition of the DAPK1-DAPK3-FILIP1L complex blocked centrosome repositioning and microtubule polarization toward the leading edge of mesenchymal-like HCC cells, directed cell migration, and invasion. Our morphokin-MS method and comprehensive kinome profiling data will serve as a valuable resource for the cancer research community; our discovery of an inducible mesenchymal-like DAPK1-DAPK3-FILIP1L polarity complex that controls centrosome positioning in motile HCC cells may lead to the development of novel therapeutics for combatting cancer metastasis. - Source: PubMed
Publication date: 2026/09/18
Rantso Thankhoe AWoods KathrynJensen PaigeWalker Katie AChan Alexandria MMaguire Kathleen MZitnay Rebecca GLovely Lotfa HYang JingshuTakyi AugustineStewart PaulEvason KimberleyJudson-Torres Robert LGolkowski Martin - We previously demonstrated that apolipoprotein E (apoE4) accelerates neurodegeneration in a transgenic mouse model, but the mechanism is still unclear. A previous study reported that death-associated protein kinase 1 (DAPK1) interacts with the NR2B subunit of the N-methyl-D-aspartate (NMDA) receptor, this DAPK1-NR2B interaction increases calcium intake in cells, leading to cell damage. As apoE4 is the strongest genetic risk factor for sporadic Alzheimer's disease (sAD) and calcium dyshomeostasis is a key driver of sAD-related neurotoxicity, the unclear mechanism linking apoE4 to calcium imbalance remains a critical gap in developing targeted therapies for sAD. Addressing this gap is urgent to advance our understanding of sAD pathogenesis and identify new therapeutic targets. Our study aimed to determine whether the neurotoxic effects of apoE4 are mediated by the interaction between DAPK-1 and the NMDA receptor NR2B subunit. - Source: PubMed
Publication date: 2026/09/03
Liu DeshanZhuo YifenChen SisiWang YinzhouChen XiaochunYao Yusheng - Death-associated protein kinase 1 (DAPK1) is a key regulator of apoptosis and immune responses; however, its prognostic significance in oral cancer remains insufficiently characterized. This study investigated the prognostic relevance of DAPK1 in oral squamous cell carcinoma (OSCC) and examined its associations with immune infiltration and apoptosis-related signaling pathways. - Source: PubMed
Publication date: 2026/08/28
Lai Hsiao-ChiChang Keng-MingLee Ching-Chih - has shown antitumor activity across multiple malignancies, yet its molecular targets and mechanisms of action in diffuse large B-cell lymphoma (DLBCL) remain incompletely defined. We integrated genetic causality, multi-omics data, and functional validation to identify berberine-related molecular pathways relevant to DLBCL. - Source: PubMed
Publication date: 2026/08/28
Tan JiewenXu YunmanHe YuepingChen ChangLuo JingwenZhang ChangxiuZhong JinmanXiong Dan - The treatment of osteosarcoma still relies on surgery combined with chemotherapy. However, the development of chemotherapy resistance severely weakens treatment efficacy and leads to poor prognosis. Endoplasmic reticulum‑selective autophagy (ER-phagy) can maintain intracellular homeostasis by clearing ER fragments, and has been reported to contribute to chemotherapy resistance. However, the role of ER-phagy in chemotherapy resistance in osteosarcoma remains unclear. This study aims to investigate the potential role and molecular mechanisms of death-associated protein kinase 1 (DAPK1) in vincristine (VCR) resistance in osteosarcoma. - Source: PubMed
Publication date: 2026/09/06
Yao PeifengCui XinyaoZheng ZiangWang YifanLin JiabinLiang Haidong