mProX™ Human MAPK12 Stable Cell Line
- Product Category:
- Membrane Protein Stable Cell Lines
- Subcategory:
- Kinase Cell Lines
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Published Data
Fig.1 MAPK12 knockdown can stop osteosarcoma cells from proliferating.
In order to examine the function of MAPK12 in the advancement of osteosarcoma, siRNAs were used to reduce the expression of MAPK12 in two different osteosarcoma cell lines. Osteosarcoma cell proliferation was significantly reduced by MAPK12 knockdown, as indicated by CCK-8.
Ref: Cui, Chengliang, and Xiaoyu Shi. "miR-187 inhibits tumor growth and invasion by directly targeting MAPK12 in osteosarcoma." Experimental and Therapeutic Medicine 14.2 (2017): 1045-1050.
Pubmed: 28810556
DOI: 10.3892/etm.2017.4624
Research Highlights
Natarajan, Pradeep. et al. "3-deazaadenosine: A promising novel p38γ antagonist with potential as a breast cancer therapeutic agent." Cancer treatment and research communications, 2023.
The human p38γ protein kinase, also known as MAPK12, plays a vital role in transmitting membrane signals to the nucleus within the MAPK cascade pathway, a pathway associated with various malignancies including breast and colorectal cancer, as well as atherosclerotic lesions. Its multifunctional nature contributes significantly to the advancement of breast carcinoma. Exploring p38γ as a target for potent antagonists in breast cancer therapy represents a novel and appealing approach. Using computational drug design techniques, a collection of 1909 geometrically analogous compounds to known inhibitors, such as BIRB796, SB202190, ANP, CHEBI: 620708, and CHEBI: 524699, was created via high-throughput virtual screening. Ensuring chemical accuracy through LigPrep for the independent library and Prep Wizard for p38γ via Maestro v.11.5, 18 potential lead compounds were identified within p38γ binding sites. Subsequent evaluation of their ADMET properties led to the selection of Lead '1', which exhibited robust and consistent bonding interactions with p38γ during 100 ns molecular dynamics simulations. Furthermore, it established water bridges, strengthening its association with the protein. Notably, Lead '1' (3-deazaadenosine) displayed favorable root-mean-square deviation (RMSD) and root-mean-square fluctuation (RMSF) within the acceptable range of pharmacological characteristics, suggesting the potential of 3-deazaadenosine and its mimetics as a promising avenue for developing a novel class of breast cancer antagonists.
Natarajan, Pradeep. et al. "3-deazaadenosine: A promising novel p38γ antagonist with potential as a breast cancer therapeutic agent." Cancer treatment and research communications, 2023.
Pubmed:
37481995
DOI:
10.1016/j.ctarc.2023.100744
Escós, Alejandra, et al. "p38γ and p38δ modulate innate immune response by regulating MEF2D activation." Elife 12 (2023): e86200.
They studied p38γ and p38δ's roles in inflammation by using a modified mouse model (p38γ/δKIKO). Unlike previous models which had skewed TPL2 levels, this new model had standard TPL2 readings. This mouse provided clearer insights into p38γ and p38δ's specific functions. Notably, the p38γ/δKIKO mice had a subdued inflammatory reaction and were more resistant to certain septic shocks and infections than typical mice. Gene tests revealed that p38γ/p38δ influenced many genes related to the body's initial defense mechanisms. Further analysis highlighted that the protein MEF2D's activity was managed by p38γ/p38δ-driven modifications, thereby controlling innate immunity responses.
Escós, Alejandra, et al. "p38γ and p38δ modulate innate immune response by regulating MEF2D activation." Elife 12 (2023): e86200.
Pubmed:
37458356
DOI:
10.7554/eLife.86200