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Protein kinases are enzymes that play a pivotal role in regulating cellular activities by adding phosphate groups to target proteins, a process called phosphorylation. This modification can activate or deactivate proteins, allowing cells to respond to a wide range of signals. Kinases molecules are involved in critical pathways that influence cell growth, division, apoptosis, differentiation, and metabolism, making them essential for maintaining cellular health and function.
AnyGenes qPCR arrays provide advanced tools for studying protein kinase-related pathways, allowing researchers to investigate gene expression profiles of these crucial regulators. These arrays help uncover the molecular mechanisms by which kinases influence health and disease, offering insights into new therapeutic targets and precision medicine approaches.
Protein kinases mediated signaling pathways in heart failure and hypertrophy. (A) The role of protein kinases in physiological hypertrophy. (B) The role of protein kinases in heart failure and pathological hypertrophy. 4EBP1: eiF4E-binding protein 1; AKT: Protein kinases B; AMPK: Adenosine monophosphate-activated protein kinase; C/EBPβ: CCAAT/enhancer binding protein-β; CaMK: Calcium/calmodulin-dependent protein kinases; CITED4: CBP/p300-interacting transactivator 4; eIF2Bε: eukaryotic translation initiation factor; eIF4E: eukaryotic translation initiation factor 4E; ERK: Extracellular signal-regulated kinase; FOXO3: Forkhead box protein O3; GSK: Glycogen synthase kinase; HDAC4: Histone deacetylase 4; IGF1: Insulin-like growth factor 1; MEK: MAPK/ERK kinase; mTOR: Mechanistic target of rapamycin; PI3K: Phosphoinositide 3-kinase; PINK: PTEN-induced putative kinase; PKA: Protein kinase A; PKC: Protein kinase C; PKG: Protein kinase G; PLN: Phospholamban; RGS: Regulator of G-protein signaling; RYR2: Ryanodine receptor; S6K1: Ribosomal protein S6 kinaseβ1; UBE2T: Ubiquitin-conjugating enzyme E2T.
Kinases molecules are divided into major categories based on the specific amino acids they target:
Recent developments have highlighted the importance of targeting kinases molecules in cancer therapy. Numerous kinase inhibitors have been approved by the FDA for treating various cancers. For instance, inhibitors like tepotinib (MET kinase), tivozanib (VEGFR), and mobocertinib (EGFR) represent significant advancements in targeted cancer therapies. Additionally, novel strategies such as PROteolysis TArgeting Chimeras (PROTACs) are being explored to induce degradation of specific kinases rather than merely inhibiting their activity.
Dysregulation of protein kinase activity is associated with numerous diseases, including cancer, diabetes, cardiovascular disease, and neurodegenerative disorders. Mutations or overexpression of certain kinases can lead to uncontrolled cell growth, immune dysfunction, or metabolic imbalances. Research into kinase molecules has led to targeted therapies, including kinase inhibitors, which are used to treat cancers and inflammatory diseases. For example, inhibitors targeting casein kinase 1 (CK1) have shown promise in treating hematological cancers by disrupting oncogenic signaling pathways.
The FDA has approved numerous small-molecule kinase inhibitors (SMKIs), which primarily interact with the ATP-binding site of kinases. Despite significant progress, several challenges remain in developing effective kinase-targeted therapies:
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