What are protein kinases ?

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.

Discover our advanced qPCR arrays for Protein Kinases research.

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.

Types of protein kinases

Kinases molecules are divided into major categories based on the specific amino acids they target:

Serine/Threonine Kinases: These kinases phosphorylate the amino acids serine or threonine on target proteins, affecting pathways involved in growth and stress response.
Tyrosine Kinases: Tyrosine kinases target the amino acid tyrosine and are crucial in pathways controlling cell division and immune responses.
Dual-Specificity Kinases: These kinases can phosphorylate serine, threonine, and tyrosine residues, playing versatile roles in cellular signaling.

Targeting kinases molecules in cancer

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.

Protein kinases and diseases

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.

Challenges in kinase drug development

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:

Selectivity: Achieving high selectivity for specific kinases is critical to minimize side effects. Many current SMKIs target structurally similar kinases, leading to unwanted interactions.
Toxicity: The lack of selectivity often results in toxicities that limit the therapeutic window of these drugs.
Resistance Mechanisms: Cancer cells can develop resistance to kinase inhibitors through various mechanisms, necessitating ongoing research into combination therapies and novel inhibitors.

Analyze your pathway data with AnyGenes® software

Scientific data is only as powerful as the analysis behind it.

AnyGenes® provides a dedicated data analysis tool specifically developed for SignArrays® pathway panels.

What does it allow you to do?

Automated ΔCq calculation
Normalization with selected housekeeping genes
Comparison of up to 10 experimental conditions
Generation of descriptive statistics
Publication-ready graphs
Exportable tables for manuscripts and presentations

Developed on Excel (compatible with 2007+), the software is user-friendly and requires no advanced bioinformatics skills.

Customize your own signaling pathways (SignArrays®) with the factors of your choice!
Simply download and complete our Personalized SignArrays® information file and send it at [email protected] to initiate your project.

Protein kinases biomarker list

You can check the biomarker list included in this pathway, see below:

Species : Homo sapiens (human)

Human signaling pathways

Signaling Pathways	Product ref	Informations
Protein Kinases	PK1H1	Download biomarker list

Species : Mus musculus (mouse)

Mouse signaling pathways

Signaling Pathways	Product ref	Informations
Protein Kinases	*******	Biomarker list in progress.

Species : Rattus norvegicus (rat)

Rat signaling pathways

Signaling Pathways	Product ref	Informations
Protein Kinases	*******	Biomarker list in progress.

Species : Sus Scrofa (Pig)

Pig Protein Kinases

Signaling Pathways	Product ref	Informations
Protein Kinases	*******	Biomarker list in progress.

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Bibliography

1. Plaza-Menacho I. Redox takes control. Elife. (2024)20;13:e99765.

2. ilnitsky S, et al. An Update on Protein Kinases as Therapeutic Targets—Part I: Protein Kinase C Activation and Its Role in Cancer and Cardiovascular Diseases. Int J Mol Sci. (2023)18;24(24):17600.

3. Luukkonen S, et aal. Large-Scale Modeling of Sparse Protein Kinase Activity Data. J Chem Inf Model. (2023)26;63(12):3688-3696.

4. Chen J, et al. Protein kinases in cardiovascular diseases. Chin Med J (Engl). (2022)2;135(5):557–570.

5. Yan Z, et al. Recent Advances in Protein Kinase Activity Analysis Based on Nanomaterials. Int J Mol Sci. (2019)21;20(6):1440.

6. Cipak L. Protein Kinases: Function, Substrates, and Implication in Diseases. Int J Mol Sci. (2022)24;23(7):3560 (2020)28;21(7):2346.

7. Riegel K, et al. Recent advances in targeting protein kinases and pseudokinases in cancer biology. Front Cell Dev Biol. (2022)22:10:942500.

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