Cited by 1,369Protein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancerCancer Mechanisms and Therapy

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The specificities of protein kinase inhibitors: an update

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BAIN, Jenny, McLAUCHLAN, Hilary, ELLIOTT, Matthew, COHEN, Philip·2003·Biochemical Journal

DOI 10.1042/bj20021535PMC PMC1223271

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Abstract

We have previously examined the specificities of 28 commercially available compounds, reported to be relatively selective inhibitors of particular serine/threonine-specific protein kinases [Davies, Reddy, Caivano and Cohen (2000) Biochem. J. 351, 95—105]. In the present study, we have extended this analysis to a further 14 compounds. Of these, indirubin-3′-monoxime, SP 600125, KT 5823 and ML-9 were found to inhibit a number of protein kinases and conclusions drawn from their use in cell-based assays are likely to be erroneous. Kenpaullone, Alsterpaullone, Purvalanol, Roscovitine, pyrazolopyrimidine 1 (PP1), PP2 and ML-7 were more specific, but still inhibited two or more protein kinases with similar potency. Our results suggest that the combined use of Roscovitine and Kenpaullone may be useful for identifying substrates and physiological roles of cyclin-dependent protein kinases, whereas the combined use of Kenpaullone and LiCl may be useful for identifying substrates and physiological roles of glycogen synthase kinase 3. The combined use of SU 6656 and either PP1 or PP2 may be useful for identifying substrates of Src family members. Epigallocatechin 3-gallate, one of the main polyphenolic constituents of tea, inhibited two of the 28 protein kinases in the panel, dual-specificity, tyrosine-phosphorylated and regulated kinase 1A (DYRK1A; IC50 = 0.33μM) and p38-regulated/activated kinase (PRAK; IC50 = 1.0μM).

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Method
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BackgroundInfluential
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Background
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BackgroundMethod
Prostanoid F receptors elicit an inotropic effect in rat left ventricle by enhancing myosin light chain phosphorylation
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BackgroundInfluential
The Substrate-Activity-Screening methodology applied to receptor tyrosine kinases: A proof-of-concept study
Chapelat, J., Berst, F., Marzinzik, A. L., Möbitz, H., Drueckes, P., Trappe, J., Fabbro, D., & Seebàch, D. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.08.038 · Cited by 15
Cyclic GMP-dependent protein kinase-I localized in nociceptors modulates nociceptive cortical neuronal activity and pain hypersensitivity
Gangadharan, V., Wang, X., & Luo, C. (2017) · Molecular Pain · doi:10.1177/1744806917701743 · Cited by 15
“The most plausible explanation for these contradictory findings is the serious lack of specificity of commonly used pharmacological modulators of the cGMP-PKG pathway; for example, KT5823, which was used a ‘‘specific’’ PKG-I inhibitor in several studies, has been shown to block several other kinases and only unreliabl…”
High-content screening assay-based discovery of paullones as novel podocyte-protective agents
Lee, H. W., Arif, E., Altintas, M. M., Quick, K. L., Maheshwari, S., Plezia, A., Mahmood, A., Reiser, J., Nihalani, D., & Gupta, V. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00338.2017 · Cited by 15
“GSK-3 is a direct target of kenpaullone (4), suggesting GSK-3 inhibition as the primary mechanism behind the efficacy of these paullone derivatives in podocytes.”
Background
Sulbactam Protects Hippocampal Neurons Against Oxygen-Glucose Deprivation by Up-Regulating Astrocytic GLT-1 via p38 MAPK Signal Pathway
Qi, J., Xian, X., Li, L., Zhang, M., Hu, Y., Zhang, J., & Li, W. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00281 · Cited by 15
“SB203580, a highly specific, cell-permeable inhibitor of p38 MAPK, could bind competitively to the ATP binding site of p38 MAPK to inhibit the activation of downstream pathway of p38 MAPK (Lee et al., 1994; Cuenda et al., 1995; Bain et al., 2003).”
Background
Anti-Inflammatory Effects of Licania macrocarpa Cuatrec Methanol Extract Target Src- and TAK1-Mediated Pathways
Shin, K. K., Park, J. G., Hong, Y. H., Aziz, N., Park, S. H., Kim, S.-G., Kim, E., & Cho, J. Y. (2019) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2019/4873870 · Cited by 15
JUN Amino-Terminal Kinase 1 Signaling in the Proximal Tubule Causes Cell Death and Acute Renal Failure in Rat and Mouse Models of Renal Ischemia/Reperfusion Injury
Grynberg, K., Ozols, E., Mulley, W. R., Davis, R. J., Flavell, R. A., Nikolic‐Paterson, D. J., & Ma, F. Y. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.02.004 · Cited by 15
Src-Family Tyrosine Kinases in Oogenesis, Oocyte Maturation and Fertilization: An Evolutionary Perspective
Kinsey, W. H. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-0817-2_3 · Cited by 15
Counteraction of axonal growth inhibitory properties of Semaphorin 3A and myelin‐associated proteins by a synthetic neurotrophic compound
Hanbali, M., Bernard, F., Berton, C., Gatineau, G., Perraut, M., Aunis, D., Luu, B., & Bagnard, D. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02601.x · Cited by 15
“For instance, EGCG also inhibits protein kinases such as PRAK, DYRK and ROCK-II (Bain et al. 2003).”
Background
Early myeloid cells expressing c-KIT isoforms differ in signal transduction, survival and chemotactic responses to Stem Cell Factor
Young, S. M., Cambareri, A. C., Odell, A. F., Geary, S. M., & Ashman, L. K. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.08.004 · Cited by 15
Proapoptotic function of protein kinase CK2α" is mediated by a JNK signaling cascade
Hilgard, P. A., Czaja, M. J., Gerken, G., & Stockert, R. J. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00507.2003 · Cited by 15
Src family tyrosine kinases mediate contraction of rat isolated tail arteries in response to a hyposmotic stimulus
Wijetunge, S., & Hughes, A. D. (2007) · Journal of Hypertension · doi:10.1097/hjh.0b013e328255e8f0 · Cited by 15
Requirement for active glycogen synthase kinase-3β in TGF-β 1 upregulation of connective tissue growth factor (CCN2/CTGF) levels in human gingival fibroblasts
Bahammam, M. A., Black, S. A., Sume, S. S., Assaggaf, M., Faibish, M., & Trackman, P. C. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00032.2013 · Cited by 16
Bombesin and angiotensin II rapidly stimulate Src phosphorylation at Tyr-418 in fibroblasts and intestinal epithelial cells through a PP2-insensitive pathway
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Regeneration of Pancreatic β-Cells for Diabetes Therapeutics by Natural DYRK1A Inhibitors
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“In addition, it was reported that EGCG could inhibit DYRK1A with an IC50 of 0.33 mM, while it exhibited low affinity for other kinases in the CMGC family, such as MAPK and GSK3β [84], indicating its distinct potential against diabetes.”
BackgroundInfluential
Different responses in transformation of MDCK cells in 2D and 3D culture by v-Src as revealed by microarray techniques, RT-PCR and functional assays
Töyli, M., Rosberg-Kulha, L., Capra, J., Vuoristo, J. T., & Eskelinen, S. M. (2010) · Laboratory Investigation · doi:10.1038/labinvest.2010.63 · Cited by 14
“This is in line with the results obtained by de Diesbach et al.23 on the same ts-Src MDCK cell line transfected with exactly the same clone of v-Src.”
BackgroundInfluential
Crystallography for protein kinase drug design: PKA and SRC case studies
Breitenlechner, C. B., Bossemeyer, D., & Engh, R. A. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.09.014 · Cited by 14
Pyk2 regulates H + -ATPase-mediated proton secretion in the outer medullary collecting duct via an ERK1/2 signaling pathway
Fisher, K. D., Codina, J., Petrović, S., & DuBose, T. D. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00008.2012 · Cited by 14
Regulation of proline-directed kinases and the trans-histone code H3K9me3/H4K20me3 during human myogenesis
Bhanu, N. V., Sidoli, S., Yuan, Z., Molden, R. C., & Garcia, B. A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004977 · Cited by 13
“In pancreatic cells, GW8510 may have JNK- and p38-dependent stimulatory effects on transcriptional activity (53); at the 1– 40 M range, roscovitine inhibits a wide variety of kinases including ERK1 and ERK2 (42, 54, 55).”
Background
Catechins as a Potential Dietary Supplementation in Prevention of Comorbidities Linked with Down Syndrome
Noll, C., Kandiah, J., Moroy, G., Gu, Y., Dairou, J., & Janel, N. (2022) · Nutrients · doi:10.3390/nu14102039 · Cited by 14
“Among them, EGCG [80] has been used many times in preclinical studies, considering its capacity to inhibit DYRK1A activity with IC50 of 0.”
Background
A critical update on the strategies towards small molecule inhibitors targeting Serine/arginine-rich (SR) proteins and Serine/arginine-rich proteins related kinases in alternative splicing
Tang, J., Xie, Y., Huang, J., Zhang, L., Jiang, W., Li, Z., & Bian, J. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116921 · Cited by 15
Calcium transients regulate titin organization during myofibrillogenesis
Harris, B. N., Li, H., Terry, M., & Ferrari, M. B. (2005) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20054 · Cited by 14
“ML-7 has been shown to inhibit smooth MLCK and is one of the most highly specific of the commonly used kinase inhibitors [Bain et al., 2003].”
Background
MEK/Erk-based negative feedback mechanism involved in control of Steel Factor-triggered production of Krüppel-like factor 2 in mast cells
Marschall, J., Wilhelm, T., Schuh, W., & Huber, M. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.12.007 · Cited by 14
Src family kinase involvement in rat preglomerular microvascular contractile and [Ca2+]iresponses to ANG II
Che, Q., & Carmines, P. K. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00392.2004 · Cited by 14
“PP2 inhibits Src family kinases with IC50 values in the low nanomolar range (2, 18); a few other protein kinases (Csk, p38) are inhibited an order of magnitude less potently (2).”
Background
Regulation of N-Formyl Peptide Receptor Signaling and Trafficking by Arrestin-Src Kinase Interaction
Wagener, B. M., Marjon, N. A., & Prossnitz, E. R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147442 · Cited by 14
Regulation of thrombin-induced plasminogen activator inhibitor-1 in 4T1 murine breast cancer cells
McEachron, T. A., Church, F., & Mackman, N. (2011) · Blood Coagulation & Fibrinolysis · doi:10.1097/mbc.0b013e3283497647 · Cited by 14
The relationship between basal and regulated Gnrhr expression in rodent pituitary gonadotrophs
Bjelobaba, I. M., Janjic, M. M., Tavcar, J. S., Kučka, M., Tomić, M., & Stojilković, S. S. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.08.040 · Cited by 14
“In contrast, inhibition of MEK1/2 with U0126, p38 MAPK with SB203580 [38], big MAPK with BIX02189 [39], and JNK with SP600125 [40], did not affect basal gene expression (Fig.”
Background
Profiling Subcellular Protein Phosphatase Responses to Coxsackievirus B3 Infection of Cardiomyocytes
Shah, M., Smolko, C. M., Kinicki, S., Chapman, Z. D., Brautigan, D. L., & Janes, K. A. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o116.063487 · Cited by 14
“Prior CVB3 studies involving the JNK pathway relied on a first-generation inhibitor that is now known to inhibit many other kinases (38, 111, 112).”
Background
Phosphomimetic substitution at Ser-33 of the chloroquine resistance transporter PfCRT reconstitutes drug responses in Plasmodium falciparum
Sanchez, C. P., Cubel, S. M., Nyboer, B., Jankowska-Döllken, M., Schaeffer‐Reiss, C., Ayoub, D., Planelles, G., & Lanzer, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009464 · Cited by 14
“falciparum, and studies conducted in other systems have demonstrated that kinase inhibitors often lack selectivity and specificity (33, 34).”
Background
Prospects for the development of small molecular weight compounds to replace anti-tumour necrosis factor biological agents
Foxwell, B. M. J., Andreakos, E., Brennan, F., Feldmann, M., Smith, C., & Conron, M. (2003) · Annals of the Rheumatic Diseases · doi:10.1136/ard.62.suppl_2.ii90 · Cited by 14
Expression of cyclin E in resting and activated B‐chronic lymphocytic leukaemia cells: cyclin E/cdk2 as a potential therapeutic target
Decker, T. W., Hipp, S., Hahntow, I. N., Schneller, F., & Peschel, C. (2004) · British Journal of Haematology · doi:10.1111/j.1365-2141.2004.04901.x · Cited by 14
“In addition, we investigated the importance of cyclin E-dependent cdk2 kinase activity for cell cycle progression in cycling B-CLL cells by performing in vitro kinase assays and pharmacological inhibition with Roscovitine, a cdk2 inhibitor with high specificity (Bain et al, 2003).”
BackgroundInfluential
Inhibition of ERK and JNK Decreases Both Osmosensitive Taurine Release and Cell Proliferation in Glioma Cells
Belsey, M. J., Davies, A. R. L., Witchel, H. J., & Kozlowski, R. Z. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9389-7 · Cited by 14
“less specific and inhibits proteins such as p70 ribosomal protein S6 kinase [50].”
Background
Improved yields for baculovirus-mediated expression of human His6-PDK1 and His6-PKBβ/Akt2 and characterization of phospho-specific isoforms for design of inhibitors that stabilize inactive conformations
Gao, X., Yo, P., & Harris, T. K. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.03.017 · Cited by 14
c-Jun N-terminal kinase mediates constitutive human eosinophil apoptosis
Hasala, H., Zhang, X., Saarelainen, S., Moilanen, E., & Kankaanranta, H. (2006) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2006.06.004 · Cited by 14
“Addressing the question of the specificity of the JNK inhibitors, which is essential when drawing conclusions from studies made with protein kinase inhibitors, Bain and co-workers [28] have recently shown that the most commonly used JNK inhibitor SP600125 is a relatively weak and non-specific inhibitor of JNK.”
Background
Overcoming the Hurdle of Fluorescent Compounds in Kinase Screening: A Case Study
Perrin, D., Martin, T., Cambet, Y., Frémaux, C., & Scheer, A. (2006) · Assay and Drug Development Technologies · doi:10.1089/adt.2006.4.185 · Cited by 14
“26 One way to solve this problem would be to screen by affinity, in order to try to impede interactions between the kinase and either its substrate, regulatory or scaffolding proteins, or lipids.”
Different roles for non-receptor tyrosine kinases in arachidonate release induced by zymosan and Staphylococcus aureus in macrophages
Olsson, S., & Sundler, R. (2006) · Journal of Inflammation · doi:10.1186/1476-9255-3-8 · Cited by 14
“PP2 has been shown to inhibit human p38 with similar potency as the SFK member Lck [23] which could, potentially, influence the interpretation of our data on arachidonate release.”
Background
Transforming Growth Factor B1 Stimulated DNA Synthesis in the Granulosa Cells of Preantral Follicles: Negative Interaction with Epidermal Growth Factor1
Yang, P., & Roy, S. K. (2006) · Biology of Reproduction · doi:10.1095/biolreprod.105.050294 · Cited by 14
“Follicles were cultured for 1 h with 10 lM PD98059 [21], 100 nM GFXI [26], or 100 nM SB203580 [27] to block MAPK3/1, PKC, or MAPK14 activity, respectively, before the administration of 5 ng/ml TGFB1 and [3H]thymidine.”
MethodInfluential
Combining RNA interference and kinase inhibitors against cell signalling components involved in cancer
O'Grady, M., Raha, D., Hanson, B. J., Bunting, M., & Hanson, G. T. (2005) · BMC Cancer · doi:10.1186/1471-2407-5-125 · Cited by 14
“Most kinase inhibitors target the ATP-binding site common to all kinases, and can bind multiple kinases [17].”
BackgroundResult
Activation of the Apoptotic JNK Pathway Through the Rac1‐Binding Scaffold Protein POSH
Xu, Z., & Greene, L. A. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)06036-8 · Cited by 14
Imprint of evolutionary conservation and protein structure variation on the binding function of protein tyrosine kinases
Verkhivker, G. M. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl199 · Cited by 14
Protocols for Regulation and Study of Diphosphoinositol Polyphosphates
Safrany, S. T. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.002667 · Cited by 13
“One is also able to exclude any roles played by Rho-associated, coiled-coil-forming protein kinase II, protein kinase C-related protein kinase 2, mitogen- and stress-activated protein kinase 1, mitogen-activated protein kinase-activated protein kinase-1b, and p70 ribosomal protein S6 kinase, because HA1077 (3 mM) and…”
Background
Src kinases play a novel dual role in acute pancreatitis affecting severity but no role in stimulated enzyme secretion
Nuche‐Berenguer, B., Ramos-Álvarez, I., & Jensen, R. T. (2016) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00349.2015 · Cited by 13
“In our previous study (51) assessing the effect of the widely used Src inhibitor PP2 and its inactive control PP3 (2, 3) on acinar cell signaling cascades, the incubation periods were short ( 10 min), whereas studies using in vitro CCK-induced rat models of pancreatitis generally require an incubation with supramaxima…”
Background
Elucidating Pathogenic Mechanisms of Early-onset Alzheimer's Disease in Down Syndrome Patients
Asai, M., Kawakubo, T., Mori, R., & Iwata, N. (2017) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.16-00236-2 · Cited by 13
c-Src kinase inhibits osteogenic differentiation via enhancing STAT1 stability
Alvandi, Z., & Opas, M. (2020) · PLoS ONE · doi:10.1371/journal.pone.0241646 · Cited by 13
“[29] wherever indicated.”

Authors: BAIN, J., McLAUCHLAN, H., ELLIOTT, M., & COHEN, P.
Affiliations: University of Dundee (GB)
Corresponding author: BAIN, Jenny
McLAUCHLAN, Hilary
ELLIOTT, Matthew
COHEN, Philip
ORCID: ELLIOTT, Matthew
COHEN, Philip
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2003-04-01
Volume: 371
Issue: 1
Pages: 199-204
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20021535
PMC: PMC1223271
OpenAlex: W2011588737
Cited by: 1,369
References: 42
Citations by year: 2026: 9 · 2025: 21 · 2024: 12 · 2023: 16 · 2022: 26 · 2021: 35 · 2020: 28 · 2019: 38 · 2018: 42 · 2017: 48 · 2016: 42 · 2015: 44 · 2014: 52 · 2013: 66 · 2012: 70
FWCI: 43.75
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Mechanisms and Therapy
Keywords: protein kinase inhibitors, kinase selectivity, serine/threonine kinase, indirubin-3'-monoxime, KT5823, ML-9, kenpaullone, roscovitine, pyrazolopyrimidines, cyclin-dependent kinases, glycogen synthase kinase-3, Src family kinases, epigallocatechin gallate, DYRK1A, kinase substrate identification
MeSH terms: Alkaloids, Anthracenes, Azepines, Benzazepines, Carbazoles, Catechin, Enzyme Inhibitors, Indoles, Kinetin, Naphthalenes, Oximes, Purines, Pyrazoles, Pyrimidines, Substrate Specificity, Signal Transduction, Cyclin-Dependent Kinases, src-Family Kinases, Mitogen-Activated Protein Kinases, Glycogen Synthase Kinase 3, Protein Kinase Inhibitors, JNK Mitogen-Activated Protein Kinases

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The specificities of protein kinase inhibitors: an update

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