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Journal articles on the topic 'TYROSINE KINASE ASSAY'

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Published: 11 March 2023

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1

Tyner, Jeffrey W., Stephanie Willis, Michael W. N. Deininger, and Brian J. Druker. "RNAi Functional Screening of the Tyrosine Kinome Identifies Therapeutic Targets in Acute Myeloid Leukemia Patients." Blood 110, no. 11 (2007): 208. http://dx.doi.org/10.1182/blood.v110.11.208.208.

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Abstract A large percentage of cancer cases present without knowledge of the causative genetic events. Tyrosine kinases are frequently implicated in the pathogenesis of cancer, but identification of specific tyrosine kinases as cancer targets has been a slow process. Tyrosine kinases are thought to play a causative role in acute myeloid leukemia (AML), based in part on the high percentage of cases with phosphorylation of STAT5—a marker for activity of tyrosine kinase signaling. However, known abnormalities in tyrosine kinases in AML are restricted to internal tandem duplications of FLT3 or gen

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2

Pritz, Stephan, Gabriele Meder, Klaus Doering, et al. "A Fluorescence Lifetime-Based Assay for Abelson Kinase." Journal of Biomolecular Screening 16, no. 1 (2010): 65–72. http://dx.doi.org/10.1177/1087057110385817.

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We present a novel homogeneous in vitro assay format and apply it to the quantitative determination of the enzymatic activity of a tyrosine kinase. The assay employs a short peptidic substrate containing a single tyrosine and a single probe attached via a cysteine side chain. The structural flexibility of the peptide allows for the dynamic quenching of the probe by the nonphosphorylated tyrosine side chain. The probe responds with changes in its fluorescence lifetime depending on the phosphorylation state of the tyrosine. We use this effect to directly follow the enzymatic phosphorylation of t

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3

Lebakken, Connie S., Hee Chol Kang, and Kurt W. Vogel. "A Fluorescence Lifetime–Based Binding Assay to Characterize Kinase Inhibitors." Journal of Biomolecular Screening 12, no. 6 (2007): 828–41. http://dx.doi.org/10.1177/1087057107304480.

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The authors present a fluorescence lifetime—based kinase binding assay that identifies and characterizes compounds that bind to the adenosine triphosphate (ATP)—binding pocket of a range of tyrosine and serine/threonine kinases. The assay is based on displacement of an Alexa Fluor® 647 conjugate of staurosporine from the ATP-binding site of a kinase, which is detected by a change in the fluorescence lifetime of the probe between the free (displaced) and kinase-bound states. The authors screened 257 kinases for specific binding and displacement of the Alexa Fluor® 647-staurosporine probe and fo

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4

Kobayashi, Tomoko, Shun-Ichi Nakamura, and Hirohei Yamamura. "Cytosolic Protein-Tyrosine Kinase Activities in Various Rat Tissues." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 26, no. 2 (1989): 164–68. http://dx.doi.org/10.1177/000456328902600213.

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Suitable assay conditions for the detection of cytosolic protein-tyrosine kinase activities in crude extracts of various rat tissues have been determined. Cytosolic protein-tyrosine kinases showed common characteristics including substrate specificity and divalent cation requirement. Using (Val5) angiotensin II and Mn2+ rather than a src-related synthetic peptide, E11G1, and Mg2+, we obtained higher activities of cytosolic protein-tyrosine kinases. Among various rat tissues tested, spleen, bone marrow, thymus, small intestine, appendix and lung, in decreasing order of total activity, contained

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5

Tyner, Jeffrey W., Denise K. Walters, Stephanie G. Willis, et al. "RNAi screening of the tyrosine kinome identifies therapeutic targets in acute myeloid leukemia." Blood 111, no. 4 (2008): 2238–45. http://dx.doi.org/10.1182/blood-2007-06-097253.

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Despite vast improvements in our understanding of cancer genetics, a large percentage of cancer cases present without knowledge of the causative genetic events. Tyrosine kinases are frequently implicated in the pathogenesis of numerous types of cancer, but identification and validation of tyrosine kinase targets in cancer can be a time-consuming process. We report the establishment of an efficient, functional screening assay using RNAi technology to directly assess and compare the effect of individually targeting each member of the tyrosine kinase family. We demonstrate that siRNA screening ca

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6

Wu, Jinzi J., Donna R. Yarwood, Quynhchi Pham, and Matthew A. Sills. "Identification of a High-Affinity Anti-Phosphoserine Antibody for the Development of a Homogeneous Fluorescence Polarization Assay of Protein Kinase C." Journal of Biomolecular Screening 5, no. 1 (2000): 23–30. http://dx.doi.org/10.1177/108705710000500106.

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In the last few years, fluorescence polarization (FP) has been applied to the development of robust, homogeneous, high throughput assays in molecular recognition research, such as ligand-protein interactions. Recently, this technology has been applied to the development of homogeneous tyrosine kinase assays, since there are high-affinity anti-phosphotyrosine antibodies available. Unlike tyrosine kinases, application of FP to assay development for serine/threonine kinases has been impeded because of lack of high-affinity anti-phosphoserine/threonine antibodies. In the present study, we report t

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7

Tyner, Jeffrey W., Luke Fletcher, Wayne Yang, et al. "Development of a Small-Molecule Inhibitor Screen to Rapidly Identify Key Signaling Pathways in Leukemogenesis." Blood 114, no. 22 (2009): 708. http://dx.doi.org/10.1182/blood.v114.22.708.708.

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Abstract Abstract 708 Aberrantly activated tyrosine kinases and their associated signaling pathways are critical to leukemogenesis and primary acute myeloid leukemia (AML) cell viability. While aberrant kinase activation has been confirmed in a significant percentage of AML, constitutive phosphorylation of STAT5, a marker of tyrosine kinase activation, is present in the majority of AML samples indicating that as yet unidentified tyrosine kinases can be aberrantly activated and contribute to leukemogenesis. Efforts to identify activating tyrosine kinase mutations using high-throughput sequencin

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8

Nakayama, Grace R., Michael P. Nova, and Zahra Parandoosh. "A Scintillating Microplate Assay for the Assessment of Protein Kinase Activity." Journal of Biomolecular Screening 3, no. 1 (1998): 43–48. http://dx.doi.org/10.1177/108705719800300106.

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Protein kinases, a class of enzymes that phosphorylate certain tyrosine, serine, and threonine residues, play an important role in cellular functions and are important targets in drug discovery research. Thus, it is of interest to develop a simple assay that can be used to measure protein kinase activity toward specific substrates and is suitable for the high throughput screening (HTS) of potential kinase inhibitors. The scintillation proximity concept has been successfully applied for measuring specific kinase activity using surfaces passively coated with a peptide substrate. In this study, w

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9

Binns, Kathleen L., Paul P. Taylor, Frank Sicheri, Tony Pawson, and Sacha J. Holland. "Phosphorylation of Tyrosine Residues in the Kinase Domain and Juxtamembrane Region Regulates the Biological and Catalytic Activities of Eph Receptors." Molecular and Cellular Biology 20, no. 13 (2000): 4791–805. http://dx.doi.org/10.1128/mcb.20.13.4791-4805.2000.

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ABSTRACT Members of the Eph family of receptor tyrosine kinases exhibit a striking degree of amino acid homology, particularly notable in the kinase and membrane-proximal regions. A mutagenesis approach was taken to address the functions of specific conserved tyrosine residues within these catalytic and juxtamembrane domains. Ligand stimulation of wild-type EphB2 in neuronal NG108-15 cells resulted in an upregulation of catalytic activity and an increase in cellular tyrosine phosphorylation, accompanied by a retraction of neuritic processes. Tyrosine-to-phenylalanine substitutions within the c

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10

Rivard, N., G. Rydzewska, J. S. Lods, and J. Morisset. "Novel model of integration of signaling pathways in rat pancreatic acinar cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 269, no. 3 (1995): G352—G362. http://dx.doi.org/10.1152/ajpgi.1995.269.3.g352.

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Cholecystokinin (CCK) is the major pancreatic secretagogue and acinar cell mitogen. This study was performed to determine by which effector systems CCK regulates tyrosine kinases, phosphatidylinositol (PtdIns) 3-kinase, and phospholipase D (PLD) activities. Pancreatic acini loaded with [3H]myristic acid or [3H]inositol were used to assay PLD and PtdIns 3-kinase. G protein activation with NaF increased particulate and crude cytosolic tyrosine kinase and PLD activities. PLD activation was pertussis toxin sensitive. Inhibition of phospholipase C (PLC) slightly reduced caerulein-stimulated particu

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11

Dailey, D., G. L. Schieven, M. Y. Lim, et al. "Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton phosphotyrosyl protein associated with protein-tyrosine kinase activity." Molecular and Cellular Biology 10, no. 12 (1990): 6244–56. http://dx.doi.org/10.1128/mcb.10.12.6244-6256.1990.

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Extracts of bakers' yeast (Saccharomyces cerevisiae) contain protein-tyrosine kinase activity that can be detected with a synthetic Glu-Tyr copolymer as substrate (G. Schieven, J. Thorner, and G.S. Martin, Science 231:390-393, 1986). By using this assay in conjunction with ion-exchange and affinity chromatography, a soluble tyrosine kinase activity was purified over 8,000-fold from yeast extracts. The purified activity did not utilize typical substrates for mammalian protein-tyrosine kinases (enolase, casein, and histones). The level of tyrosine kinase activity at all steps of each preparation

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Dailey, D., G. L. Schieven, M. Y. Lim, et al. "Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton phosphotyrosyl protein associated with protein-tyrosine kinase activity." Molecular and Cellular Biology 10, no. 12 (1990): 6244–56. http://dx.doi.org/10.1128/mcb.10.12.6244.

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Extracts of bakers' yeast (Saccharomyces cerevisiae) contain protein-tyrosine kinase activity that can be detected with a synthetic Glu-Tyr copolymer as substrate (G. Schieven, J. Thorner, and G.S. Martin, Science 231:390-393, 1986). By using this assay in conjunction with ion-exchange and affinity chromatography, a soluble tyrosine kinase activity was purified over 8,000-fold from yeast extracts. The purified activity did not utilize typical substrates for mammalian protein-tyrosine kinases (enolase, casein, and histones). The level of tyrosine kinase activity at all steps of each preparation

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13

Nevenzel, Hadas, Amit Zur, and Doron Gerber. "A Microfluidic-Based Tyrosine Kinase and Phosphatase Assay." Biophysical Journal 102, no. 3 (2012): 187a—188a. http://dx.doi.org/10.1016/j.bpj.2011.11.1023.

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14

Kashem, Mohammed A., Richard M. Nelson, Jeffrey D. Yingling, et al. "Three Mechanistically Distinct Kinase Assays Compared: Measurement of Intrinsic ATPase Activity Identified the Most Comprehensive Set of ITK Inhibitors." Journal of Biomolecular Screening 12, no. 1 (2006): 70–83. http://dx.doi.org/10.1177/1087057106296047.

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Numerous assay methods have been developed to identify small-molecule effectors of protein kinases, but no single method can be applied to all isolated kinases. The authors developed a set of 3 high-throughput screening (HTS)–compatible biochemical assays that can measure 3 mechanistically distinct properties of a kinase active site, with the goal that at least 1 of the 3 would be applicable to any kinase selected as a target for drug discovery efforts. Two assays measure catalytically active enzyme: A dissociation-enhanced lanthanide fluoroimmuno assay (DELFIA) uses an antibody to quantitate

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15

MELANDER, Fredrik, Tommy ANDERSSON, and Karim DIB. "Fgr but not Syk tyrosine kinase is a target for beta2 integrin-induced c-Cbl-mediated ubiquitination in adherent human neutrophils." Biochemical Journal 370, no. 2 (2003): 687–94. http://dx.doi.org/10.1042/bj20021201.

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An early and critical event in β2 integrin signalling during neutrophil adhesion is activation of Src tyrosine kinases and Syk. In the present study, we report Src kinase-dependent β2 integrin-induced tyrosine phosphorylation of Cbl occurring in parallel with increased Cbl-associated tyrosine kinase activity. These events concurred with activation of Fgr and, surprisingly, also with dissociation of this Src tyrosine kinase from Cbl. Moreover, the presence of the Src kinase inhibitor PP1 in an in vitro assay had only a limited effect on the Cbl-associated kinase activity. These results suggest

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16

Yu, C. L., R. Jove, and S. J. Burakoff. "Constitutive activation of the Janus kinase-STAT pathway in T lymphoma overexpressing the Lck protein tyrosine kinase." Journal of Immunology 159, no. 11 (1997): 5206–10. http://dx.doi.org/10.4049/jimmunol.159.11.5206.

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Abstract The Lck protein, a Src family tyrosine kinase, plays a critical role in T cell maturation and activation. Dysregulation of Lck expression or Lck kinase activity has been implicated in T cell leukemias from mice to humans, although the mechanism underlying Lck-mediated oncogenesis is still largely unclear. We report here that both DNA binding activities and tyrosine phosphorylation of STAT3 and STAT5, but not STAT1, are constitutively enhanced in the mouse T cell lymphoma LSTRA, which is a well-characterized cell line that overexpresses Lck protein and exhibits high levels of Lck kinas

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17

Pazdrak, K., L. Justement, and R. Alam. "Mechanism of inhibition of eosinophil activation by transforming growth factor-beta. Inhibition of Lyn, MAP, Jak2 kinases and STAT1 nuclear factor." Journal of Immunology 155, no. 9 (1995): 4454–58. http://dx.doi.org/10.4049/jimmunol.155.9.4454.

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Abstract The activation of eosinophils by IL-5 plays a crucial role in the pathogenesis of allergic and parasitic disorders. IL-5 has recently been shown to activate Lyn and Jak2 tyrosine kinases, MAP kinases, and STAT1 nuclear factor. We have previously reported that TGF-beta blocks the IL-5-induced activation of eosinophils. In this study, we investigated the effect of TGF-beta on the IL-5-induced signaling molecules in eosinophils. Purified eosinophils from mildly allergic patients were preincubated with TGF-beta and then stimulated with IL-5. The cell lysates were then immunoprecipitated a

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18

Laniyonu, Adebayo, Seiji Eto, Jerry H. Wang, and Morley D. Hollenberg. "Detection of sarcoma virus family tyrosine kinase activity in coronary arterial tissue." Canadian Journal of Physiology and Pharmacology 73, no. 11 (1995): 1552–60. http://dx.doi.org/10.1139/y95-214.

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We have observed that the tyrosine kinase inhibitors genistein and tyrphostin can selectively block angiotensin II mediated and vasopressin-mediated contractions in porcine coronary arterial strips, without affecting the action of acetylcholine. Therefore, we assessed the presence of tyrosine kinase activity in the porcine coronary artery tissue, using an assay specific for sarcoma virus (src) related tyrosine kinases. In both membrane and cytosolic fractions of porcine coronary artery, we detected src-related tyrosine kinase activity that could be inhibited by both genistein and tyrphostin. T

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19

Bicocca, Vincent, Bill H. Chang, Markus Muschen, Brian J. Druker, and Jeffrey W. Tyner. "ROR1 as a Therapeutic Target In E2A-PBX1-Positive Acute Lymphoblastic Leukemia." Blood 116, no. 21 (2010): 539. http://dx.doi.org/10.1182/blood.v116.21.539.539.

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Abstract Abstract 539 Background: Aberrant tyrosine kinase activity is commonly implicated in the pathogenesis of leukemia and other cancers. Identification of these leukemogenic tyrosine kinases has proven invaluable for diagnostic and prognostic stratification of patients as well as for the development of novel strategies for therapeutic intervention. We previously demonstrated that siRNA screening of mononuclear cells from leukemia patients can determine sensitivity to individual tyrosine kinases. With the goal of uncovering novel viability-dependent tyrosine kinases in leukemia patients, w

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20

Freiberg, Gail, Julie Wilkins, Caroline David та ін. "Utilization of Microarrayed Compound Screening (μARCS) to Identify Inhibitors of p56lck Tyrosine Kinase". Journal of Biomolecular Screening 9, № 1 (2004): 12–21. http://dx.doi.org/10.1177/1087057103259667.

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Protein tyrosine kinases play critical roles in cell signaling and are considered attractive targets for drug discovery. The authors have applied μARCS (microarrayed compound screening) technology to develop a high-throughput screen for finding inhibitors of the p56lck tyrosine kinase. Initial assay development was performed in a homogeneous time-resolved (LANCE™) format in 96-well microplates and then converted into the gel-based μARCS format. The μARCS methodology is a well-less screening format in which 8640 compounds are arrayed on a microplate-sized piece of polystyene and subsequently as

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21

Lee, Jennifer Y., Sheri Miraglia, Xiongwei Yan, et al. "Oncology Drug Discovery Applications Using the FMAT™ 8100 HTS System." Journal of Biomolecular Screening 8, no. 1 (2003): 81–88. http://dx.doi.org/10.1177/1087057102239668.

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High-throughput screening (HTS) for potential anticancer agents requires a broad portfolio of assay platforms that may include kinase enzyme assays, protein-protein binding assays, and functional cell-based apoptosis assays. The authors have explored the use of fluorometric microvolume assay technology (the FMAT™ 8100 HTS System) in three distinct homogeneous HTS assays: (1) a Src tyrosine kinase enzyme assay, (2) a Grb2-SH2 protein-peptide interaction assay, and (3) an annexin V binding apoptosis assay. Data obtained from all three assays suggest that the FMAT system should facilitate the imp

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Hsu, Jonathan, Jun Zhang, Chris Kitson та ін. "Development of a Pharmacodynamic Assay Based on PLCγ2 Phosphorylation for Quantifying Spleen Tyrosine Kinase (SYK)–Bruton’s Tyrosine Kinase (BTK) Signaling". Journal of Biomolecular Screening 18, № 8 (2013): 890–98. http://dx.doi.org/10.1177/1087057113489881.

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Spleen tyrosine kinase (SYK) and Bruton’s tyrosine kinase (BTK) are key mediators in coupling cell surface receptors, such as the B-cell receptor (BCR), to downstream signaling events affecting diverse biological functions. There is therefore tremendous interest in the development of pharmacological inhibitors targeting the SYK-BTK axis for the treatment of inflammatory disorders and hematological malignancies. A good pharmacodynamic (PD) assay, ideally a blood-based assay that measures proximal events, is warranted for evaluation of such inhibitors. In platelets, collagen-induced activation o

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23

Babcook, John, Julian Watts, Ruedi Aebersold, and Hermann J. Ziltener. "Automated nonisotopic assay for protein-tyrosine kinase and protein-tyrosine phosphatase activities." Analytical Biochemistry 196, no. 2 (1991): 245–51. http://dx.doi.org/10.1016/0003-2697(91)90461-2.

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24

Beeler, J. F., W. J. LaRochelle, M. Chedid, S. R. Tronick, and S. A. Aaronson. "Prokaryotic expression cloning of a novel human tyrosine kinase." Molecular and Cellular Biology 14, no. 2 (1994): 982–88. http://dx.doi.org/10.1128/mcb.14.2.982-988.1994.

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Screening of a human embryonic lung fibroblast cDNA expression library with antiphosphotyrosine antibodies led to isolation of a novel protein kinase. A clone, designated A6, contained a 3-kb cDNA insert with a predicted open reading frame of 350 amino acids. DNA sequence analysis failed to reveal any detectable similarity with previously known genes, and the predicted A6 protein lacked any of the motifs commonly conserved in the catalytic domains of protein kinases. However, the bacterially expressed beta-galactosidase-A6 fusion protein demonstrated both tyrosine and serine phosphorylation in

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Beeler, J. F., W. J. LaRochelle, M. Chedid, S. R. Tronick, and S. A. Aaronson. "Prokaryotic expression cloning of a novel human tyrosine kinase." Molecular and Cellular Biology 14, no. 2 (1994): 982–88. http://dx.doi.org/10.1128/mcb.14.2.982.

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Screening of a human embryonic lung fibroblast cDNA expression library with antiphosphotyrosine antibodies led to isolation of a novel protein kinase. A clone, designated A6, contained a 3-kb cDNA insert with a predicted open reading frame of 350 amino acids. DNA sequence analysis failed to reveal any detectable similarity with previously known genes, and the predicted A6 protein lacked any of the motifs commonly conserved in the catalytic domains of protein kinases. However, the bacterially expressed beta-galactosidase-A6 fusion protein demonstrated both tyrosine and serine phosphorylation in

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Gaudry, M., C. Gilbert, F. Barabe, PE Poubelle, and PH Naccache. "Activation of Lyn is a common element of the stimulation of human neutrophils by soluble and particulate agonists." Blood 86, no. 9 (1995): 3567–74. http://dx.doi.org/10.1182/blood.v86.9.3567.bloodjournal8693567.

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The functional responsiveness of human neutrophils is known to be initiated and modulated by protein tyrosine phosphorylation. The regulation of the levels of tyrosine phosphorylation is most likely the result of the coordinated actions of tyrosine kinases and phosphatases, which have so far been only very partially characterized. In the present study, we present evidence demonstrating that the stimulation of neutrophils by a variety of agonists (soluble as well as particulate) leads to the activation of the src-related tyrosine kinase lyn. The stimulation of tyrosine kinase activity of lyn wa

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27

Sills, Matthew A., Donna Weiss, Quynhchi Pham, Robert Schweitzer, Xiang Wu, and Jinzi J. Wu. "Comparison of Assay Technologies for a Tyrosine Kinase Assay Generates Different Results in High Throughput Screening." Journal of Biomolecular Screening 7, no. 3 (2002): 191–214. http://dx.doi.org/10.1177/108705710200700304.

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In today's high-throughput screening (HTS) environment, an increasing number of assay detection technologies are routinely utilized in lead finding programs. Because of the relatively broad applicability of several of these technologies, one is often faced with a choice of which technology to utilize for a specific assay. The aim of this study was to address the question of whether the same compounds would be identified from screening a set of samples in three different versions of an HTS assay. Here, three different versions of a tyrosine kinase assay were established using scintillation prox

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O'Bryan, J. P., R. A. Frye, P. C. Cogswell, et al. "axl, a transforming gene isolated from primary human myeloid leukemia cells, encodes a novel receptor tyrosine kinase." Molecular and Cellular Biology 11, no. 10 (1991): 5016–31. http://dx.doi.org/10.1128/mcb.11.10.5016-5031.1991.

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Using a sensitive transfection-tumorigenicity assay, we have isolated a novel transforming gene from the DNA of two patients with chronic myelogenous leukemia. Sequence analysis indicates that the product of this gene, axl, is a receptor tyrosine kinase. Overexpression of axl cDNA in NIH 3T3 cells induces neoplastic transformation with the concomitant appearance of a 140-kDa axl tyrosine-phosphorylated protein. Expression of axl cDNA in the baculovirus system results in the expression of the appropriate recombinant protein that is recognized by antiphosphotyrosine antibodies, confirming that t

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O'Bryan, J. P., R. A. Frye, P. C. Cogswell, et al. "axl, a transforming gene isolated from primary human myeloid leukemia cells, encodes a novel receptor tyrosine kinase." Molecular and Cellular Biology 11, no. 10 (1991): 5016–31. http://dx.doi.org/10.1128/mcb.11.10.5016.

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Using a sensitive transfection-tumorigenicity assay, we have isolated a novel transforming gene from the DNA of two patients with chronic myelogenous leukemia. Sequence analysis indicates that the product of this gene, axl, is a receptor tyrosine kinase. Overexpression of axl cDNA in NIH 3T3 cells induces neoplastic transformation with the concomitant appearance of a 140-kDa axl tyrosine-phosphorylated protein. Expression of axl cDNA in the baculovirus system results in the expression of the appropriate recombinant protein that is recognized by antiphosphotyrosine antibodies, confirming that t

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Lamaze, C., and S. L. Schmid. "Recruitment of epidermal growth factor receptors into coated pits requires their activated tyrosine kinase." Journal of Cell Biology 129, no. 1 (1995): 47–54. http://dx.doi.org/10.1083/jcb.129.1.47.

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EGF-receptor (EGF-R) tyrosine kinase is required for the down-regulation of activated EGF-R. However, controversy exists as to whether ligand-induced activation of the EGF-R tyrosine kinase is required for internalization or for lysosomal targeting. We have addressed this issue using a cell-free assay that selectively measures the recruitment of EGF-R into coated pits. Here we show that EGF bound to wild-type receptors is efficiently sequestered in coated pits. In contrast, sequestration of kinase-deficient receptors occurs inefficiently and at the same basal rate of endocytosis of unoccupied

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Konopka, J. B., and O. N. Witte. "Detection of c-abl tyrosine kinase activity in vitro permits direct comparison of normal and altered abl gene products." Molecular and Cellular Biology 5, no. 11 (1985): 3116–23. http://dx.doi.org/10.1128/mcb.5.11.3116-3123.1985.

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The v-abl transforming protein P160v-abl and the P210c-abl gene product of the translocated c-abl gene in Philadelphia chromosome-positive chronic myelogenous leukemia cells have tyrosine-specific protein kinase activity. Under similar assay conditions the normal c-abl gene products, murine P150c-abl and human P145c-abl, lacked detectable kinase activity. Reaction conditions were modified to identify conditions which would permit the detection of c-abl tyrosine kinase activity. It was found that the Formalin-fixed Staphylococcus aureus formerly used for immunoprecipitation inhibits in vitro ab

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Konopka, J. B., and O. N. Witte. "Detection of c-abl tyrosine kinase activity in vitro permits direct comparison of normal and altered abl gene products." Molecular and Cellular Biology 5, no. 11 (1985): 3116–23. http://dx.doi.org/10.1128/mcb.5.11.3116.

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The v-abl transforming protein P160v-abl and the P210c-abl gene product of the translocated c-abl gene in Philadelphia chromosome-positive chronic myelogenous leukemia cells have tyrosine-specific protein kinase activity. Under similar assay conditions the normal c-abl gene products, murine P150c-abl and human P145c-abl, lacked detectable kinase activity. Reaction conditions were modified to identify conditions which would permit the detection of c-abl tyrosine kinase activity. It was found that the Formalin-fixed Staphylococcus aureus formerly used for immunoprecipitation inhibits in vitro ab

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Patel, Jay, Christopher J. Stanley, and Stuart M. Wilson. "Homogeneous Assay for Tyrosine Kinase: Use of Bacteriophage Antibody Conjugates in an Assay for p56lck Kinase." Clinical Chemistry 48, no. 10 (2002): 1860–62. http://dx.doi.org/10.1093/clinchem/48.10.1860.

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Tyner, Jeffrey W., Stephen Spurgeon, Luke B. Fletcher, et al. "A Small-Molecule Inhibitor Screen Rapidly Identifies Therapeutic Targets and Individualized Therapeutic Strategies In Patients with Acute and Chronic Leukemias." Blood 116, no. 21 (2010): 2754. http://dx.doi.org/10.1182/blood.v116.21.2754.2754.

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Abstract Abstract 2754 The development of more effective and less toxic therapies for acute and chronic leukemias will require the identification of the molecular abnormalities contributing to leukemogenesis and the identification of drugs that specifically block the activity of these lesions. We hypothesize that aberrantly activated tyrosine kinase signaling pathways play a critical role in the pathogenesis of a substantial proportion of leukemia cases, and our preliminary data suggest that the molecular abnormalities causing aberrant kinase activation are unique in a significant number of pa

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35

SIERKE, Susan L., Kunrong CHENG, Hong-Hee KIM, and John G. KOLAND. "Biochemical characterization of the protein tyrosine kinase homology domain of the ErbB3 (HER3) receptor protein." Biochemical Journal 322, no. 3 (1997): 757–63. http://dx.doi.org/10.1042/bj3220757.

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The putative protein tyrosine kinase domain (TKD) of the ErbB3 (HER3) receptor protein was generated as a histidine-tagged recombinant protein (hisTKD-B3) and characterized enzymologically. CD spectroscopy indicated that the hisTKD-B3 protein assumed a native conformation with a secondary structure similar to that of the epidermal growth factor (EGF) receptor TKD. However, when compared with the EGF receptor-derived protein, hisTKD-B3 exhibited negligible intrinsic protein tyrosine kinase activity. Immune complex kinase assays of full-length ErbB3 proteins also yielded no evidence of catalytic

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Angeles, Thelma S., Catherine Steffler, Becky A. Bartlett, et al. "Enzyme-Linked Immunosorbent Assay for trkA Tyrosine Kinase Activity." Analytical Biochemistry 236, no. 1 (1996): 49–55. http://dx.doi.org/10.1006/abio.1996.0130.

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Zhang, Zheng, Hava Avraham, and David M. Cohen. "Urea and NaCl differentially regulate FAK and RAFTK/PYK2 in mIMCD3 renal medullary cells." American Journal of Physiology-Renal Physiology 275, no. 3 (1998): F447—F451. http://dx.doi.org/10.1152/ajprenal.1998.275.3.f447.

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Two cytosolic tyrosine kinases, focal adhesion kinase (FAK) and the newly described FAK homolog, related adhesion focal tyrosine kinase (RAFTK, also called PYK2 and CAKβ), have been implicated in signaling to multiple mitogen-activated protein kinase (MAPK) pathways. Therefore, the ability of NaCl and urea to activate these kinases was investigated by in vitro kinase assay and anti-phosphotyrosine immunoblotting. RAFTK was promptly but only transiently activated by urea (within 1 min; 45%), whereas NaCl activated this kinase at 1, 5, 15, and 30 min of treatment (35–60%). In contrast, FAK exhib

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Jiang, Chao, Ya Li, Chenghui Liu, Liying Qiu, and Zhengping Li. "A general and versatile fluorescence turn-on assay for detecting the activity of protein tyrosine kinases based on phosphorylation-inhibited tyrosyl oxidation." Chemical Communications 52, no. 85 (2016): 12570–73. http://dx.doi.org/10.1039/c6cc07035c.

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Parker, Gregory J., Tong Lin Law, Francis J. Lenoch, and Randall E. Bolger. "Development of High Throughput Screening Assays Using Fluorescence Polarization: Nuclear Receptor-Ligand-Binding and Kinase/Phosphatase Assays." Journal of Biomolecular Screening 5, no. 2 (2000): 77–88. http://dx.doi.org/10.1177/108705710000500204.

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Fluorescence polarization (FP) has been used to develop high throughput screening (HTS) assays for nuclear receptor-ligand displacement and kinase inhibition. FP is a solution-based, homogeneous technique requiring no immobilization or separation of reaction components. The FP-based estrogen receptor (ER) assay is based on the competition of fluorescein-labeled estradiol and estrogen-like compounds for binding to ER. These studies determined the Kd for this interaction to be 3 nM for ERα and 2 nM for ERβ; IC50 values for 17β-estradiol, tamoxifen, 4-OH-tamoxifen, and diethylstibestrol were dete

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Atienza, Josephine M., Naichen Yu, Xiaobo Wang, Xiao Xu, and Yama Abassi. "Label-Free and Real-Time Cell-Based Kinase Assay for Screening Selective and Potent Receptor Tyrosine Kinase Inhibitors Using Microelectronic Sensor Array." Journal of Biomolecular Screening 11, no. 6 (2006): 634–43. http://dx.doi.org/10.1177/1087057106289334.

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Kinases are the 2nd largest group of therapeutic targets in the human genome. In this article, a label-free and real-time cell-based receptor tyrosine kinase (RTK) assay that addresses limitation of existing kinase assays and can be used for high-throughput screening and lead optimization studies was validated and characterized. Using impedance, growth factor-induced morphological changes were quantitatively assessed in real time and used as a measure of RTK activity. COS7 cells treated with epidermal growth factor (EGF) and insulin results in a rapid increase in cell impedance. Assessment of

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Smotrov, Nadya, Anjili Mathur, Ilona Kariv, Christopher M. Moxham, and Nathan Bays. "Development of a Cell-Based Assay for Measurement of c-Met Phosphorylation Using AlphaScreenTM Technology and High-Content Imaging Analysis." Journal of Biomolecular Screening 14, no. 4 (2009): 404–11. http://dx.doi.org/10.1177/1087057109331803.

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c-Met is a receptor tyrosine kinase (RTK) with a critical role in many fundamental cellular processes, including cell proliferation and differentiation. Deregulated c-Met signaling has been implicated in both the initiation and progression of human cancers and therefore represents an attractive target for anticancer therapy. Monitoring the phosphorylation status of relevant tyrosine residues provides an important method of assessing c-Met kinase activity. This report describes a novel assay to monitor c-Met phosphorylation in cells using Amplified Luminescent Proximity Homogeneous Assay (Alpha

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Pazdrak, K., D. Schreiber, P. Forsythe, L. Justement, and R. Alam. "The intracellular signal transduction mechanism of interleukin 5 in eosinophils: the involvement of lyn tyrosine kinase and the Ras-Raf-1-MEK-microtubule-associated protein kinase pathway." Journal of Experimental Medicine 181, no. 5 (1995): 1827–34. http://dx.doi.org/10.1084/jem.181.5.1827.

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Interleukin 5 (IL-5) regulates the growth and function of eosinophils. The objective of this study was to investigate the intracellular signal transduction mechanism of IL-5 in eosinophils. Purified eosinophils were stimulated with IL-5, and the involvement of various kinases was investigated by immunoblotting, immune complex kinase assay, and in situ denatured/renatured kinase assay. We found that IL-5 induced tyrosine phosphorylation and activation of a number of kinases. Two species of lyn kinases (53 and 56 kD) were present in eosinophils. Both forms were Tyr-phosphorylated and activated r

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Kinoshita-Kikuta, Emiko, Momoka Yoshimoto, Marina Yano, Eiji Kinoshita, and Tohru Koike. "An assay of human tyrosine protein kinase ABL activity using an Escherichia coli protein expression system." BioTechniques 70, no. 4 (2021): 209–17. http://dx.doi.org/10.2144/btn-2020-0154.

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ABL, a human tyrosine protein kinase, and its substrate are co-expressed in Escherichia coli. Tyrosine phosphorylation of the substrate in E. coli was detected using Phos-tag SDS-PAGE. The bacterial co-expression system was used as a field for the kinase reaction to evaluate the enzymatic activity of five types of ABL kinase domain mutants. Relative to wild-type ABL, kinase activity was comparable in the H396P mutant, reduced in both Y253F and E255K mutants and undetectable in T315I and M351T mutants. These comparative results demonstrated that the phosphorylation states of the mutants correla

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Dong, Z., X. Qi, and I. J. Fidler. "Tyrosine phosphorylation of mitogen-activated protein kinases is necessary for activation of murine macrophages by natural and synthetic bacterial products." Journal of Experimental Medicine 177, no. 4 (1993): 1071–77. http://dx.doi.org/10.1084/jem.177.4.1071.

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The purpose of these studies was to determine the intracellular signal transduction pathways of bacterial products in murine macrophages from lipopolysaccharide (LPS)-responder C3H/HeN and LPS-nonresponder C3H/HeJ mice. Both LPS and synthetic lipopeptide CGP 31362 (LPP) induced production of tumor necrosis factor alpha (TNF-alpha) in C3H/HeN macrophages. In C3H/HeJ macrophages, however, TNF-alpha was induced only by incubation with LPP. Both LPS and LPP induced tyrosine phosphorylation on proteins with apparent molecular masses of 39, 41, and 45 kD (p35, p41, and p45) in C3H/HeN macrophages, w

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Park, Young-Whan, Richard T. Cummings, Lin Wu, et al. "Homogeneous Proximity Tyrosine Kinase Assays: Scintillation Proximity Assay versus Homogeneous Time-Resolved Fluorescence." Analytical Biochemistry 269, no. 1 (1999): 94–104. http://dx.doi.org/10.1006/abio.1999.4029.

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Xue, Liang, Robert L. Geahlen, and W. Andy Tao. "Identification of Direct Tyrosine Kinase Substrates Based on Protein Kinase Assay-Linked Phosphoproteomics." Molecular & Cellular Proteomics 12, no. 10 (2013): 2969–80. http://dx.doi.org/10.1074/mcp.o113.027722.

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Naldini, L., E. Vigna, R. Ferracini, et al. "The tyrosine kinase encoded by the MET proto-oncogene is activated by autophosphorylation." Molecular and Cellular Biology 11, no. 4 (1991): 1793–803. http://dx.doi.org/10.1128/mcb.11.4.1793-1803.1991.

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Protein tyrosine kinases are crucially involved in the control of cell proliferation. Therefore, the regulation of their activity in both normal and neoplastic cells has been under intense scrutiny. The product of the MET oncogene is a transmembrane receptorlike tyrosine kinase with a unique disulfide-linked heterodimeric structure. Here we show that the tyrosine kinase activity of the MET-encoded protein is powerfully activated by tyrosine autophosphorylation. The enhancement of activity was quantitated with a phosphorylation assay of exogenous substrates. It involved an increase in the Vmax

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Naldini, L., E. Vigna, R. Ferracini, et al. "The tyrosine kinase encoded by the MET proto-oncogene is activated by autophosphorylation." Molecular and Cellular Biology 11, no. 4 (1991): 1793–803. http://dx.doi.org/10.1128/mcb.11.4.1793.

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Protein tyrosine kinases are crucially involved in the control of cell proliferation. Therefore, the regulation of their activity in both normal and neoplastic cells has been under intense scrutiny. The product of the MET oncogene is a transmembrane receptorlike tyrosine kinase with a unique disulfide-linked heterodimeric structure. Here we show that the tyrosine kinase activity of the MET-encoded protein is powerfully activated by tyrosine autophosphorylation. The enhancement of activity was quantitated with a phosphorylation assay of exogenous substrates. It involved an increase in the Vmax

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Ferrell, J. E., and G. S. Martin. "Identification of a 42-kilodalton phosphotyrosyl protein as a serine(threonine) protein kinase by renaturation." Molecular and Cellular Biology 10, no. 6 (1990): 3020–26. http://dx.doi.org/10.1128/mcb.10.6.3020-3026.1990.

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We have surveyed fibroblast lysates for protein kinases that might be involved in mitogenesis. The assay we have used exploits the ability of blotted, sodium dodecyl sulfate-denatured proteins to regain enzymatic activity after guanidine treatment. About 20 electrophoretically distinct protein kinases could be detected by this method in lysates from NIH 3T3 cells. One of the kinases, a 42-kilodalton serine(threonine) kinase (PK42), was found to possess two- to fourfold-higher in vitro activity when isolated from serum-stimulated cells than when isolated from serum-starved cells. This kinase co

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50

Ferrell, J. E., and G. S. Martin. "Identification of a 42-kilodalton phosphotyrosyl protein as a serine(threonine) protein kinase by renaturation." Molecular and Cellular Biology 10, no. 6 (1990): 3020–26. http://dx.doi.org/10.1128/mcb.10.6.3020.

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We have surveyed fibroblast lysates for protein kinases that might be involved in mitogenesis. The assay we have used exploits the ability of blotted, sodium dodecyl sulfate-denatured proteins to regain enzymatic activity after guanidine treatment. About 20 electrophoretically distinct protein kinases could be detected by this method in lysates from NIH 3T3 cells. One of the kinases, a 42-kilodalton serine(threonine) kinase (PK42), was found to possess two- to fourfold-higher in vitro activity when isolated from serum-stimulated cells than when isolated from serum-starved cells. This kinase co

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