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Journal articles on the topic 'P65BTK'

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Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Basile, Debora, Lorenzo Gerratana, Angela Buonadonna, Silvio Garattini, Tiziana Perin, Emanuela Grassilli, Gianmaria Miolo, et al. "Role of Bruton’s Tyrosine Kinase in Stage III Colorectal Cancer." Cancers 11, no. 6 (June 24, 2019): 880. http://dx.doi.org/10.3390/cancers11060880.

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Background: Bruton’s tyrosine kinase (BTK) is involved in the immune response and its deficiency impairs B cell maturation. We evaluated the expression of a novel BTK isoform, p65BTK, in colorectal cancer (CRC), to identify its impact on survival. Materials and Methods: This retrospective study evaluated 87 consecutive stage III CRC patients treated at the National Cancer Institute of Aviano (1999–2017). Multiple specimens were collected and analyzed for staining intensity and percentage of tumor cells positive for p65BTK. Prognostic impact was tested by univariate Cox regression analysis. Results: After a median follow-up of 82.59 months, median disease-free survival (DFS) and overall survival (OS) were 11.67 months and 31.33 months, respectively. Interestingly, 10% of patients did not express p65BTK. For the immunohistochemistry IHC intensity 1, the best cutoff point was 1% of p65BTK positivity; for IHC intensity 2, it was 50%; and for IHC intensity 3, it was 80%. Through univariate analysis, patients with highly expressed p65BTK (IHC intensity 3 and ≥80%) were shown to have the worst prognosis in terms of DFS (HR: 6.23; p = 0.005; 95% C.I. 1.75–22.79) and OS (HR: 2.54; p = 0.025; 95% C.I. 1.12–5.76). Conclusions: p65BTK is frequently expressed in CRC and, if highly expressed, is an unfavourable prognostic factor. However, further confirmation is needed and its potential targeting needs to be studied.

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2

Ianzano, L., S. Bonomo, A. Cialdella, F. Pisano, M. G. Cerrito, M. Carola, C. McLean, et al. "p65BTK targeting restores the apoptotic response to chemotherapy of p53-null drug-resistant colon cancer cells." European Journal of Cancer 69 (December 2016): S140. http://dx.doi.org/10.1016/s0959-8049(16)33016-7.

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3

Sorenson, Ann Marie, and Carl Grindstaff. "Adolescent Mothers: The Impact of Living Arrangements on Long-Term Economic Outcomes." Canadian Studies in Population 22, no. 2 (December 31, 1995): 91. http://dx.doi.org/10.25336/p6530k.

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4

Velaz-Faircloth, Maria, Alison J. Cobb, Amanda L. Horstman, Stanley C. Henry, and Richard Frothingham. "Protection against Mycobacterium aviumby DNA Vaccines Expressing Mycobacterial Antigens as Fusion Proteins with Green Fluorescent Protein." Infection and Immunity 67, no. 8 (August 1, 1999): 4243–50. http://dx.doi.org/10.1128/iai.67.8.4243-4250.1999.

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ABSTRACT Mycobacterium avium causes disseminated disease in humans with AIDS, paratuberculosis in ruminants, lymphadenopathy in swine, and tuberculosis in birds. We constructed DNA vaccines expressing mycobacterial antigens as fusion proteins with enhanced green fluorescent protein (EGFP). Plasmids p65K-EGFP, p85A-EGFP, and p85B-EGFP expressed the M. avium 65-kDa antigen, theMycobacterium bovis BCG 85A antigen, and the M. avium 85B antigen, respectively, as EGFP fusion proteins. We visualized protein expression directly in cultured murine fibroblasts and intact muscle. p65K-EGFP expressed fusion protein in a diffuse cytoplasmic pattern, and p85A-EGFP and p85B-EGFP produced a speckled pattern. We vaccinated C57BL/6 mice with three doses of plasmid DNA and then challenged them intraperitoneally with M. avium. Negative controls received saline, and positive controls received one dose of BCG vaccine. Mice in all groups developed disseminated infection with a high burden of organisms. Compared to negative controls, mice vaccinated with p85A-EGFP had an eightfold reduction in spleen M. avium CFU at 4 weeks after infection and a fourfold reduction at 8 weeks, reductions similar to those generated by BCG vaccine. Mice vaccinated with p65K-EGFP had a fourfold CFU reduction at 4 weeks and no effect at 8 weeks. This is the first report of DNA vaccines expressing foreign antigens as fusion proteins with EGFP and the first report of successful DNA vaccination againstM. avium.

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5

Espinosa, Lluı́s, Julia Inglés-Esteve, Alex Robert-Moreno, and Anna Bigas. "IκBα and p65 Regulate the Cytoplasmic Shuttling of Nuclear Corepressors: Cross-talk between Notch and NFκB Pathways." Molecular Biology of the Cell 14, no. 2 (February 2003): 491–502. http://dx.doi.org/10.1091/mbc.e02-07-0404.

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Notch and NFκB pathways are key regulators of numerous cellular events such as proliferation, differentiation, or apoptosis. In both pathways, association of effector proteins with nuclear corepressors is responsible for their negative regulation. We have previously described that expression of a p65-NFκB mutant that lacks the transactivation domain (p65ΔTA) induces cytoplasmic translocation of N-CoR leading to a positive regulation of different promoters. Now, we show that cytoplasmic sequestration of p65 by IκBα is sufficient to both translocate nuclear corepressors SMRT/N-CoR to the cytoplasm and upregulate transcription of Notch-dependent genes. Moreover, p65 and IκBα are able to directly bind SMRT, and this interaction can be inhibited in a dose-dependent manner by the CREB binding protein (CBP) coactivator and after TNF-α treatment, suggesting that p65 acetylation is modulating this interaction. In agreement with this, TNF-α treatment results in downregulation of the Hes1 gene. Finally, we present evidence on how this mechanism may influence cell differentiation in the 32D myeloid progenitor system.

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6

Daub, Henrik, Kris Gevaert, Joel Vandekerckhove, André Sobel, and Alan Hall. "Rac/Cdc42 and p65PAK Regulate the Microtubule-destabilizing Protein Stathmin through Phosphorylation at Serine 16." Journal of Biological Chemistry 276, no. 3 (October 31, 2000): 1677–80. http://dx.doi.org/10.1074/jbc.c000635200.

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7

Lamarche, Nathalie, Nicolas Tapon, Lisa Stowers, Peter D. Burbelo, Pontus Aspenström, Tina Bridges, John Chant, and Alan Hall. "Rac and Cdc42 Induce Actin Polymerization and G1 Cell Cycle Progression Independently of p65PAK and the JNK/SAPK MAP Kinase Cascade." Cell 87, no. 3 (November 1996): 519–29. http://dx.doi.org/10.1016/s0092-8674(00)81371-9.

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8

Tang, Y., Z. Chen, D. Ambrose, J. Liu, J. B. Gibbs, J. Chernoff, and J. Field. "Kinase-deficient Pak1 mutants inhibit Ras transformation of Rat-1 fibroblasts." Molecular and Cellular Biology 17, no. 8 (August 1997): 4454–64. http://dx.doi.org/10.1128/mcb.17.8.4454.

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Among the mechanisms by which the Ras oncogene induces cellular transformation, Ras activates the mitogen-activated protein kinase (MAPK or ERK) cascade and a related cascade leading to activation of Jun kinase (JNK or SAPK). JNK is additionally regulated by the Ras-related G proteins Rac and Cdc42. Ras also regulates the actin cytoskeleton through an incompletely elucidated Rac-dependent mechanism. A candidate for the physiological effector for both JNK and actin regulation by Rac and Cdc42 is the serine/threonine kinase Pak (p65pak). We show here that expression of a catalytically inactive mutant Pak, Pak1(R299), inhibits Ras transformation of Rat-1 fibroblasts but not of NIH 3T3 cells. Typically, 90 to 95% fewer transformed colonies were observed in cotransfection assays with Rat-1 cells. Pak1(R299) did not inhibit transformation by the Raf oncogene, indicating that inhibition was specific for Ras. Furthermore, Rat-1 cell lines expressing Pak1(R299) were highly resistant to Ras transformation, while cells expressing wild-type Pak1 were efficiently transformed by Ras. Pak1(L83,L86,R299), a mutant that fails to bind either Rac or Cdc42, also inhibited Ras transformation. Rac and Ras activation of JNK was inhibited by Pak1(R299) but not by Pak1(L83,L86,R299). Ras activation of ERK was inhibited by both Pak1(R299) and Pak1(L83,L86,R299), while neither mutant inhibited Raf activation of ERK. These results suggest that Pak1 interacts with components essential for Ras transformation and that inhibition can be uncoupled from JNK but not ERK signaling.

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9

Seko, Yoshinori, Naoyuki Takahashi, Kazuyuki Tobe, Takashi Kadowaki, and Yoshio Yazaki. "Hypoxia and Hypoxia/Reoxygenation Activate p65PAK, p38Mitogen-Activated Protein Kinase (MAPK), and Stress-Activated Protein Kinase (SAPK) in Cultured Rat Cardiac Myocytes." Biochemical and Biophysical Research Communications 239, no. 3 (October 1997): 840–44. http://dx.doi.org/10.1006/bbrc.1997.7570.

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10

Osada, Shin-ichi, Masaki Izawa, Tatsunobu Koyama, Syu-ichi Hirai, and Shigeo Ohno. "A domain containing the Cdc42/Rac interactive binding (CRIB) region of p65PAK inhibits transcriptional activation and cell transformation mediated by the Ras-Rac pathway." FEBS Letters 404, no. 2-3 (March 10, 1997): 227–33. http://dx.doi.org/10.1016/s0014-5793(97)00139-7.

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11

Tang, Yi, Jong Yu, and Jeffrey Field. "Signals from the Ras, Rac, and Rho GTPases Converge on the Pak Protein Kinase in Rat-1 Fibroblasts." Molecular and Cellular Biology 19, no. 3 (March 1, 1999): 1881–91. http://dx.doi.org/10.1128/mcb.19.3.1881.

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ABSTRACT Ras plays a key role in regulating cellular proliferation, differentiation, and transformation. Raf is the major effector of Ras in the Ras > Raf > Mek > extracellular signal-activated kinase (ERK) cascade. A second effector is phosphoinositide 3-OH kinase (PI 3-kinase), which, in turn, activates the small G protein Rac. Rac also has multiple effectors, one of which is the serine threonine kinase Pak (p65Pak). Here we show that Ras, but not Raf, activates Pak1 in cotransfection assays of Rat-1 cells but not NIH 3T3 cells. We tested agents that activate or block specific components downstream of Ras and demonstrate a Ras > PI 3-kinase > Rac/Cdc42 > Pak signal. Although these studies suggest that the signal from Ras through PI 3-kinase is sufficient to activate Pak, additional studies suggested that other effectors contribute to Pak activation. RasV12S35 and RasV12G37, two effector mutant proteins which fail to activate PI 3-kinase, did not activate Pak when tested alone but activated Pak when they were cotransfected. Similarly, RacV12H40, an effector mutant that does not bind Pak, and Rho both cooperated with Raf to activate Pak. A dominant negative Rho mutant also inhibited Ras activation of Pak. All combinations of Rac/Raf and Ras/Raf and Rho/Raf effector mutants that transform cells cooperatively stimulated ERK. Cooperation was Pak dependent, since all combinations were inhibited by kinase-deficient Pak mutants in both transformation assays and ERK activation assays. These data suggest that other Ras effectors can collaborate with PI 3-kinase and with each other to activate Pak. Furthermore, the strong correlation between Pak activation and cooperative transformation suggests that Pak activation is necessary, although not sufficient, for cooperative transformation of Rat-1 fibroblasts by Ras, Rac, and Rho.

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12

Marcus, S., A. Polverino, E. Chang, D. Robbins, M. H. Cobb, and M. H. Wigler. "Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe." Proceedings of the National Academy of Sciences 92, no. 13 (June 20, 1995): 6180–84. http://dx.doi.org/10.1073/pnas.92.13.6180.

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13

Grassilli, Emanuela, Maria Grazia Cerrito, Sara Bonomo, Roberto Giovannoni, Donatella Conconi, and Marialuisa Lavitrano. "p65BTK Is a Novel Biomarker and Therapeutic Target in Solid Tumors." Frontiers in Cell and Developmental Biology 9 (June 7, 2021). http://dx.doi.org/10.3389/fcell.2021.690365.

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Bruton’s tyrosine kinase (BTK) is a non-receptor intracellular kinase playing a key role in the proliferation and survival of normal and malignant B-lymphocytes. Its targeting by Ibrutinib, the first specific inhibitor, represented a turning point for the therapy of certain types of B-cell leukemias/lymphomas and several more BTK inhibitors are today in the clinic or advanced clinical trials. BTK expression was successively found to occur also outside of the hematopoietic compartment. In fact, we identified p65BTK, a novel 65 kDa isoform lacking an N-term stretch of 86 amino acids (compared to the 77 kDa protein expressed in B cells) as highly expressed in colon cancer patients. We demonstrated that p65BTK is a powerful oncogene acting downstream of the RAS/MAPK pathway and necessary for RAS-mediated transformation. Notably, the kinase domain is conserved and therefore inhibited by the available BTK-targeting drugs (Ibrutinib, Spebrutinib, etc.) which we used to demonstrate that p65BTK is an actionable target in drug-resistant colorectal carcinomas. We found p65BTK expressed also in >50% non-small cell lung cancers (NSCLC) and demonstrated that it is an actionable target in KRAS-mutated/EGFR-wild type drug-resistant NSCLC models (for which no targeted therapy is available). We also reported a significant correlation between p65BTK expression and low-grade tumors and overall survival of patients with grade III gliomas and showed that its targeting induced a significant decrease in the viability of in glioma stem cells. Finally, in ovarian cancer patients, p65BTK expression levels correlate with early relapse and shorter progression-free survival, both indicators of resistance to therapy. Remarkably, Ibrutinib is more effective than standard of care (SOC) therapeutics in in vitro and ex vivo settings. On the whole, our preclinical data indicate that, depending on the tumor type, BTK inhibitors used alone can induce cytotoxicity (gliomas), be more effective than SOC chemotherapy (ovarian cancer) or can kill drug-resistant tumor cells when used in combination with SOC chemotherapy (colon cancer and NSCLC) or targeted therapy (NSCLC and ovarian cancer), thus suggesting that p65BTK may be an actionable target in different solid tumors. In addition, our data also give the proof-of-concept for starting clinical trials using BTK inhibitors, alone or in combination, to improve the therapeutic options for solid tumors treatment.

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14

Sala, Luca, Giovanni Cirillo, Gabriele Riva, Gabriele Romano, Carlo Giussani, Annamaria Cialdella, Antonio Todisco, et al. "Specific Expression of a New Bruton Tyrosine Kinase Isoform (p65BTK) in the Glioblastoma Gemistocytic Histotype." Frontiers in Molecular Neuroscience 12 (January 24, 2019). http://dx.doi.org/10.3389/fnmol.2019.00002.

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15

Giordano, Federica, Valentina Vaira, Diego Cortinovis, Sara Bonomo, Joyce Goedmakers, Federica Brena, Annamaria Cialdella, et al. "p65BTK is a novel potential actionable target in KRAS-mutated/EGFR-wild type lung adenocarcinoma." Journal of Experimental & Clinical Cancer Research 38, no. 1 (June 14, 2019). http://dx.doi.org/10.1186/s13046-019-1199-7.

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