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Auteur : Grafiati
Publié le 11 mars 2023

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1

Jouhilahti, Eeva-Mari, Sirkku Peltonen et Juha Peltonen. « Class III β-Tubulin Is a Component of the Mitotic Spindle in Multiple Cell Types ». Journal of Histochemistry & ; Cytochemistry 56, no 12 (2 septembre 2008) : 1113–19. http://dx.doi.org/10.1369/jhc.2008.952002.

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The findings of this study show that Class III β-tubulin is a component of the mitotic spindle in multiple cell types. Class III β-tubulin has been widely used as a neuron-specific marker, but it has been detected also in association with breast and pancreatic cancers. In this study, we describe a novel finding of Class III β-tubulin in a subpopulation of cells in malignant peripheral nerve sheath tumor. The findings of this study also show that Class III β-tubulin is expressed by normal mesenchymal and epithelial cells (fibroblasts and keratinocytes), two transitional cell carcinoma cell lines, and neurofibroma Schwann cells, as shown by immunolabeling and Western transfer analysis using two different Tuj-1 antibodies that are specific for Class III β-tubulin. The corresponding mRNA was detected using RT-PCR and whole human genome microarrays. Both antibodies localized Class III β-tubulin to the mitotic spindle and showed a colocalization with α-tubulin. The immuno-reaction became visible in early prophase, and the most intense immunoreaction was detected during metaphase and anaphase when microtubules were connected to the kinetochores on chromosomes. Class III β-tubulin–specific immunoreaction lasted to the point when the midbody of cytokinesis became detectable.
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Reader, Jocelyn, Amy K. Harper, Teklu Legesse, Paul N. Staats, Olga Goloubeva, Gautam G. Rao, Amy Fulton et Dana M. Roque. « EP4 and Class III β-Tubulin Expression in Uterine Smooth Muscle Tumors : Implications for Prognosis and Treatment ». Cancers 11, no 10 (18 octobre 2019) : 1590. http://dx.doi.org/10.3390/cancers11101590.

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The microtubule-stabilizing agent docetaxel in combination with gemcitabine represents one of the most effective regimens against the aggressive gynecologic tumor leiomyosarcoma (LMS). Upregulation of class III β-tubulin has previously been shown to confer taxane resistance in a variety of human cancers. Prostaglandin E2 receptor EP4 is linked to progression of a variety of human cancers and may represent a novel target for tumor inhibition in LMS. We evaluated the hypotheses that EP4 and class III β-tubulin have increased expression in LMS in comparison to normal myometrium or benign tumors and that expression of class III β-tubulin correlates with resistance to taxanes and poor clinical outcome. Gene expression was examined using TCGA data and correlated with clinicopathologic outcome which demonstrated that class III β-tubulin is more highly expressed in more aggressive sarcomas with EP4 being widely expressed in all subtypes of sarcoma. Immunohistochemistry for EP4 and class III β-tubulin was performed on patients with LMS, leiomyomatosis/STUMP, leiomyoma, and normal myometrium. Expression of EP4 and class III β-tubulin were characterized for cell lines SK-UT-1, SK-UT-1B, and PHM-41 and these cell lines were treated with docetaxel alone and in combination with EP4 inhibitors. In taxane-resistant cell lines that overexpress class III β-tubulin and EP4, treatment with EP4 inhibitor resulted in at least 2-fold sensitization to docetaxel. Expression of class III β-tubulin and EP4 in LMS may identify patients at risk of resistance to standard chemotherapies and candidates for augmentation of therapy through EP4 inhibition.
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Laferrière, Nicole B., et D. L. Brown. « Effects of taxol on the polymerization and posttranslational modification of class III β-tubulin in P19 embryonal carcinoma cells ». Biochemistry and Cell Biology 73, no 9-10 (1 septembre 1995) : 687–94. http://dx.doi.org/10.1139/o95-076.

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Undifferentiated P19 embryonal carcinoma cells and P19 cells induced to differentiate along a neuronal pathway by 10−6 M retinoic acid were treated with taxol to examine the effects of this microtubule-stabilizing drug on the subcellular sorting of class III β-tubulin and on neurite outgrowth. P19 cells were grown on cover slips and then treated with taxol at concentrations of 10−6 to 10−9 M for 24 h. The microtubule cytoskeleton was examined after double-immunofluorescence labelling with a monoclonal antibody to α-tubulin (YOL 1/34) and a monoclonal neuron-specific class III β-tubulin antibody (TuJ1). Treatment of undifferentiated P19 cells with concentrations of taxol greater than 4 × 10−8 M caused microtubule bundling and multiple aster formation and promoted polymerization of the low levels of class III β-tubulin found in these cells. In neurons, at 2 × 10−8 M taxol, bundling of microtubules at the base of the neurite was apparent. At taxol concentrations greater than 1 × 10−7 M, enhanced assembly of class III β-tubulin was apparent, although long neurites were not observed. Using isoelectric focusing followed by western blotting, we detected an additional isoform of class III β-tubulin after treatment with 10−6 M taxol. These results indicate taxol treatment alters the normal subcellular sorting of tubulin isotypes, promotes the polymerization and posttranslational modification of class III β-tubulin, and interferes with neurite outgrowth.Key words: tubulin, taxol, microtubule, posttranslational modification, neurite outgrowth.
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Linhartová, I., P. Dráber, E. Dráberová et V. Viklický. « Immunological discrimination of β-tubulin isoforms in developing mouse brain. Post-translational modification of non-class-III β-tubulins ». Biochemical Journal 288, no 3 (15 décembre 1992) : 919–24. http://dx.doi.org/10.1042/bj2880919.

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Individual beta-tubulin isoforms in developing mouse brain were characterized using immunoblotting, after preceding high-resolution isoelectric focusing, with monoclonal antibodies against different structural regions of beta-tubulin. Some of the antibodies reacted with a limited number of tubulin isoforms in all stages of brain development and in HeLa cells. The epitope for the TU-14 antibody was located in the isotype-defining domain and was present on the beta-tubulin isotypes of classes I, II and IV, but absent on the neuron-specific class-III isotype. The data suggest that non-class-III beta-tubulins in mouse brain are substrates for developmentally regulated post-translational modifications and that beta-tubulins of non-neuronal cells are also post-translationally modified.
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Guo, Huiqin, Yu Zhao, Jiangyang Lu et Zejian Li. « ERCC1, class III β-tubulin, p53, and RRM1-tailored selection of personalized chemotherapy for stage IV NSCLC patients : A prospective study. » Journal of Clinical Oncology 30, no 15_suppl (20 mai 2012) : e18087-e18087. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.e18087.

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e18087 Background: ERCC1, class III β-tubulin, p53, and RRM1 are predictive molecular biomarkers of platinum agents, taxel, vinorelbine and gemcitabine respectively in personalized therapies of NSCLC. Tailored therapy with several of these markers suggested patient benefit was reported previously. But there was no report about prospective study involving all of these biomarkers. Here we report a prospective study that patients were treated with the personalized therapy tailored by these 4 markers to assess this new therapy approach. Methods: From Feb. 2009 to Feb. 2011, in our single group at the thoracic surgical department of PUMC hospital, we identified 48 patients with previously untreated stage IV NSCLC, ECOG PS of 0-2, and at least 2 of the 4 low expression level markers were eligible. The expression level of ERCC1, class III β-tubulin, p53, and RRM1 was assayed by immunohistochemical (IHC) staining with the tissue samples obtained from bronchoscopy biopsy, percutaneous lung biopsy or operation. Patients with low ERCC1/low class III β-tubulin expression received cisplatin/taxel, patients with high ERCC1/low class III β-tubulin expression received gemcitabine(with low RRM1 level) or vinorelbine (with low p53 level)/taxel, patients with low ERCC1/high class III β-tubulin expression received cisplatin/gemcitabine(low RRM1) or vinorelbine (low p53), and patients with high ERCC1/high class IIIβ-tubulin expression received gemcitabine/vinorelbine. A follow-up CT was performed after every 2 cycles chemotherapy and every 3 months after chemotherapy. PFS and OS were estimated by the Kaplan-Meier method. Results: Follow-up period was 35 months till Jan. 2012. 16(33.3%) patients died within follow-up period, 32(66.7%) patients are still alive. The overall response(CR+PR) rate is 85.4% with 10CR, 31 PR, 5 SD and 2 PD. Median PFS is 14 months and median OS was 27 months. And 1-year OS was 88.3% Conclusions: Our study suggest ERCC1, class III β-tubulin, p53, and RRM1-tailored selection of personalized chemotherapy of NSCLC could dramatically raise response rate and improve survival over standard chemotherapy. It might be a promising treatment option in the future..
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Zhang, Shucai, Qi Li, Quan Zhang, Jinghui Wang, Haiqing Zhang, Zongde Zhang, Qunhui Wang, Xinjie Yang, Yanfei Gu et Hui Zhang. « Expression of ERCC1 and Class III β-Tubulin in Resected Non-Small Cell Lung Cancer and its Correlation with Platinum-Based Adjuvant Chemotherapy ». International Journal of Biological Markers 25, no 3 (juillet 2010) : 141–49. http://dx.doi.org/10.1177/172460081002500304.

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Objective To explore the relationship between the expression of excision repair cross-complementation group 1 (ERCC1) and class III β-tubulin and the clinical characteristics and overall survival of patients with non-small cell lung cancer (NSCLC). Methods Immunohistochemical analysis was used to determine the protein expression of ERCC1 and class III β-tubulin in 160 completely resected NSCLC primary tumor samples, 50 of which were paired with adjacent normal tissue samples and another 40 benign lung lesion tissue samples as controls. Clinical data at baseline, disease-free survival and overall survival were also collected. Univariate and multivariate Cox models were used to analyze the risk factors. Results In 160 tumor samples, the ERCC1 and class III β-tubulin positive rates obtained with immunohistochemistry were 46.9% and 49.4%, respectively. Both biomarkers had a higher positive rate in male patients. For patients who did not receive adjuvant chemotherapy, ERCC1 positivity was associated with longer survival (median survival time 73 vs 53 months, p=0.041), while in patients treated with platinum chemotherapy, ERCC1 positivity tended to be associated with poor survival (median survival time 41 vs 54 months, p=0.014). Class III β-tubulin positivity was also associated with poor survival (median survival time 38 vs 58 months, p<0.001), but had no influence on the survival of patients who did not receive adjuvant chemotherapy. Conclusions ERCC1 and class III β-tubulin could be important survival predictors for completely resected NSCLC patients treated with adjuvant chemotherapy. Further prospective studies need to be performed to test this hypothesis in Chinese patients.
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Mariani, Marisa, Roshan Karki, Manuela Spennato, Deep Pandya, Shiquan He, Mirko Andreoli, Paul Fiedler et Cristiano Ferlini. « Class III β-tubulin in normal and cancer tissues ». Gene 563, no 2 (juin 2015) : 109–14. http://dx.doi.org/10.1016/j.gene.2015.03.061.

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Katsetos, Christos D., Mary M. Herman et Sverre J. Mörk. « Class III β-tubulin in human development and cancer ». Cell Motility and the Cytoskeleton 55, no 2 (24 avril 2003) : 77–96. http://dx.doi.org/10.1002/cm.10116.

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Alfano, Alan, Jin Xu, Xi Yang, Dhanraj Deshmukh et Yun Qiu. « SRC Kinase-Mediated Tyrosine Phosphorylation of TUBB3 Regulates Its Stability and Mitotic Spindle Dynamics in Prostate Cancer Cells ». Pharmaceutics 14, no 5 (25 avril 2022) : 932. http://dx.doi.org/10.3390/pharmaceutics14050932.

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Tubulin is an integral part of the cytoskeleton and plays a pivotal role in cellular signaling, maintenance, and division. β-tubulin is also the molecular target for taxane compounds such as docetaxel (DTX) and cabazitaxel (CTX), both first-line treatments for several solid cancers. Increased expression of Class III β-tubulin (TUBB3), a primarily neural isoform of β-tubulin, correlates with taxane resistance and poor prognosis. Although tyrosine kinase c-Src has been implicated to phosphorylate β-tubulins during both hematopoietic and neural differentiation, the mechanisms by which Src modulates tubulins functions are still poorly understood. Here, we report, for the first time, that TUBB3 is phosphorylated at Tyrosine 340 (Y340) by c-SRC in prostate cancer cells. We also showed that Y340 phosphorylation regulates TUBB3 protein stability and subcellular localization. Furthermore, we demonstrated that inhibition of SRC kinase activity compromises spindle stability in mitotic cells, at least partly due to the lack of TUBB3 Y340 phosphorylation. Given the importance of TUBB3 as a clinical biomarker of poor prognosis and drug resistance, characterization of TUBB3 posttranslational regulation could potentially serve as new biomarkers for disease recurrence and/or treatment failure.
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Alfano, Alan, Jin Xu, Xi Yang, Dhanraj Deshmukh et Yun Qiu. « SRC Kinase-Mediated Tyrosine Phosphorylation of TUBB3 Regulates Its Stability and Mitotic Spindle Dynamics in Prostate Cancer Cells ». Pharmaceutics 14, no 5 (25 avril 2022) : 932. http://dx.doi.org/10.3390/pharmaceutics14050932.

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Tubulin is an integral part of the cytoskeleton and plays a pivotal role in cellular signaling, maintenance, and division. β-tubulin is also the molecular target for taxane compounds such as docetaxel (DTX) and cabazitaxel (CTX), both first-line treatments for several solid cancers. Increased expression of Class III β-tubulin (TUBB3), a primarily neural isoform of β-tubulin, correlates with taxane resistance and poor prognosis. Although tyrosine kinase c-Src has been implicated to phosphorylate β-tubulins during both hematopoietic and neural differentiation, the mechanisms by which Src modulates tubulins functions are still poorly understood. Here, we report, for the first time, that TUBB3 is phosphorylated at Tyrosine 340 (Y340) by c-SRC in prostate cancer cells. We also showed that Y340 phosphorylation regulates TUBB3 protein stability and subcellular localization. Furthermore, we demonstrated that inhibition of SRC kinase activity compromises spindle stability in mitotic cells, at least partly due to the lack of TUBB3 Y340 phosphorylation. Given the importance of TUBB3 as a clinical biomarker of poor prognosis and drug resistance, characterization of TUBB3 posttranslational regulation could potentially serve as new biomarkers for disease recurrence and/or treatment failure.
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Cicchillitti, Lucia, Roberta Penci, Michela Di Michele, Flavia Filippetti, Domenico Rotilio, Maria Benedetta Donati, Giovanni Scambia et Cristiano Ferlini. « Proteomic characterization of cytoskeletal and mitochondrial class III β-tubulin ». Molecular Cancer Therapeutics 7, no 7 (juillet 2008) : 2070–79. http://dx.doi.org/10.1158/1535-7163.mct-07-2370.

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Sève, Pascal, et Charles Dumontet. « Is class III β-tubulin a predictive factor in patients receiving tubulin-binding agents ? » Lancet Oncology 9, no 2 (février 2008) : 168–75. http://dx.doi.org/10.1016/s1470-2045(08)70029-9.

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Don, Sima, Nicole M. Verrills, Tracy Y. E. Liaw, Marjorie L. M. Liu, Murray D. Norris, Michelle Haber et Maria Kavallaris. « Neuronal-associated microtubule proteins class III β-tubulin and MAP2c in neuroblastoma : Role in resistance to microtubule-targeted drugs ». Molecular Cancer Therapeutics 3, no 9 (1 septembre 2004) : 1137–46. http://dx.doi.org/10.1158/1535-7163.1137.3.9.

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Abstract Advanced stage neuroblastoma has a poor clinical outcome and microtubule-destabilizing agents, such as the Vinca alkaloids, are an important component in the treatment of this childhood cancer. Vinca alkaloids bind to β-tubulin on the α/β-tubulin heterodimer and disrupt microtubule dynamics, leading to cell death. To date, studies examining the contribution of microtubules and associated proteins to the efficacy of microtubule-destabilizing agents in neuroblastoma have been limited. In this study, BE(2)-C neuroblastoma cells previously selected for resistance to either vincristine (BE/VCR10) or colchicine (BE/CHCb0.2) were found to display significant decreases in neuronal-specific class III β-tubulin. Interestingly, vincristine-selected cells exhibited increased levels of polymerized tubulin that were not due to α-tubulin and class I, II, or III β-tubulin mutations. Expression levels of the microtubule-depolymerizing protein stathmin were significantly increased in BE/VCR10 cells. In contrast, levels of MAP2a and MAP2b were relatively unaltered. A marked decrease in the neuronal protein, MAP2c, was identified in the vincristine-selected cells and, to a lesser extent, in the colchicine-selected cells. This is the first report describing specific microtubule alterations in neuroblastoma cells resistant to tubulin-targeted agents. The results indicate a need to identify the factors responsible for resistance to tubulin-targeted agents in neuroblastoma so that improved and novel treatment strategies can be developed for this drug refractory disease.
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Namal, Esat, Mustafa Bozkurt, Akin Ozturk, Kezban Nur Planci, Nuray Bassullu, Ozgul Pamukcu, Gulen Bulbul Dogusoy, Sezer Saglam, Zafer Akcali et Gokhan Demir. « Biologic markers guiding the treatment of non-small cell lung cancer : RRM-1, class III ß tubulin, and ERCC-1. » Journal of Clinical Oncology 31, no 15_suppl (20 mai 2013) : e19127-e19127. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.e19127.

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e19127 Background: Lung cancer is the most common cause of cancer deaths in the world. Despite the developments in diagnosis and treatment, the high mortality rate in metastatic non small cell lung cancer (NSCLC) is still an important problem. Recent non-targeted standard therapy for NSCLC is the dual therapy regimens which involve platins. Our former knowledge whether these therapies can be effective or not would save the patient from the redundant toxicity and provide us to use more effective drugs formerly. Understanding the biology of NSCLC can allow choosing the effective and appropriate therapy in terms of life quality, survival rate and relapses. There are ongoing studies upon prognostic and predictive values of ERCC1, RRM1 and β tubulin in NSCLC patients. In this study we aimed to investigate the role of β tubulin, ERCC1 and RRM1 expressions as predictive biomarkers. Methods: 47 patients who are on follow up by Bilim University, Medical Oncology Department, were taken to the study. ß tubulin, ERCC1 and RRM1 over expressions were investigated in the biopsy materials of these patients by Pathology Department. Retrospectively, it was evaluated whether there is correlation between these biological markers and patients’ survial rates and responses to antineoplastic therapies. Results: In the literature, there are some studies which show that β tubulin score is a predictive marker for the good response to taxan therapy. On the other hand, it was shown that taxans enhance the platin sensitivity decreasing the β tubulin expressions. Our study was also correlated with these studies in the literature. Furthermore, there was relationship between the β tubulin score and age. 15 patients (%32) were 65 or under 65 and these were accepted as ‘young patient population’; 32 patients were over 65 and were accepted as ‘old patient population’. Most of the patients whose β tubulin score was high (n=29), were young (n=19); and most of the patients whose β tubulin score was low (n=18) were old patients (n=12) (p=0.032). Conclusions: Detecting the levels of β tubulin, ERCC1 and RRM1 before treatment in NSCLC patients, can be predictive to organize the treatment. Unquestionably, it must be supported by the studies involve more patients.
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Katsetos, Christos D., Eduarda Dráberová, Agustin Legido, Charles Dumontet et Pavel Dráber. « Tubulin targets in the pathobiology and therapy of glioblastoma multiforme. I. class III β-tubulin ». Journal of Cellular Physiology 221, no 3 (31 juillet 2009) : 505–13. http://dx.doi.org/10.1002/jcp.21870.

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Katsetos, Christos D., Luis Del Valle, Jennian F. Geddes, Martha Assimakopoulou, Agustin Legido, James C. Boyd, Brian Balin et al. « Aberrant Localization of the Neuronal Class III β-Tubulin in Astrocytomas ». Archives of Pathology & ; Laboratory Medicine 125, no 5 (1 mai 2001) : 613–24. http://dx.doi.org/10.5858/2001-125-0613-alotnc.

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Abstract Background.—The class III β-tubulin isotype (βIII) is widely regarded as a neuronal marker in development and neoplasia. In previous work, we have shown that the expression of βIII in neuronal/neuroblastic tumors is differentiation dependent. In contrast, the aberrant localization of this isotype in certain nonneuronal neoplasms, such as epithelial neuroendocrine lung tumors, is associated with anaplastic potential. Objective.—To test the generality of this observation, we investigated the immunoreactivity profile of βIII in astrocytomas. Design.—Sixty archival, surgically excised astrocytomas (8 pilocytic astrocytomas, WHO grade 1; 18 diffuse fibrillary astrocytomas, WHO grade 2; 4 anaplastic astrocytomas, WHO grade 3; and 30 glioblastomas, WHO grade 4), were studied by immunohistochemistry using anti-βIII monoclonal (TuJ1) and polyclonal antibodies. A monoclonal antibody to Ki-67 nuclear antigen (NC-MM1) was used as a marker for cell proliferation. Antibodies to glial fibrillary acidic protein (GFAP) and BM89 synaptic vesicle antigen/synaptophysin were used as glial and neuronal markers, respectively. Results.—The βIII immunoreactivity was significantly greater in high-grade astrocytomas (anaplastic astrocytomas and glioblastomas; median labeling index [MLI], 35%; interquartile range [IQR], 20%–47%) as compared with diffuse fibrillary astrocytomas (MLI, 4%; IQR, 0.2%–21%) (P &lt; .0001) and was rarely detectable in pilocytic astrocytomas (MLI, 0%; IQR, 0%–0.5%) (P &lt; .0001 vs high-grade astrocytomas; P &lt; .01 vs diffuse fibrillary astrocytomas). A highly significant, grade-dependent relationship was observed between βIII and Ki-67 labeling and malignancy, but this association was stronger for Ki-67 than for βIII (βIII, P &lt; .006; Ki-67, P &lt; .0001). There was co-localization of βIII and GFAP in neoplastic astrocytes, but no BM89 synaptic vesicle antigen/synaptophysin staining was detected. Conclusions.—In the context of astrocytic gliomas, βIII immunoreactivity is associated with an ascending gradient of malignancy and thus may be a useful ancillary diagnostic marker. However, the significance of βIII-positive phenotypes in diffuse fibrillary astrocytomas with respect to prognostic and predictive value requires further evaluation. Under certain neoplastic conditions, βIII expression is not neuron specific, calling for a cautious interpretation of βIII-positive phenotypes in brain tumors.
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Katsetos, Christos D., George Kontogeorgos, Jennian F. Geddes, Mary M. Herman, Hera Tsimara-Papastamatiou, Yunxia Yu, Lazaros I. Sakkas et al. « Differential Distribution of the Neuron-Associated Class III β-Tubulin in Neuroendocrine Lung Tumors ». Archives of Pathology & ; Laboratory Medicine 124, no 4 (1 avril 2000) : 535–44. http://dx.doi.org/10.5858/2000-124-0535-ddotna.

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AbstractObjective.—To study the immunoreactivity profile of the neuron-associated class III β-tubulin isotype (β III) in epithelial lung tumors.Design.—One hundred four formalin-fixed, paraffin-embedded primary and metastatic lung cancer specimens were immunostained with an anti–β III mouse monoclonal antibody (TuJ1) and an anti–β III affinity-purified rabbit antiserum. Paraffin sections from fetal, infantile, and adult nonneoplastic lung tissues were also examined.Results.—In the fetal airway epithelium, β III staining is detected transiently in rare Kulchitsky-like cells from lung tissues corresponding to the pseudoglandular and canalicular but not the saccular or alveolar stages of development. β III is absent in healthy, hyperplastic, metaplastic, and dysplastic airway epithelium of the adult lung. In contrast, β III is highly expressed in small cell lung cancer, large cell neuroendocrine carcinoma, and in some non–small cell lung cancers, particularly adenocarcinomas. There is no correlation between expression of β III and generic neuroendocrine markers, such as chromogranin A and/or synaptophysin, in pulmonary adenocarcinomas. Also, focal β III staining is present in primary and metastatic adenocarcinomas (to the lung) originating in the colon, prostate, and ovary. β III is expressed to a much lesser extent in atypical carcinoids and is rarely detectable in typical carcinoids and squamous cell carcinomas of the lung. The distribution of β III in small cell lung cancer and adenocarcinoma metastases to regional lymph nodes and brain approaches 100% of tumor cells, which is substantially greater than in the primary tumors.Conclusions.—In the context of neuroendocrine lung tumors, β III immunoreactivity is a molecular signature of high-grade malignant neoplasms (small cell lung cancer and large cell neuroendocrine carcinoma) although its importance in atypical carcinoids must be evaluated further. In addition, β III may be a useful diagnostic marker in distinguishing between small cell lung cancers and certain non–small cell lung cancers (poorly differentiated squamous cell carcinomas), especially in small biopsy specimens. To our knowledge, β III is the only tumor biomarker that exhibits a substantially more widespread distribution in poorly differentiated than in better differentiated pulmonary neuroendocrine tumors. However, the significance of β III phenotypes in non–small cell lung cancer, particularly adenocarcinoma, with respect to neuroendocrine differentiation and prognostic value, requires further evaluation.
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Karkavelas, George, Christos D. Katsetos, Jennian F. Geddes, Mary M. Herman, Stanley A. Vinores, Harry S. Cooper, Javier Provencio et Anthony Frankfurter. « Class III β-Tubulin isotype (β III) in the adrenal medulla : II. Localization in primary human pheochromocytomas ». Anatomical Record 250, no 3 (mars 1998) : 344–50. http://dx.doi.org/10.1002/(sici)1097-0185(199803)250:3<344 ::aid-ar9>3.0.co;2-#.

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Sharma, Rajesh K., et Peter A. Netland. « Early born lineage of retinal neurons express class III β-tubulin isotype ». Brain Research 1176 (octobre 2007) : 11–17. http://dx.doi.org/10.1016/j.brainres.2007.07.090.

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Škoda, D., K. Kranda, M. Bojar, L. Glosová, J. Bäurle, J. Kenney, D. Romportl, M. Pelichovská et K. Cvachovec. « Antibody formation against β-tubulin class III in response to brain trauma ». Brain Research Bulletin 68, no 4 (janvier 2006) : 213–16. http://dx.doi.org/10.1016/j.brainresbull.2005.05.032.

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POWELL, STEVEN, ALEX KAIZER, JOSEPH S. KOOPMEINERS, CARLOS IWAMOTO et MARK KLEIN. « High expression of class III β-tubulin in small cell lung carcinoma ». Oncology Letters 7, no 2 (6 décembre 2013) : 405–10. http://dx.doi.org/10.3892/ol.2013.1734.

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Giordana, M. T., P. Cavalla, A. Dutto et D. Schiffer. « CLASS III β-TUBULIN AND CALBINDIN IN MEDULLOBLASTOMA OF CHILDREN AND ADULTS ». Journal of Neuropathology and Experimental Neurology 55, no 5 (mai 1996) : 625. http://dx.doi.org/10.1097/00005072-199605000-00093.

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Liu, Li, Eldon E. Geisert, Anthony Frankfurter, Anthony J. Spano, Chloe Xue Jiang, Junming Yue, Ioannis Dragatsis et Dan Goldowitz. « A transgenic mouse Class-III β tubulin reporter using yellow fluorescent protein ». genesis 45, no 9 (septembre 2007) : 560–69. http://dx.doi.org/10.1002/dvg.20325.

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Locher, Heiko, Karien E. de Rooij, John C. M. J. de Groot, Remco van Doorn, Nelleke A. Gruis, Clemens W. G. M. Löwik, Susana M. Chuva de Sousa Lopes, Johan H. M. Frijns et Margriet A. Huisman. « Class III β-tubulin, a novel biomarker in the human melanocyte lineage ». Differentiation 85, no 4-5 (avril 2013) : 173–81. http://dx.doi.org/10.1016/j.diff.2013.05.003.

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Woulfe, J. « Class III β-tubulin immunoreactive intranuclear inclusions in human ependymomas and gangliogliomas ». Acta Neuropathologica 100, no 4 (28 octobre 2000) : 427–34. http://dx.doi.org/10.1007/s004010000191.

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Locher, H., N. Saadah, S. de Groot, J. C. M. J. de Groot, J. H. M. Frijns et M. A. Huisman. « Hair follicle bulge cultures yield class III β-tubulin-positive melanoglial cells ». Histochemistry and Cell Biology 144, no 1 (28 février 2015) : 87–91. http://dx.doi.org/10.1007/s00418-015-1312-8.

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Katsetos, Christos D., Eduarda Dráberová, Barbora Šmejkalová, Goutham Reddy, Louise Bertrand, Jean-Pierre de Chadarévian, Agustin Legido, Jonathan Nissanov, Peter W. Baas et Pavel Dráber. « Class III β-Tubulin and γ-Tubulin are Co-expressed and Form Complexes in Human Glioblastoma Cells ». Neurochemical Research 32, no 8 (4 avril 2007) : 1387–98. http://dx.doi.org/10.1007/s11064-007-9321-1.

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Katsetos, Christos D., George Karkavelas, Mary M. Herman, Stanley A. Vinores, Javier Provencio, Anthony J. Spano et Anthony Frankfurter. « Class III β-Tubulin isotype (β III) in the adrenal medulla : I. Localization in the developing human adrenal medulla ». Anatomical Record 250, no 3 (mars 1998) : 335–43. http://dx.doi.org/10.1002/(sici)1097-0185(199803)250:3<335 ::aid-ar8>3.0.co;2-z.

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Ganguly, Anutosh, Hailing Yang et Fernando Cabral. « Class III β-Tubulin Counteracts the Ability of Paclitaxel to Inhibit Cell Migration ». Oncotarget 2, no 5 (16 mai 2011) : 368–77. http://dx.doi.org/10.18632/oncotarget.250.

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Oshima, Shohei, et Yasutaka Yawaka. « Class III β-tubulin expression during hard tissue formation in developing mouse teeth ». Pediatric Dental Journal 30, no 1 (avril 2020) : 9–16. http://dx.doi.org/10.1016/j.pdj.2019.12.002.

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Stapor, Peter C., et Walter L. Murfee. « Identification of class III β-tubulin as a marker of angiogenic perivascular cells ». Microvascular Research 83, no 2 (mars 2012) : 257–62. http://dx.doi.org/10.1016/j.mvr.2011.09.003.

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Kang, Jun, et Inchul Lee. « TuJ1 (class III β-tubulin) as phenotypic marker of lymphatic and venous valves ». Cardiovascular Pathology 15, no 4 (juillet 2006) : 218–21. http://dx.doi.org/10.1016/j.carpath.2006.04.001.

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Terry, S., G. Ploussard, Y. Allory, N. Nicolaiew, F. Boissière-Michot, P. Maillé, L. Kheuang et al. « Increased expression of class III β-tubulin in castration-resistant human prostate cancer ». British Journal of Cancer 101, no 6 (18 août 2009) : 951–56. http://dx.doi.org/10.1038/sj.bjc.6605245.

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Stengel, C., S. P. Newman, M. P. Leese, B. V. L. Potter, M. J. Reed et A. Purohit. « Class III β-tubulin expression and in vitro resistance to microtubule targeting agents ». British Journal of Cancer 102, no 2 (22 décembre 2009) : 316–24. http://dx.doi.org/10.1038/sj.bjc.6605489.

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Kavallaris, M., C. A. Burkhart et S. B. Horwitz. « Antisense oligonucleotides to class III β-tubulin sensitize drug-resistant cells to Taxol ». British Journal of Cancer 80, no 7 (7 mai 1999) : 1020–25. http://dx.doi.org/10.1038/sj.bjc.6690507.

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Ferreira, Adriana, et A. Caceres. « Expression of the Class III β-tubulin isotype in developing neurons in culture ». Journal of Neuroscience Research 32, no 4 (août 1992) : 516–29. http://dx.doi.org/10.1002/jnr.490320407.

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Altonsy, Mohammed O., Anutosh Ganguly, Matthias Amrein, Philip Surmanowicz, Shu Shun Li, Gilles J. Lauzon et P. Régine Mydlarski. « Beta3-Tubulin Is Critical for Microtubule Dynamics, Cell Cycle Regulation, and Spontaneous Release of Microvesicles in Human Malignant Melanoma Cells (A375) ». International Journal of Molecular Sciences 21, no 5 (28 février 2020) : 1656. http://dx.doi.org/10.3390/ijms21051656.

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Microtubules (MTs), microfilaments, and intermediate filaments, the main constituents of the cytoskeleton, undergo continuous structural changes (metamorphosis), which are central to cellular growth, division, and release of microvesicles (MVs). Altered MTs dynamics, uncontrolled proliferation, and increased production of MVs are hallmarks of carcinogenesis. Class III beta-tubulin (β3-tubulin), one of seven β-tubulin isotypes, is a primary component of MT, which correlates with enhanced neoplastic cell survival, metastasis and resistance to chemotherapy. We studied the effects of β3-tubulin gene silencing on MTs dynamics, cell cycle, and MVs release in human malignant melanoma cells (A375). The knockdown of β3-tubulin induced G2/M cell cycle arrest, impaired MTs dynamics, and reduced spontaneous MVs release. Additional studies are therefore required to elucidate the pathophysiologic and therapeutic role of β3-tubulin in melanoma.
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Guo, Huiqin, Yu Zhao, Jiangyang Lu, David C. Christiani, Xihong Lin et Zhaoxi Wang. « Extensive surgical resection in stage IV non-small cell lung cancer patients after tailored chemotherapy. » Journal of Clinical Oncology 31, no 15_suppl (20 mai 2013) : e19080-e19080. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.e19080.

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e19080 Background: The treatment of stage IV non-small cell lung cancer patients is a problem for thoracic surgeons and the optimal treatment is discussed controversially. ERCC1, class III β-tubulin, p53, and RRM1 are predictive molecular biomarkers reported for neoadjuvant chemotherapy. Here we report a prospectively enrolled case series that patients were treated with extensive surgical resection after personalized chemotherapy tailored by these 4 markers. Methods: Patients with previously untreated stage IV NSCLC, ECOG PS of 0-2 were enrolled. The expression of ERCC1, class III β-tubulin, p53, and RRM1 was tested with IHC staining method for the tumor samples by bronchoscopy biopsy or percutaneous lung biopsy. Patients were treated with 2 of four drugs including cisplatin, taxol, gemcitabine and vinorelbine, selected by the expression of ERCC1, class III β-tubulin, RRM1 and p53, respectively. Then patients received surgical resection after evaluation with continuing adjuvant chemotherapy. A follow-up CT was performed after every 2 cycles chemotherapy and every 3 months post chemotherapy. PFS and OS were estimated by the Kaplan-Meier method. Results: 26 patients were included from May 2008 to Dec 2011 with a follow-up period 12–58 months till Nov 2011. 8 (30.8%) patients died within Follow-up period. The overall response (CR+PR) rate of tailored neoadjuvant chemotherapy was 88.5% with 23 PR. A complete resection (R0) was achieved in 24 (92.3%) patients and R1 in 2 (7.7%) patients. Median PFS was 27.0 months (95% CI: 21.0–32.9 months) and median OS was 41.6 months (95% CI: 23.1–60.0 months). Conclusions: Our study suggest extensive surgical resection in stage IV non-small cell lung cancer patients after tailored chemotherapy should be performed because it may improve survival dramatically over conservative chemotherapy. Surgery within multimodality approach will be a promise treatment option in the future.
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Pêknicová, Jana, Alena Kubátová, Vadym Sulimenko, Eduarda Dráberová, Vladimír Viklický, Pavel Hozák et Pavel Dráber. « Differential Subcellular Distribution of Tubulin Epitopes in Boar Spermatozoa : Recognition of Class III β-Tubulin Epitope in Sperm Tail1 ». Biology of Reproduction 65, no 3 (1 septembre 2001) : 672–79. http://dx.doi.org/10.1095/biolreprod65.3.672.

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Martinelli, Enrica, Andrea Fattorossi, Alessandra Battaglia, Marco Petrillo, Giuseppina Raspaglio, Gian Franco Zannoni, Mara Fanelli, Daniela Gallo et Giovanni Scambia. « Preoperative Anti-Class III β-Tubulin Antibodies As Relevant Clinical Biomarkers in Ovarian Cancer ». Translational Oncology 11, no 2 (avril 2018) : 358–65. http://dx.doi.org/10.1016/j.tranon.2018.01.016.

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Yahiro, Kenichiro, Yoshihiro Matsumoto, Jun-ichi Fukushi, Ken-ichi Kawaguchi, Makoto Endo, Nokitaka Setsu, Keiichiro IIda et al. « Class III β-Tubulin Overexpression Induces Chemoresistance to Eribulin in a Leiomyosarcoma Cell Line ». Analytical Cellular Pathology 2018 (21 juin 2018) : 1–11. http://dx.doi.org/10.1155/2018/8987568.

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Eribulin is a new drug to treat soft tissue sarcoma (STS) that exerts antitumor activity by binding to microtubules. The prognosis of STS is poor, and eribulin is expected to improve the treatment outcome. We observed several cases that exhibited resistance to eribulin and developed an eribulin-resistant leiomyosarcoma cell line to investigate the mechanism of resistance. The IC50 of eribulin was 125 times higher in the resistant cell line than in the parental cell line, and eribulin did not induce G2/M arrest in resistant cells. The resistant cell line showed increased expression of MDR1 transcript, but protein levels and functional analysis results were similar to the parental cell line. We found that class III β-tubulin (TUBB3) was overexpressed in the resistant cell line, and siRNA knockdown of TUBB3 partially recovered sensitivity to eribulin. TUBB3 expression in clinical samples varied, suggesting that TUBB3 has the potential to be a biomarker for selection of anticancer drugs and may be a target for overcoming resistance to eribulin.
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Linhartová, Irena, Eduarda Dráberová, Vladimír Viklický et Pavel Dráber. « Distribution of non-class-III β-tubulin isoforms in neuronal and non-neuronal cells ». FEBS Letters 320, no 1 (29 mars 1993) : 79–82. http://dx.doi.org/10.1016/0014-5793(93)81662-j.

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De Donato, Marta, Marisa Mariani, Lella Petrella, Enrica Martinelli, Gian Franco Zannoni, Valerio Vellone, Gabriella Ferrandina, Shohreh Shahabi, Giovanni Scambia et Cristiano Ferlini. « Class III β-tubulin and the cytoskeletal gateway for drug resistance in ovarian cancer ». Journal of Cellular Physiology 227, no 3 (22 décembre 2011) : 1034–41. http://dx.doi.org/10.1002/jcp.22813.

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Zhao, Xiaoli, Changli Yue, Jiamin Chen, Cheng Tian, Dongmei Yang, Li Xing, Honggang Liu et Yulan Jin. « Class III β-Tubulin in Colorectal Cancer : Tissue Distribution and Clinical Analysis of Chinese Patients ». Medical Science Monitor 22 (23 octobre 2016) : 3915–24. http://dx.doi.org/10.12659/msm.901252.

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Gan, Pei Pei, Eddy Pasquier et Maria Kavallaris. « Class III β-Tubulin Mediates Sensitivity to Chemotherapeutic Drugs in Non–Small Cell Lung Cancer ». Cancer Research 67, no 19 (1 octobre 2007) : 9356–63. http://dx.doi.org/10.1158/0008-5472.can-07-0509.

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Hisaoka, Masanori, Sumika Okamoto, Shune Koyama, Tsuyoshi Ishida, Tetsuo Imamura, Hiroaki Kanda, Toru Kameya, Jeanne M. Meis-Kindblom, Lars-Gunnar Kindblom et Hiroshi Hashimoto. « Microtubule-Associated Protein-2 and Class III β-Tubulin Are Expressed in Extraskeletal Myxoid Chondrosarcoma ». Modern Pathology 16, no 5 (mai 2003) : 453–59. http://dx.doi.org/10.1097/01.mp.0000067422.61241.64.

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Mhaidat, Nizar M., Rick F. Thorne, Charles Edo de Bock, Xu Dong Zhang et Peter Hersey. « Melanoma cell sensitivity to Docetaxel-induced apoptosis is determined by class III β-tubulin levels ». FEBS Letters 582, no 2 (18 décembre 2007) : 267–72. http://dx.doi.org/10.1016/j.febslet.2007.12.014.

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Yang, Liang, Zhi-Fei Wang, Hao Wu et Wei Wang. « miR-142-5p Improves Neural Differentiation and Proliferation of Adipose-Derived Stem Cells ». Cellular Physiology and Biochemistry 50, no 6 (2018) : 2097–107. http://dx.doi.org/10.1159/000495054.

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Background/Aims: MiRNAs may regulate neurogenic differentiation of adipose-derived stem cells (ADSCs). In this study, we hypothesized that the miR-142-5p can repress the expression of RhoA/ROCK1 pathway on the neurogenesis of ADSCs. Methods: Deregulated miRNA during neurogenic differentiation of ADSCs were identified. The expression of neuron-specific enolase (NSE) and β III tubulin (Neuron-specific class III beta-tubulin) were detected as the markers of neurogenic differentiation by immunostaining and western blot. The targeting of miR-142-5p on RhoA and ROCK1 was verified by dual luciferase assay, qRT-PCR and western blot. The roles of miR-142-5p and the RhoA/ROCK1 signaling pathway were explored by using functional experiments including cell viability and colony formation assays. Results: MiR-142-5p is significantly upregulated during neurogenic differentiation of ADSCs. Knockdown of endogenous miR-142-5p hampered neurogenic differentiation. MiR-142-5p could directly target RhoA and ROCK1 mRNA and repress their expressions, through which it increased the proportion of differentiated cells with positive NSE and β III tubulin. RhoA/ROCK1 signaling pathway is involved in miR-142-5p effect on the process of neurogenic differentiation of ADSCs. Conclusion: Our results demonstrate that miR-142-5p functions as a growth promotive miRNA and plays an important role in neurogenic differentiation by targeting RhoA/ROCK1 in ADSCs.
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Martinez-Diaz, Hilda, B. K. Kleinschmidt-DeMasters, Suzanne Z. Powell et Anthony T. Yachnis. « Giant Cell Glioblastoma and Pleomorphic Xanthoastrocytoma Show Different Immunohistochemical Profiles for Neuronal Antigens and p53 but Share Reactivity for Class III β-Tubulin ». Archives of Pathology & ; Laboratory Medicine 127, no 9 (1 septembre 2003) : 1187–91. http://dx.doi.org/10.5858/2003-127-1187-gcgapx.

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Abstract Context.—Giant cell glioblastoma multiforme (GCGBM) and pleomorphic xanthoastrocytoma (PXA) are clinically, radiographically, and histologically distinct tumors of the central nervous system. However, they share features of gross circumscription, reticulin deposition, lymphocytic infiltrates, and prominent populations of tumor giant cells. Neuronal antigens have been detected in the neoplastic cells of PXAs, but to our knowledge have not been studied previously in GCGBMs. While TP53 is mutated in most GCGBMs, a feature usually paralleled by strong immunostaining of the protein, the expression pattern of PXAs has not been extensively studied. Objectives.—To compare the immunoprofiles of GCGBM and PXA with regard to neuronal antigens and p53 and to evaluate the potential diagnostic utility of such a panel. Design.—Archival paraffin sections of 9 GCGBMs and 9 PXAs were immunostained for class III β-tubulin, neuronal nuclear antigen, neurofilament protein, synaptophysin, glial fibrillary acidic protein, and p53. Results.—Giant cell glioblastomas were strongly immunoreactive for class III β-tubulin and glial fibrillary acidic protein, but showed only rare staining for the other neuronal polypeptides. In contrast, PXAs usually showed at least focal staining of individual tumor cells for most of the neuronal antigens tested. Tubulin was strongly positive in tumor giant cells and in smaller neoplastic cells of both tumor types. Double-immunolabeling revealed distinct populations of tumor cells that expressed either glial fibrillary acidic protein or tubulin and dual-labeling of individual cells in GCGBM and PXA. Strong p53 staining was observed in many tumor cells in 5 of 8 GCGBMs tested, while staining for this antigen was negative or focally positive in 6 of 8 PXAs examined. Conclusions.—Giant cell glioblastoma multiforme and PXA show distinct patterns of immunoreactivity for neuronal antigens and p53 that may be useful diagnostically in difficult cases or in limited samples. These results provide further evidence of neuronal antigen expression by PXA.
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ÖZTOP, SIDIKA, AYNUR IŞIK, GÜNEŞ GÜNER, HAKAN GÜRDAL, ERDEM KARABULUT, ERKAN YILMAZ et AYTEKİN AKYOL. « Class III β-tubulin Expression in Colorectal Neoplasms Is a Potential Predictive Biomarker for Paclitaxel Response ». Anticancer Research 39, no 2 (février 2019) : 655–62. http://dx.doi.org/10.21873/anticanres.13160.

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