scholarly journals αTubulin 67C and Ncd Are Essential for Establishing a Cortical Microtubular Network and Formation of the Bicoid mRNA Gradient in Drosophila

PLoS ONE ◽  
2014 ◽  
Vol 9 (11) ◽  
pp. e112053 ◽  
Author(s):  
Khalid Fahmy ◽  
Mira Akber ◽  
Xiaoli Cai ◽  
Aabid Koul ◽  
Awais Hayder ◽  
...  
Keyword(s):  
Microtubular Network

scholarly journals Involvement of Microtubular Network and Its Motors in Productive Endocytic Trafficking of Mouse Polyomavirus

PLoS ONE ◽  
2014 ◽  
Vol 9 (5) ◽  
pp. e96922 ◽  
Author(s):  
Vojtech Zila ◽  
Francesco Difato ◽  
Lucie Klimova ◽  
Sandra Huerfano ◽  
Jitka Forstova
Keyword(s):  
Endocytic Trafficking ◽  
Microtubular Network

Study of possible interactions of tubulin, microtubular network, and STOP protein with mitochondria in muscle cells

2009 ◽  
Vol 337 (1-2) ◽  
pp. 239-249 ◽  
Author(s):  
Karen Guerrero ◽  
Claire Monge ◽  
Anna Brückner ◽  
Ülo Puurand ◽  
Lumme Kadaja ◽  
...  
Keyword(s):  
Muscle Cells ◽  
Microtubular Network

scholarly journals Microtubules regulate cardiomyocyte transversal Young’s modulus

2020 ◽  
Vol 117 (6) ◽  
pp. 2764-2766 ◽  
Author(s):  
Pamela Swiatlowska ◽  
Jose L. Sanchez-Alonso ◽  
Peter T. Wright ◽  
Pavel Novak ◽  
Julia Gorelik
Keyword(s):  
Young’S Modulus ◽  
Mechanical Loading ◽  
Posttranslational Modifications ◽  
Young's Modulus ◽  
Cardiac Mechanics ◽  
Ion Conductance ◽  
Loading And Unloading ◽  
Microtubular Network ◽  
Significant Attention

The field of cardiomyocyte mechanobiology is gaining significant attention, due to accumulating evidence concerning the significant role of cellular mechanical effects on the integrated function of the heart. To date, the protein titin has been demonstrated as a major contributor to the cardiomyocytes Young’s modulus (YM). The microtubular network represents another potential regulator of cardiac mechanics. However, the contribution of microtubules (MTs) to the membrane YM is still understudied and has not been interrogated in the context of myocardial infarction (MI) or mechanical loading and unloading. Using nanoscale mechanoscanning ion conductance microscopy, we demonstrate that MTs contribute to cardiomyocyte transverse YM in healthy and pathological states with different mechanical loading. Specifically, we show that posttranslational modifications of MTs have differing effects on cardiomyocyte YM: Acetylation provides flexibility, whereas detyrosination imparts rigidity. Further studies demonstrate that there is no correlation between the total protein amount of acetylated and detyrosinated MT. Yet, in the polymerized-only populations, an increased level of acetylation results in a decline of detyrosinated MTs in an MI model.

Nocodazole Induces Myeloma Cell Death by Disrupting the Microtubular Network, Resulting in G2/M Arrest

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 3673-3673
Author(s):  
Rentian Feng ◽  
Jorge A Rios ◽  
Markus Mapara ◽  
Suzanne Lentzsch
Keyword(s):  
Cell Cycle ◽  
Multiple Myeloma ◽  
Bone Marrow ◽  
Cell Death ◽  
Cell Lines ◽  
Myeloma Cell ◽  
Caspase 8 ◽  
Inhibition Rate ◽  
Growth And Survival ◽  
Microtubular Network

Abstract Patients with relapsed multiple myeloma (MM) previously treated with bortezomib and lenalidomide often fail to respond to further therapies. To identify potential new treatment approaches for MM, we used Luminex technology to screen a library of 1,120 compounds provided by the Multiple Myeloma Research Foundation. By multiplex cytokine array, we identified benzimidazoles including the anthelmintics mebendazole, fenbendazole, albendazole, nocodazole and pyrvinium pamoate, as inhibiting the production of cytokines essential for MM cell growth and survival, such as IL-6 (inhibition rate 40–70%), MIP-1α (inhibition rate 65–75%), VEGF (inhibition rate 75%), and soluble IL-6R (inhibition rate 40–52%). Consequently, these anthelmintics demonstrated dose-dependent inhibition of myeloma cell (RPMI-8226, H929, U266 and MM1S) proliferation. The lead compound, nocodazole, caused nuclear fragmentation and caspase-8 activation in MM cell lines and primary CD138+ cells in dose- and time-dependent fashion (IC50: 30–60 nM). Importantly, growth and survival signals provided by bone marrow stromal cells in bone marrow co-cultures failed to protect MM cells from nocodazole-induced cell death. In the apoptotic cells, caspase-8 was more activated than caspase-9, suggesting that mitochondrial signaling is not a major apoptotic pathway. Cell cycle analysis indicated that G2/M cell cycle arrest reached a peak at 17 hr. Sub-G1 proportion was strongly increased after treatment for 24 hr in all tested cell lines. Electron microscope (EM) and nuclear staining studies consistently showed the accumulation of metaphase cells, and morphologic elongation at 7 hr, at which time G2/M arrest was obvious. Most of the elongated cells had only one nucleus, suggesting that they failed to progress to mitosis due to overall microtubular network disarray. We conclude that nocodazole exposure induced microtubular network disarray with cell elongation, and G2/M arrest with a late stage mitotic block resulting in cell death. Benzimidazoles including nocodazole, traditionally used as antihelmintic drugs, have shown antitumor activity against hepatocellular, lung and adrenocortical carcinoma, and melanoma. In our study, we identified the anthelmintic compound nocodazole as a new anti-myeloma agent. Nocodazole warrants further investigation for its anti-MM effects in vitro and in vivo.

scholarly journals Platelet septin complexes form rings and associate with the microtubular network

2006 ◽  
Vol 4 (6) ◽  
pp. 1388-1395 ◽  
Author(s):  
C. MARTINEZ ◽  
J. CORRAL ◽  
J. A. DENT ◽  
L. SESMA ◽  
V. VICENTE ◽  
...  
Keyword(s):  
Microtubular Network

Skin fibroblast microtubular network in Alzheimer disease

1979 ◽  
Vol 6 (6) ◽  
pp. 548-552 ◽  
Author(s):  
C. G. Harper ◽  
D. Buck ◽  
N. K. Gonatas ◽  
B. Guilbert ◽  
S. Avrameas
Keyword(s):  
Alzheimer Disease ◽  
Skin Fibroblast ◽  
Microtubular Network

scholarly journals Mechanical Counterbalance of Kinesin and Dynein Motors in a Microtubular Network Regulates Cell Mechanics, 3D Architecture, and Mechanosensing

ACS Nano ◽  
2021 ◽  
Author(s):  
Alexander S. Zhovmer ◽  
Alexis Manning ◽  
Chynna Smith ◽  
James B. Hayes ◽  
Dylan T. Burnette ◽  
...  
Keyword(s):  
Cell Mechanics ◽  
3D Architecture ◽  
Microtubular Network

THE MICROTUBULAR NETWORK IN CULTURED FIBROBLASTS FROM ALZHEIMERʼS DISEASE

1979 ◽  
Vol 38 (3) ◽  
pp. 317
Author(s):  
C. Harper ◽  
S. Avrameas ◽  
B. Guilbert ◽  
N. K. Gonatas
Keyword(s):  
Cultured Fibroblasts ◽  
Microtubular Network

Nocodazole Induces Multiple Myeloma Cell Death and Reduces Tumor Growth through Sequential Microtubular Network Damage and C-Jun N-Terminal Kinase-Mediated Bcl-2 Phosphorylation.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 296-296
Author(s):  
Rentian Feng ◽  
Huihui Ma ◽  
Noriyoshi Kurihara ◽  
Shirong Li ◽  
Judy A Ziegler ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Bone Marrow ◽  
Cell Death ◽  
Tumor Growth ◽  
Murine Model ◽  
Immunofluorescent Staining ◽  
Solid Cancer ◽  
Dependent Manner ◽  
Microtubular Network ◽  
Induced Apoptosis

Abstract Abstract 296 Background: Benzimidazoles, originally categorized as broad-spectrum anthelmintic drugs, have been recently reported to induce growth arrest and apoptosis in some solid cancer models (e.g. colorectal and lung). We performed a multiplex drug-screening assay that identified benzimidazoles as potential anti-multiple myeloma (MM) agents. Methods and Results: In this study, we demonstrate that one of the benzimidazole members, nocodazole, inhibited proliferation and induced apoptosis in MM cell lines and primary MM cells alone and in co-culture with bone marrow stromal cells. The resistant phenotype of those MM cells resistant to conventional therapies could be completely reversed by nocodazole. The IC50 values were 60 nM (RPMI8226-S), 25 nM (RPMI8226-Dox40), 80 nM (RPMI8226-MR20), 60 nM (RPMI8226-LR5), 65 nM (MM.1S) and 60 nM (MM.1R). Viability of primary cells decreased by 66% in CD138+ cells and 7% in CD138− mononucleated bone marrow cells after 48 hour treatment. Cell cycle analysis revealed a G2/M arrest and subsequent cell death induced by nocodazole. Nocodazole also caused morphologic elongation in MM cells in a dose-dependent manner during prometaphase. The morphologically changed cells exhibited a microtubular network disarray as evidenced by microtubular immunofluorescent staining. Signaling studies indicated that increased expression of Bim protein and reduced XIAP and Mcl-1 levels were involved in nocodazole-induced apoptosis. Further investigation showed Bcl-2 phosphorylation as a critical mediator of cell death, which was triggered by the activation of JNK, instead of p38 kinase or ERKs. Treatment with JNK inhibitor SP600125 completely inhibited Bcl-2 phosphorylation at Ser70 and Thr56 induced by nocodazole. Nocodazole-induced cell death subsequently decreased from 79% to 28% after pretreatment with SP600125. Combination of nocodazole with dexamethasone induced significantly stronger induction of cell death at either drug dose. Dexamethasone at 20 nM, nocodazole at 15 or 30 nM could only induce 19%, 10.3% and 16% cell death, respectively. However, their combinations resulted in 67% and 92% nuclear fragmentation, respectively. Based on our in vitro data, we analyzed nocodazole in a SCID xenograft murine model. Nocodazole alone (5 and 20 mg/kg) or combined with dexamethasone (2 mg/kg) at a lower dose of 12 mg/kg significantly inhibited H929 tumor growth and prolonged survival in a SCID xenograft murine model. Conclusions: Our studies demonstrate that nocodazole has a potent anti-MM activity and might be a promising new treatment approach for MM. * Supported by a grant from the Multiple Myeloma Research Foundation. Disclosures: Roodman: Acceleron: Consultancy; Novartis: Consultancy, Research Funding, Speakers Bureau; Amgen: Consultancy; Celgene: Consultancy. Lentzsch:Celgene: Consultancy, Speakers Bureau; Pfizer: Consultancy.

Thyroid hormone regulates tubulin expression in mammalian liver. Effects of deleting thyroid hormone receptor-α or -β

2005 ◽  
Vol 289 (1) ◽  
pp. E87-E94 ◽  
Author(s):  
Carmen G. Vallejo ◽  
Ana M. Seguido ◽  
Pilar S. Testillano ◽  
María-Carmen Risueño
Keyword(s):  
Thyroid Hormone ◽  
Thyroid Hormone Receptor ◽  
Positive Control ◽  
Β Subunit ◽  
Α Subunit ◽  
Mammalian Liver ◽  
Microtubular Network ◽  
Tubulin Protein ◽  
Β Tubulin

Microtubules are made from polymers of α/β dimers. We have observed in rat liver that, on the first day after birth, α-subunit is relatively high and β-subunit low with respect to adult values. In the hypothyroid neonate, both subunits were found to be low, therefore indicating that thyroid hormone (TH) regulates these developmental changes. TH was also found to activate tubulin expression in adult liver, especially β-subunit. To investigate the role of TH receptors (TRs) in tubulin expression, we analyzed mice lacking TRα or TRβ compared with the wild type in both normal and TH-deprived adult animals. The results suggest that, in vivo, β-tubulin protein expression in the liver is primarily under TRβ positive control. In euthyroid mice lacking TRβ, β-tubulin expression was low. However, in the corresponding hypothyroid animals, it was found increased, therefore suggesting that the unliganded TRα might also upregulate β-tubulin expression. Accordingly, TH administration to hypothyroid TRβ-deprived mice reduced their high β-tubulin expression. In parallel, the relatively high messenger level observed with these hypothyroid animals was reduced to the euthyroid level after T3 treatment. The microtubular network of the mutant livers appeared, by immunofluorescence confocal microscopy, generally disorganized and drastically reduced in β-tubulin in mice lacking TRβ. In conclusion, our results indicate that β-tubulin is critically controlled by TRβ in the liver and that both TRs are probably needed to maintain the microtubular network organization of the liver.

Sign in / Sign up

Export Citation Format

Share Document