Log in

Relevant bibliographies by topics / Drebrin A / Journal articles

Journal articles on the topic 'Drebrin A'

To see the other types of publications on this topic, follow the link: Drebrin A.

Author: Grafiati

Published: 10 December 2022

Last updated: 30 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Drebrin A.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Chew, Catherine S., Curtis T. Okamoto, Xunsheng Chen, and Ruby Thomas. "Drebrin E2 is differentially expressed and phosphorylated in parietal cells in the gastric mucosa." American Journal of Physiology-Gastrointestinal and Liver Physiology 289, no. 2 (August 2005): G320—G331. http://dx.doi.org/10.1152/ajpgi.00002.2005.

Full text

Abstract:

Developmentally regulated brain proteins (drebrins) are highly expressed in brain where they may regulate actin filament formation in dendritic spines. Recently, the drebrin E2 isoform was detected in certain epithelial cell types including the gastric parietal cell. In gastric parietal cells, activation of HCl secretion is correlated with actin filament formation and elongation within intracellular canaliculi, which are the sites of acid secretion. The aim of this study was to define the pattern of drebrin expression in gland units in the intact rabbit oxyntic gastric mucosa and to initiate approaches to define the functions of this protein in parietal cells. Drebrin E2 expression was limited entirely or almost entirely to parietal cells and depended upon the localization of parietal cells along the gland axis. Rabbit drebrin E2 was cloned and found to share 86% identity with human drebrin 1a and to possess a number of cross-species conserved protein-protein interaction and phosphorylation consensus sites. Two-dimensional Western blot and phosphoaffinity column analyses confirmed that drebrin is phosphorylated in parietal cells, and several candidate phosphorylation sites were identified by mass spectrometry. Overexpression of epitope-tagged drebrin E2 led to the formation of microspikes and F-actin-rich ring-like structures in cultured parietal cells and suppressed cAMP-dependent acid secretory responses. In Madin-Darby canine kidney cells, coexpression of epitope-tagged drebrin and the Rho family GTPase Cdc42, which induces filopodial extension, produced an additive increase in the length of microspike projections. Coexpression of dominant negative Cdc42 with drebrin E2 did not prevent drebrin-induced microspike formation. These findings suggest that 1) drebrin can induce the formation of F-actin-rich membrane projections by Cdc42-dependent and -independent mechanisms; and that 2) drebrin plays an active role in directing the secretagogue-dependent formation of F-actin-rich filaments on the parietal cell canalicular membrane. Finally, the differential distribution of drebrin in parietal cells along the gland axis suggests that drebrin E2 may be an important marker of parietal cell differentiation and functionality.

APA, Harvard, Vancouver, ISO, and other styles

2

Grintsevich, Elena E. "Effects of neuronal drebrin on actin dynamics." Biochemical Society Transactions 49, no. 2 (March 19, 2021): 685–92. http://dx.doi.org/10.1042/bst20200577.

Full text

Abstract:

Drebrin is a key regulator of actin cytoskeleton in neuronal cells which is critical for synaptic plasticity, neuritogenesis, and neuronal migration. It is also known to orchestrate a cross-talk between actin and microtubules. Decreased level of drebrin is a hallmark of multiple neurodegenerative disorders such as Alzheimer's disease. Despite its established importance in health and disease, we still have a lot to learn about drebrin's interactome and its effects on cytoskeletal dynamics. This review aims to summarize the recently reported novel effects of drebrin on actin and its regulators. Here I will also reflect on the most recent progress made in understanding of the role of drebrin isoforms and posttranslational modifications on its functionality.

APA, Harvard, Vancouver, ISO, and other styles

3

Shan, Yufei, Stephen Matthew Farmer, and Susan Wray. "Drebrin regulates cytoskeleton dynamics in migrating neurons through interaction with CXCR4." Proceedings of the National Academy of Sciences 118, no. 3 (January 7, 2021): e2009493118. http://dx.doi.org/10.1073/pnas.2009493118.

Full text

Abstract:

Stromal cell-derived factor-1 (SDF-1) and chemokine receptor type 4 (CXCR4) are regulators of neuronal migration (e.g., GnRH neurons, cortical neurons, and hippocampal granule cells). However, how SDF-1/CXCR4 alters cytoskeletal components remains unclear. Developmentally regulated brain protein (drebrin) stabilizes actin polymerization, interacts with microtubule plus ends, and has been proposed to directly interact with CXCR4 in T cells. The current study examined, in mice, whether CXCR4 under SDF-1 stimulation interacts with drebrin to facilitate neuronal migration. Bioinformatic prediction of protein–protein interaction highlighted binding sites between drebrin and crystallized CXCR4. In migrating GnRH neurons, drebrin, CXCR4, and the microtubule plus-end binding protein EB1 were localized close to the cell membrane. Coimmunoprecipitation (co-IP) confirmed a direct interaction between drebrin and CXCR4 using wild-type E14.5 whole head and a GnRH cell line. Analysis of drebrin knockout (DBN1 KO) mice showed delayed migration of GnRH cells into the brain. A decrease in hippocampal granule cells was also detected, and co-IP confirmed a direct interaction between drebrin and CXCR4 in PN4 hippocampi. Migration assays on primary neurons established that inhibiting drebrin (either pharmacologically or using cells from DBN1 KO mice) prevented the effects of SDF-1 on neuronal movement. Bioinformatic prediction then identified binding sites between drebrin and the microtubule plus end protein, EB1, and super-resolution microscopy revealed decreased EB1 and drebrin coexpression after drebrin inhibition. Together, these data show a mechanism by which a chemokine, via a membrane receptor, communicates with the intracellular cytoskeleton in migrating neurons during central nervous system development.

APA, Harvard, Vancouver, ISO, and other styles

4

Imamura, Kosuke, Yusuke Tomita, Ryo Sato, Tokunori Ikeda, Shinji Iyama, Takayuki Jodai, Misako Takahashi, et al. "Clinical Implications and Molecular Characterization of Drebrin-Positive, Tumor-Infiltrating Exhausted T Cells in Lung Cancer." International Journal of Molecular Sciences 23, no. 22 (November 8, 2022): 13723. http://dx.doi.org/10.3390/ijms232213723.

Full text

Abstract:

T cells express an actin-binding protein, drebrin, which is recruited to the contact site between the T cells and antigen-presenting cells during the formation of immunological synapses. However, little is known about the clinical implications of drebrin-expressing, tumor-infiltrating lymphocytes (TILs). To address this issue, we evaluated 34 surgical specimens of pathological stage I–IIIA squamous cell lung cancer. The immune context of primary tumors was investigated using fluorescent multiplex immunohistochemistry. The high-speed scanning of whole-slide images was performed, and the tissue localization of TILs in the tumor cell nest and surrounding stroma was automatically profiled and quantified. Drebrin-expressing T cells were characterized using drebrin+ T cells induced in vitro and publicly available single-cell RNA sequence (scRNA-seq) database. Survival analysis using the propensity scores revealed that a high infiltration of drebrin+ TILs within the tumor cell nest was independently associated with short relapse-free survival and overall survival. Drebrin+ T cells induced in vitro co-expressed multiple exhaustion-associated molecules. The scRNA-seq analyses confirmed that the exhausted tumor-infiltrating CD8+ T cells specifically expressed drebrin. Our study suggests that drebrin-expressing T cells present an exhausted phenotype and that tumor-infiltrating drebrin+ T cells affect clinical outcomes in patients with resectable squamous cell lung cancer.

APA, Harvard, Vancouver, ISO, and other styles

5

Alvarez-Suarez, Paloma, Natalia Nowak, Anna Protasiuk-Filipunas, Hiroyuki Yamazaki, Tomasz J. Prószyński, and Marta Gawor. "Drebrin Regulates Acetylcholine Receptor Clustering and Organization of Microtubules at the Postsynaptic Machinery." International Journal of Molecular Sciences 22, no. 17 (August 30, 2021): 9387. http://dx.doi.org/10.3390/ijms22179387.

Full text

Abstract:

Proper muscle function depends on the neuromuscular junctions (NMJs), which mature postnatally to complex “pretzel-like” structures, allowing for effective synaptic transmission. Postsynaptic acetylcholine receptors (AChRs) at NMJs are anchored in the actin cytoskeleton and clustered by the scaffold protein rapsyn, recruiting various actin-organizing proteins. Mechanisms driving the maturation of the postsynaptic machinery and regulating rapsyn interactions with the cytoskeleton are still poorly understood. Drebrin is an actin and microtubule cross-linker essential for the functioning of the synapses in the brain, but its role at NMJs remains elusive. We used immunohistochemistry, RNA interference, drebrin inhibitor 3,5-bis-trifluoromethyl pyrazole (BTP2) and co-immunopreciptation to explore the role of this protein at the postsynaptic machinery. We identify drebrin as a postsynaptic protein colocalizing with the AChRs both in vitro and in vivo. We also show that drebrin is enriched at synaptic podosomes. Downregulation of drebrin or blocking its interaction with actin in cultured myotubes impairs the organization of AChR clusters and the cluster-associated microtubule network. Finally, we demonstrate that drebrin interacts with rapsyn and a drebrin interactor, plus-end-tracking protein EB3. Our results reveal an interplay between drebrin and cluster-stabilizing machinery involving rapsyn, actin cytoskeleton, and microtubules.

APA, Harvard, Vancouver, ISO, and other styles

6

Keon, B. H., P. T. Jedrzejewski, D. L. Paul, and D. A. Goodenough. "Isoform specific expression of the neuronal F-actin binding protein, drebrin, in specialized cells of stomach and kidney epithelia." Journal of Cell Science 113, no. 2 (January 15, 2000): 325–36. http://dx.doi.org/10.1242/jcs.113.2.325.

Full text

Abstract:

To further understand the functional role that the F-actin binding protein, drebrin (developmentally regulated brain protein), plays in the regulation of F-actin, we characterized its expression in non-neuronal cells. Using nanoelectrospray mass spectrometry methods, we initially identified drebrin in non-neuronal cultured cells. Using a drebrin-specific monoclonal antibody, we were able to detect drebrin protein in several different cell lines derived from fibroblasts, astrocytomas, and simple epithelia, but not in cell lines derived from stratified epithelia. Double-label immunofluorescence experiments of cultured cell monolayers revealed the localization of drebrin at the apical plasma membrane together with a pool of submembranous F-actin. Immunoblot analysis of mouse organs revealed that, in addition to its high levels of expression in brain, drebrin was present in stomach and to a lesser degree in kidney, colon, and urinary bladder. Drebrin protein detected in the non-brain organs migrated faster through SDS-PAGE gels, indicating that the lower molecular weight embryonic brain isoform (E2) may be the prominent isoform in these organs. RT-PCR experiments confirmed the specific expression of the E2 isoform in adult stomach, kidney, and cultured cells. In situ immunofluorescence experiments revealed a cell-type specific pattern in both stomach and kidney. In stomach, drebrin was specifically expressed in the acid-secreting parietal cells of the fundic glands, where it accumulated at the extended apical membrane of the canaliculi. In kidney, drebrin was expressed in acid-secreting type A intercalated cells, where it localized specifically to the apical plasma membrane. Drebrin was expressed as well in the distal tubule epithelial cells where the protein was concentrated at the luminal surface and present at the interdigitations of the basolateral membranes.

APA, Harvard, Vancouver, ISO, and other styles

7

Ramaswamy, Madhu, Thao Do, Mary Barden, Anthony Cruz, and Richard Siegel. "A proteomic study of early signaling events regulating the Fas-FasL Death Inducing Signaling Complex (163.20)." Journal of Immunology 188, no. 1_Supplement (May 1, 2012): 163.20. http://dx.doi.org/10.4049/jimmunol.188.supp.163.20.

Full text

Abstract:

Abstract Clearance of activated T cells by the Fas-FasL pathway is a critical mechanism of peripheral CD4 T cell tolerance. This process is preferentially higher in the effector subset of memory CD4+ T cells due to efficient recruitment and formation of the Fas death inducing signaling complex (DISC). In order to elucidate mechanisms of this heightened apoptosis sensitivity, we tested for differential DISC interacting proteins in Fas sensitive and Fas resistant CTCL cell lines using 2D-DIGE and Mass Spectrometry. We found several candidate proteins and invitro studies were done to confirm Fas receptor interactions through overexpression and Flourescence Energy Transfer (FRET) studies. One of these targets, Drebrin, is an actin binding protein previously found to play a role in T cell synapse formation by facilitating CXCR4 recruitment. Overexpression in 293 indicates that Drebrin interacts with Fas receptor. Further, endogenous drebrin preassociates with Fas receptor and remains associated with the Fas DISC even after Fas ligation only in Type I SKW cell line. Interestingly, Fas DISC associated Drebrin gets cleaved after Fas treatment and invitro caspase cleavage studies indicate that drebrin is a specific downstream target of caspase-8. Our studies propose Drebrin as a novel Fas interacting protein. Investigations are currently underway to study the mechanisms by which Drebrin modifies the Fas-DISC dynamics and the significance of the caspase-cleaved Drebrin in this process.

APA, Harvard, Vancouver, ISO, and other styles

8

Worth, Daniel C., Catherine N. Daly, Sara Geraldo, Fazal Oozeer, and Phillip R. Gordon-Weeks. "Drebrin contains a cryptic F-actin–bundling activity regulated by Cdk5 phosphorylation." Journal of Cell Biology 202, no. 5 (August 26, 2013): 793–806. http://dx.doi.org/10.1083/jcb.201303005.

Full text

Abstract:

Drebrin is an actin filament (F-actin)–binding protein with crucial roles in neuritogenesis and synaptic plasticity. Drebrin couples dynamic microtubules to F-actin in growth cone filopodia via binding to the microtubule-binding +TIP protein EB3 and organizes F-actin in dendritic spines. Precisely how drebrin interacts with F-actin and how this is regulated is unknown. We used cellular and in vitro assays with a library of drebrin deletion constructs to map F-actin binding sites. We discovered two domains in the N-terminal half of drebrin—a coiled-coil domain and a helical domain—that independently bound to F-actin and cooperatively bundled F-actin. However, this activity was repressed by an intramolecular interaction relieved by Cdk5 phosphorylation of serine 142 located in the coiled-coil domain. Phospho-mimetic and phospho-dead mutants of serine 142 interfered with neuritogenesis and coupling of microtubules to F-actin in growth cone filopodia. These findings show that drebrin contains a cryptic F-actin–bundling activity regulated by phosphorylation and provide a mechanistic model for microtubule–F-actin coupling.

APA, Harvard, Vancouver, ISO, and other styles

9

Ginosyan, Anush A., Elena E. Grintsevich, and Emil Reisler. "Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly." Molecular Biology of the Cell 30, no. 5 (March 2019): 646–57. http://dx.doi.org/10.1091/mbc.e18-10-0639.

Full text

Abstract:

Dendritic spines (DS) are actin-rich postsynaptic terminals of neurons that are critical for higher-order brain functions. Maturation of DS is accompanied by a change in actin architecture from linear to branched filamentous structures. Presumably, the underlying cause of this is a switch in a mode of actin assembly from formin-driven to Arp2/3-mediated via an undefined mechanism. Here we present data suggesting that neuron-specific actin-binding drebrin A may be a part of such a switch. It is well documented that DS are highly enriched in drebrin A, which is critical for their plasticity and function. At the same time, mDia2 is known to mediate the formation of filopodia-type (immature) spines. We found that neuronal drebrin A directly interacts with mDia2 formin. Drebrin inhibits formin-mediated nucleation of actin and abolishes mDia2-induced actin bundling. Using truncated protein constructs we identified the domain requirements for drebrin–mDia2 interaction. We hypothesize that accumulation of drebrin A in DS (that coincides with spine maturation) leads to inhibition of mDia2-driven actin polymerization and, therefore, may contribute to a change in actin architecture from linear to branched filaments.

APA, Harvard, Vancouver, ISO, and other styles

10

Leslie, Mitch. "Drebrin shows self-restraint." Journal of Cell Biology 202, no. 5 (August 26, 2013): 720. http://dx.doi.org/10.1083/jcb.2025iti2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Ma, Lina, Yun Li, and Rong Wang. "Drebrin and cognitive impairment." Clinica Chimica Acta 451 (December 2015): 121–24. http://dx.doi.org/10.1016/j.cca.2015.06.021.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Ferhat, Lotfi. "Potential Role of Drebrin A, an F-Actin Binding Protein, in Reactive Synaptic Plasticity after Pilocarpine-Induced Seizures: Functional Implications in Epilepsy." International Journal of Cell Biology 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/474351.

Full text

Abstract:

Several neurological disorders characterized by cognitive deficits, including Alzheimer's disease, down syndrome, and epilepsy exhibit abnormal spine density and/or morphology. Actin-based cytoskeleton network dynamics is critical for the regulation of spine morphology and synaptic function. In this paper, I consider the functions of drebrin A in cell shaping, spine plasticity, and synaptic function. Developmentally regulated brain protein (drebrin A) is one of the most abundant neuron-specific binding proteins of F-actin and its expression is increased in parallel with synapse formation. Drebrin A is particularly concentrated in dendritic spines receiving excitatory inputs. Our recent findings point to a critical role of DA in dendritic spine structural integrity and stabilization, likely via regulation of actin cytoskeleton dynamics, and glutamatergic synaptic function that underlies the development of spontaneous recurrent seizures in pilocarpine-treated animals. Further research into this area may provide useful insights into the pathology of status epilepticus and epileptogenic mechanisms and ultimately may provide the basis for future treatment options.

APA, Harvard, Vancouver, ISO, and other styles

13

Yamazaki, Hiroyuki, Yoshio Sasagawa, Hideyuki Yamamoto, Haruhiko Bito, and Tomoaki Shirao. "CaMKIIβ is localized in dendritic spines as both drebrin-dependent and drebrin-independent pools." Journal of Neurochemistry 146, no. 2 (June 11, 2018): 145–59. http://dx.doi.org/10.1111/jnc.14449.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Shirao, Tomoaki, Nobuhiko Kojima, and Kunihiko Obata. "Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells." NeuroReport 3, no. 1 (January 1992): 109–12. http://dx.doi.org/10.1097/00001756-199201000-00029.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Shirao, T., N. Kojima, and K. Obata. "Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells." NeuroReport 3, no. 3 (March 1992): 286. http://dx.doi.org/10.1097/00001756-199203000-00020.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Shirao, Tomoaki, Kenji Hanamura, Noriko Koganezawa, Yuta Ishizuka, Hiroyuki Yamazaki, and Yuko Sekino. "The role of drebrin in neurons." Journal of Neurochemistry 141, no. 6 (April 21, 2017): 819–34. http://dx.doi.org/10.1111/jnc.13988.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Mikati, Mouna A., Elena E. Grintsevich, and Emil Reisler. "Drebrin-induced Stabilization of Actin Filaments." Journal of Biological Chemistry 288, no. 27 (May 21, 2013): 19926–38. http://dx.doi.org/10.1074/jbc.m113.472647.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Yao, Ningning, Jianchao Li, Haiyang Liu, Jun Wan, Wei Liu, and Mingjie Zhang. "The Structure of the ZMYND8/Drebrin Complex Suggests a Cytoplasmic Sequestering Mechanism of ZMYND8 by Drebrin." Structure 25, no. 11 (November 2017): 1657–66. http://dx.doi.org/10.1016/j.str.2017.08.014.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Yamada, Mie, Hidetake Kurihara, Katsuyuki Kinoshita, and Tatsuo Sakai. "Temporal Expression of Alpha–Smooth Muscle Actin and Drebrin in Septal Interstitial Cells during Alveolar Maturation." Journal of Histochemistry & Cytochemistry 53, no. 6 (June 2005): 735–44. http://dx.doi.org/10.1369/jhc.4a6483.2005.

Full text

Abstract:

In rat lung, the definitive alveoli are established during development by the outgrowth of secondary septa from the primary septa present in newborn; however, the mechanism of alveolar formation has not yet been fully clarified. In this study, we characterize the septal interstitial cells in developing alveoli. During the perinatal period, alpha-SMA–containing slender cells were found in the primitive alveolar septa. Alpha-SMA–containing cells were detected at the tips of the septa until postnatal day 21, when the alveolar formation was almost completed, but disappeared in adult. Immunoelectron microscopy demonstrated that alpha-SMA is localized mainly in the cellular protrusions, which are connected with the elastic fibers around the interstitial cells. Developmentally regulated brain protein (drebrin) is also located in the cell extensions containing alpha-SMA in immature alveolar interstitial cells. In adult lung, alpha-SMA–positive cells are located only at the alveolar ducts but are not found in the secondary septa. Desmin is expressed only in alpha-SMA–containing cells at the alveolar ducts but not in those at the tip of alveolar septa. These results suggest that a part of the septal interstitial cells are temporarily alpha-SMA– and drebrin-positive during maturation. Alpha-SMA– and drebrin-containing septal interstitial cells (termed septal myofibroblast-like cells) may play an important role in alveolar formation.

APA, Harvard, Vancouver, ISO, and other styles

20

Fucini, Raymond V., Ji-Long Chen, Catherine Sharma, Michael M. Kessels, and Mark Stamnes. "Golgi Vesicle Proteins Are Linked to the Assembly of an Actin Complex Defined by mAbp1." Molecular Biology of the Cell 13, no. 2 (February 2002): 621–31. http://dx.doi.org/10.1091/mbc.01-11-0547.

Full text

Abstract:

Recent studies indicate that regulation of the actin cytoskeleton is important for protein trafficking, but its precise role is unclear. We have characterized the ARF1-dependent assembly of actin on the Golgi apparatus. Actin recruitment involves Cdc42/Rac and requires the activation of the Arp2/3 complex. Although the actin-binding proteins mAbp1 (SH3p7) and drebrin share sequence homology, they are differentially segregated into two distinct ARF-dependent actin complexes. The binding of Cdc42 and mAbp1, which localize to the Golgi apparatus, but not drebrin, is blocked by occupation of the p23 cargo-protein-binding site on coatomer. Exogenously expressed mAbp1 is mislocalized and inhibits Golgi transport in whole cells. The ability of ARF, vesicle-coat proteins, and cargo to direct the assembly of cytoskeletal structures helps explain how only a handful of vesicle types can mediate the numerous trafficking steps in the cell.

APA, Harvard, Vancouver, ISO, and other styles

21

Lemkuil, Brian P., Brian P. Head, Matthew L. Pearn, Hemal H. Patel, John C. Drummond, and Piyush M. Patel. "Isoflurane Neurotoxicity Is Mediated by p75NTR-RhoA Activation and Actin Depolymerization." Anesthesiology 114, no. 1 (January 1, 2011): 49–57. http://dx.doi.org/10.1097/aln.0b013e318201dcb3.

Full text

Abstract:

Background The mechanisms by which isoflurane injured the developing brain are not clear. Recent work has demonstrated that it is mediated in part by activation of p75 neurotrophin receptor. This receptor activates RhoA, a small guanosine triphosphatase that can depolymerize actin. It is therefore conceivable that inhibition of RhoA or prevention of cytoskeletal depolymerization might attenuate isoflurane neurotoxicity. This study was conducted to test these hypotheses using primary cultured neurons and hippocampal slice cultures from neonatal mouse pups. Methods Primary neuron cultures (days in vitro, 4-7) and hippocampal slice cultures from postnatal day 4-7 mice were exposed to 1.4% isoflurane (4 h). Neurons were pretreated with TAT-Pep5, an intracellular inhibitor of p75 neurotrophin receptor, the cytoskeletal stabilizer jasplakinolide, or their corresponding vehicles. Hippocampal slice cultures were pretreated with TAT-Pep5 before isoflurane exposure. RhoA activation was evaluated by immunoblot. Cytoskeletal depolymerization and apoptosis were evaluated with immunofluorescence microscopy using drebrin and cleaved caspase-3 staining, respectively. Results RhoA activation was increased after 30 and 120 min of isoflurane exposure in neurons; TAT-Pep5 (10 μm) decreased isoflurane-mediated RhoA activation at both time intervals. Isoflurane decreased drebrin immunofluorescence and enhanced cleaved caspase-3 in neurons, effects that were attenuated by pretreatment with either jasplakinolide (1 μm) or TAT-Pep5. TAT-Pep5 attenuated the isoflurane-mediated decrease in phalloidin immunofluorescence. TAT-Pep5 significantly attenuated isoflurane-mediated loss of drebrin immunofluorescence in hippocampal slices. Conclusions Isoflurane results in RhoA activation, cytoskeletal depolymerization, and apoptosis. Inhibition of RhoA activation or prevention of downstream actin depolymerization significantly attenuated isoflurane-mediated neurotoxicity in developing neurons.

APA, Harvard, Vancouver, ISO, and other styles

22

Zhang, Lisheng, Jiao-Hui Wu, Tai-Qin Huang, Igor Nepliouev, Leigh Brian, Zhushan Zhang, Virginia Wertman, et al. "Drebrin regulates angiotensin II-induced aortic remodelling." Cardiovascular Research 114, no. 13 (June 20, 2018): 1806–15. http://dx.doi.org/10.1093/cvr/cvy151.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Taketomi, Ayako, Ryoki Ishikawa, and Tomoaki Shirao. "623 Analysis of functional domain of drebrin." Neuroscience Research Supplements 18 (January 1993): S78. http://dx.doi.org/10.1016/s0921-8696(05)80891-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Koganezawa, Noriko, Kenji Hanamura, Yuko Sekino, and Tomoaki Shirao. "The role of drebrin in dendritic spines." Molecular and Cellular Neuroscience 84 (October 2017): 85–92. http://dx.doi.org/10.1016/j.mcn.2017.01.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Hayashi, Kensuke, and Tomoaki Shirao. "1112 Activity dependent change in drebrin isoforms." Neuroscience Research 25 (January 1996): S115. http://dx.doi.org/10.1016/0168-0102(96)88875-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Hayashi, Yasunori. "Drebrin-Homer Interaction at An Atomic Scale." Structure 27, no. 1 (January 2019): 3–5. http://dx.doi.org/10.1016/j.str.2018.12.008.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Counts, Scott E., Bin He, Muhammad Nadeem, Joanne Wuu, Stephen W. Scheff, and Elliott J. Mufson. "Hippocampal Drebrin Loss in Mild Cognitive Impairment." Neurodegenerative Diseases 10, no. 1-4 (2012): 216–19. http://dx.doi.org/10.1159/000333122.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Mammoto, Akiko, Takuya Sasaki, Takeshi Asakura, Ikuko Hotta, Hiroshi Imamura, Kazuo Takahashi, Yoshiharu Matsuura, Tomoaki Shirao, and Yoshimi Takai. "Interactions of Drebrin and Gephyrin with Profilin." Biochemical and Biophysical Research Communications 243, no. 1 (February 1998): 86–89. http://dx.doi.org/10.1006/bbrc.1997.8068.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Peitsch, Wiebke K., Jutta Bulkescher, Herbert Spring, Ilse Hofmann, Sergij Goerdt, and Werner W. Franke. "Dynamics of the actin-binding protein drebrin in motile cells and definition of a juxtanuclear drebrin-enriched zone." Experimental Cell Research 312, no. 13 (August 2006): 2605–18. http://dx.doi.org/10.1016/j.yexcr.2006.04.017.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Irfannuddin, Irfannuddin, Minarma Siagian, Sri Jusman, Jan Purba, Ermita Ilyas, and Nurhadi Ibrahim. "Hurdle Aerobic Exercise Increases Angiogenesis and Neuroplasticity in the Hippocampus and Improves the Spatial Memory Ability of Middle-aged Mice." Open Access Macedonian Journal of Medical Sciences 8, A (July 30, 2020): 395–402. http://dx.doi.org/10.3889/oamjms.2020.3840.

Full text

Abstract:

BACKGROUND: Complex aerobic exercise is believed to induce positive effects on neuron structure and cognitive function. Long-term and continual cognitive stimulation increases neuroplasticity by stimulating the synthesis of neuronal growth proteins and the formation of new synapses. Exercise also increases the ability of neurons to survive and improves brain vascularization. Further investigations should be conducted to explore what types of aerobic exercise are beneficial for cognitive function. AIM: This study investigated the effects of hurdle aerobic exercise on developmentally regulated brain protein-A (Drebrin-A) as a neuroplasticity indicator, and on vascular endothelial growth factor (VEGF) as an angiogenesis marker in the hippocampus. METHODS: This study was an experimental study with post-test only control group design. Thirty-three adult mice were divided into control, hurdle aerobic runner (HAR), and plain aerobic runner (PAR) groups (n = 11 for each group). Fiberglass running wheels were originally designed and modified to assemble hurdles inside with adjustable speed. Speed adaptation was intended to achieve aerobic intensity. The experiment was performed 5 times a week for 8 weeks. The Morris water maze test (MWMT) was used to assess spatial memory ability. One day after the last running exercise and final MWMT, the mice were sacrificed and the right side of the hippocampus was obtained for Drebrin-A analysis by enzyme-linked immunosorbent assay (ELISA). The entire right side brain tissue after hippocampus was removed then used for the neuroglobin ELISA assay. To analyze VEGF expression and calculation of blood vessel, the left side of the brain was prepared for hematoxylin eosin and immunohistochemistry staining. To assess the effect of exercise on vascular widening, the analysis of the slides was performed by calculating the percentage of blood vessels with diameters more than 15 μm. One-way ANOVA and Fisher’s least significant difference test was used for statistical analysis. RESULTS: There was a significant difference in the levels of Drebrin-A between the HAR and PAR groups. Both exercise groups had higher levels of Drebrin-A than the control group. HAR and PAR groups exhibited significantly higher percentages of blood vessels expressing VEGF in hippocampus compared to control. HAR and PAR groups had the higher percentages of larger vessels compare to control. There was no significant difference of neuroglobin levels among the three groups. Both the HAR and PAR groups exhibited better spatial memory than the control group. CONCLUSION: Both aerobic exercises induced positive effects on brain angiogenesis, while the intensity of aerobic exercises did not result in high hypoxic stress in the brain.

APA, Harvard, Vancouver, ISO, and other styles

31

Stiber, Jonathan A., Jiao-Hui Wu, Lisheng Zhang, Igor Nepliouev, Zhu-Shan Zhang, Victoria G. Bryson, Leigh Brian, et al. "The Actin-Binding Protein Drebrin Inhibits Neointimal Hyperplasia." Arteriosclerosis, Thrombosis, and Vascular Biology 36, no. 5 (May 2016): 984–93. http://dx.doi.org/10.1161/atvbaha.115.306140.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Ning, Gang, Rachel Reynolds, and Avery August. "Drebrin Depletion Causes Abnormal Morphology in Mouse Skin." Microscopy and Microanalysis 22, S3 (July 2016): 1186–87. http://dx.doi.org/10.1017/s1431927616006772.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Li, Zhiwei, Haiyang Liu, Jianchao Li, Qingqing Yang, Zhe Feng, Yujie Li, Haibin Yang, et al. "Homer Tetramer Promotes Actin Bundling Activity of Drebrin." Structure 27, no. 1 (January 2019): 27–38. http://dx.doi.org/10.1016/j.str.2018.10.011.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Hayashi, Kensuke, and Tomoaki Shirao. "802 Subcellular localization of GFP-drebrin fusion proteins." Neuroscience Research 28 (January 1997): S100. http://dx.doi.org/10.1016/s0168-0102(97)90264-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Yong, Ren, Yuko Sekino, Mitsuhiro Kimura, and Tomoaki Shirao. "Developmental changes of drebrin subcellular localization within neurons." Neuroscience Research 31 (January 1998): S110. http://dx.doi.org/10.1016/s0168-0102(98)81961-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Grintsevich, Elena E., Vitold E. Galkin, Albina Orlova, A. Jimmy Ytterberg, Mouna M. Mikati, Dmitri S. Kudryashov, Joseph A. Loo, Edward H. Egelman, and Emil Reisler. "Mapping of Drebrin Binding Site on F-Actin." Journal of Molecular Biology 398, no. 4 (May 2010): 542–54. http://dx.doi.org/10.1016/j.jmb.2010.03.039.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Grintsevich, Elena E., and Emil Reisler. "Drebrin inhibits cofilin-induced severing of F-actin." Cytoskeleton 71, no. 8 (August 2014): 472–83. http://dx.doi.org/10.1002/cm.21184.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Ooe, Norihisa, Koichi Saito, Nobuyoshi Mikami, Iwao Nakatuka, and Hideo Kaneko. "Identification of a Novel Basic Helix-Loop-Helix-PAS Factor, NXF, Reveals a Sim2 Competitive, Positive Regulatory Role in Dendritic-Cytoskeleton Modulator Drebrin Gene Expression." Molecular and Cellular Biology 24, no. 2 (January 15, 2004): 608–16. http://dx.doi.org/10.1128/mcb.24.2.608-616.2004.

Full text

Abstract:

ABSTRACT Sim2, a basic helix-loop-helix (bHLH)-PAS transcriptional repressor, is thought to be involved in some symptoms of Down's syndrome. In the course of searching for hypothetical Sim2 relatives, we isolated another bHLH-PAS factor, NXF. NXF was a novel gene and was selectively expressed in neuronal tissues. While no striking homolog of NXF was found in vertebrates, a Caenorhabditis elegans putative transcription factor, C15C8.2, showed similarity in the bHLH-PAS domain. NXF had an activation domain as a transcription activator, and Arnt-type bHLH-PAS subfamily members were identified as the heterodimer partners of NXF. The NXF/Arnt heterodimer was capable of binding and activating a subset of Sim2/Arnt target DNA variants, and Sim2 could compete with the NXF activity on the elements. We showed that Drebrin had several such NXF/Arnt binding elements on the promoter, which could be direct or indirect cross talking points between NXF (activation) and Sim2 (repression) action. Drebrin has been reported to be engaged in dendritic-cytoskeleton modulation at synapses, and such a novel NXF signaling system on neural gene promoter may be a molecular target of the adverse effects of Sim2 in the mental retardation of Down's syndrome.

APA, Harvard, Vancouver, ISO, and other styles

39

Ren, Y. "Change in the subcellular localization of drebrin-like immunoreactivity and in the expression of the drebrin A isoform during cerebral development." Neuroscience Research 38 (2000): S134. http://dx.doi.org/10.1016/s0168-0102(00)81648-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Kojima, Nobuhiko, Tomoaki Shirao, and Kunihiko Obata. "Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene." Molecular Brain Research 19, no. 1-2 (July 1993): 101–14. http://dx.doi.org/10.1016/0169-328x(93)90154-h.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Li, Bin, Siyuan Ding, Ningguo Feng, Nancie Mooney, Yaw Shin Ooi, Lili Ren, Jonathan Diep, et al. "Drebrin restricts rotavirus entry by inhibiting dynamin-mediated endocytosis." Proceedings of the National Academy of Sciences 114, no. 18 (April 17, 2017): E3642—E3651. http://dx.doi.org/10.1073/pnas.1619266114.

Full text

Abstract:

Despite the wide administration of several effective vaccines, rotavirus (RV) remains the single most important etiological agent of severe diarrhea in infants and young children worldwide, with an annual mortality of over 200,000 people. RV attachment and internalization into target cells is mediated by its outer capsid protein VP4. To better understand the molecular details of RV entry, we performed tandem affinity purification coupled with high-resolution mass spectrometry to map the host proteins that interact with VP4. We identified an actin-binding protein, drebrin (DBN1), that coprecipitates and colocalizes with VP4 during RV infection. Importantly, blocking DBN1 function by siRNA silencing, CRISPR knockout (KO), or chemical inhibition significantly increased host cell susceptibility to RV infection.Dbn1KO mice exhibited higher incidence of diarrhea and more viral antigen shedding in their stool samples compared with the wild-type littermates. In addition, we found that uptake of other dynamin-dependent cargos, including transferrin, cholera toxin, and multiple viruses, was also enhanced in DBN1-deficient cells. Inhibition of cortactin or dynamin-2 abrogated the increased virus entry observed in DBN1-deficient cells, suggesting that DBN1 suppresses dynamin-mediated endocytosis via interaction with cortactin. Our study unveiled an unexpected role of DBN1 in restricting the entry of RV and other viruses into host cells and more broadly to function as a crucial negative regulator of diverse dynamin-dependent endocytic pathways.

APA, Harvard, Vancouver, ISO, and other styles

42

Sawada, Hisashi, Bradley C. Wright, Jeff Z. Chen, Hong S. Lu, and Alan Daugherty. "Drebrin: a new player in angiotensin II-induced aortopathies." Cardiovascular Research 114, no. 13 (August 13, 2018): 1699–701. http://dx.doi.org/10.1093/cvr/cvy205.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Sonego, Martina, Michelle Oberoi, Jake Stoddart, Sangeetha Gajendra, Rita Hendricusdottir, Fazal Oozeer, Daniel C. Worth, et al. "Drebrin Regulates Neuroblast Migration in the Postnatal Mammalian Brain." PLOS ONE 10, no. 5 (May 6, 2015): e0126478. http://dx.doi.org/10.1371/journal.pone.0126478.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Hanamura, Kenji, Yousuke Kamata, Hiroyuki Yamazaki, Nobuhiko Kojima, and Tomoaki Shirao. "Isoform-dependent Regulation of Drebrin Dynamics in Dendritic Spines." Neuroscience 379 (May 2018): 67–76. http://dx.doi.org/10.1016/j.neuroscience.2018.02.038.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Biou, Virginie, Heike Brinkhaus, Robert C. Malenka, and Andrew Matus. "Interactions between drebrin and Ras regulate dendritic spine plasticity." European Journal of Neuroscience 27, no. 11 (June 2008): 2847–59. http://dx.doi.org/10.1111/j.1460-9568.2008.06269.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Yamazaki, H. "Analysis of the intracellular distribution of SH3P7 and drebrin." Neuroscience Research 38 (2000): S105. http://dx.doi.org/10.1016/s0168-0102(00)81474-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Terakawa, Yuzo, Sameer Agnihotri, Brian Golbourn, Mustafa Nadi, Nesrin Sabha, Christian A. Smith, Sidney E. Croul, and James T. Rutka. "The role of drebrin in glioma migration and invasion." Experimental Cell Research 319, no. 4 (February 2013): 517–28. http://dx.doi.org/10.1016/j.yexcr.2012.11.008.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Ishikawa, Ryoki, Kaoru Katoh, Ayumi Takahashi, Ce Xie, Koushi Oseki, Michitoshi Watanabe, Michihiro Igarashi, Akio Nakamura, and Kazuhiro Kohama. "Drebrin attenuates the interaction between actin and myosin-V." Biochemical and Biophysical Research Communications 359, no. 2 (July 2007): 398–401. http://dx.doi.org/10.1016/j.bbrc.2007.05.123.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Pitsch, Julika, Delara Kamalizade, Anna Braun, Julia C. Kuehn, Polina E. Gulakova, Theodor Rüber, Gert Lubec, et al. "Drebrin Autoantibodies in Patients with Seizures and Suspected Encephalitis." Annals of Neurology 87, no. 6 (April 10, 2020): 869–84. http://dx.doi.org/10.1002/ana.25720.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Song, M., N. Kojima, K. Hanamura, Y. Sekino, H. K. Inoue, M. Mikuni, and T. Shirao. "Expression of drebrin E in migrating neuroblasts in adult rat brain: Coincidence between drebrin E disappearance from cell body and cessation of migration." Neuroscience 152, no. 3 (March 2008): 670–82. http://dx.doi.org/10.1016/j.neuroscience.2007.10.068.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!