scholarly journals Synaptic activation of NF-kappa B by glutamate in cerebellar granule neurons in vitro.

1995 ◽  
Vol 92 (20) ◽  
pp. 9077-9081 ◽  
Author(s):  
L. Guerrini ◽  
F. Blasi ◽  
S. Denis-Donini
Keyword(s):  
Cerebellar Granule Neurons ◽  
Granule Neurons ◽  
Synaptic Activation ◽  
Nf Kappa B ◽  
Cerebellar Granule

Cultured cerebellar granule neurons as an in vitro aging model: Topoisomerase IIβ as an additional biomarker in DNA repair and aging

2010 ◽  
Vol 24 (7) ◽  
pp. 1935-1945 ◽  
Author(s):  
M. Uday Bhanu ◽  
R.K. Mandraju ◽  
C. Bhaskar ◽  
Anand Kumar Kondapi
Keyword(s):  
Dna Repair ◽  
Cerebellar Granule Neurons ◽  
Granule Neurons ◽  
Cerebellar Granule ◽  
Aging Model ◽  
In Vitro Aging

Actin disruption alters the localization of tau in the growth cones of cerebellar granule neurons

2000 ◽  
Vol 113 (15) ◽  
pp. 2797-2809
Author(s):  
J.F. Zmuda ◽  
R.J. Rivas
Keyword(s):  
Growth Cone ◽  
Growth Cones ◽  
Cerebellar Granule Neurons ◽  
Granule Neurons ◽  
Filamentous Actin ◽  
Cerebellar Granule ◽  
Single Axon ◽  
Peripheral Domain ◽  
The Way

Cultured cerebellar granule neurons initially extend a single axon, followed by the extension of a second axon to attain a bipolar morphology. Differentiation culminates with the extension of several short dendrites from the cell body. In the present study, we determined the location of the dephosphorylated form of the microtubule-associated protein tau (dtau) within the growth cones of newly forming axons and examined whether this localization was influenced by the actin cytoskeleton. Following elongation of the initial axon at 2–3 days in vitro, dtau immunoreactivity was present along the entire length of the axon, becoming most intense just proximal to the growth cone. Dtau labeling dropped off dramatically along the microtubules of the growth cone and was undetectable along the most distal tips of these microtubules. As the initial axon continued to elongate at 3–4 days in vitro, the actin-rich growth cone peripheral domain characteristically underwent a dramatic reduction in size. Dtau immunoreactivity extended all the way to the most distal tips of the microtubules in the growth cones of these cells. Cytochalasin D and latrunculin A mimicked the effects of this characteristic reduction in growth cone size with regard to dtau localization in the growth cone. Depolymerization of filamentous actin caused the collapse of the peripheral domain and allowed dtau to bind all the way to the most distal tips of microtubules in the axon. Upon removal of the drugs, the peripheral domain of the growth cone rapidly re-formed and dtau was once again excluded from the most distal regions of growth cone microtubules. These findings suggest a novel role for actin in determining the localization of the microtubule-associated protein τ within the growth cones of neurons.

Chemotherapy-induced cell death in primary cerebellar granule neurons but not in astrocytes: in vitro paradigm of differential neurotoxicity

2004 ◽  
Vol 91 (5) ◽  
pp. 1067-1074 ◽  
Author(s):  
Antje Wick ◽  
Wolfgang Wick ◽  
Johannes Hirrlinger ◽  
Ellen Gerhardt ◽  
Ralf Dringen ◽  
...  
Keyword(s):  
Cell Death ◽  
Cerebellar Granule Neurons ◽  
Granule Neurons ◽  
Cerebellar Granule

scholarly journals Protective Effect of Edaravone in Primary Cerebellar Granule Neurons against Iodoacetic Acid-Induced Cell Injury

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Xinhua Zhou ◽  
Longjun Zhu ◽  
Liang Wang ◽  
Baojian Guo ◽  
Gaoxiao Zhang ◽  
...  
Keyword(s):  
Cell Injury ◽  
Neuronal Damage ◽  
Radical Scavenging ◽  
Iodoacetic Acid ◽  
Cerebellar Granule Neurons ◽  
Granule Neurons ◽  
Cerebellar Granule ◽  
Scavenging Effect ◽  
Underlying Mechanisms

Edaravone (EDA) is clinically used for treatment of acute ischemic stroke in Japan and China due to its potent free radical-scavenging effect. However, it has yet to be determined whether EDA can attenuate iodoacetic acid- (IAA-) induced neuronal deathin vitro. In the present study, we investigated the effect of EDA on damage of IAA-induced primary cerebellar granule neurons (CGNs) and its possible underlying mechanisms. We found that EDA attenuated IAA-induced cell injury in CGNs. Moreover, EDA significantly reduced intracellular reactive oxidative stress production, loss of mitochondrial membrane potential, and caspase 3 activity induced by IAA. Taken together, EDA protected CGNs against IAA-induced neuronal damage, which may be attributed to its antiapoptotic and antioxidative activities.

Astrotactin provides a receptor system for CNS neuronal migration

Development ◽  
1991 ◽  
Vol 113 (3) ◽  
pp. 755-765 ◽  
Author(s):  
G. Fishell ◽  
M.E. Hatten
Keyword(s):  
Neuronal Migration ◽  
Cerebellar Granule Neurons ◽  
Central Position ◽  
Granule Neurons ◽  
Receptor System ◽  
Vitro Assay ◽  
Cerebellar Granule ◽  
Migration Rates ◽  
Neuronal Receptor

CNS neuronal migration is a specialized form of cell motility that sets forth the laminar structure of cortical regions of brain. To define the neuronal receptor systems in glial-guided neuronal migration, an in vitro assay was developed for mouse cerebellar granule neurons, which provides simultaneous tracking of hundreds of migrating neurons. Three general classes of receptor systems were analyzed, the neuron-glial adhesion ligand astrotactin, the neural cell adhesion molecules of the IgG superfamily, N-CAM, L1 and TAG-1, and the beta 1 subunit of the integrin family. In the absence of immune activities, migrating cerebellar granule neurons had an average in vitro migration rate of 12 microns h-1, with individual neurons exhibiting migration rates over a range between 0 to 70 microns h-1. The addition of anti-astrotactin antibodies (or Fabs) significantly reduced the mean rate of neuronal migration by sixty-one percent, resulting in eighty percent of the neurons having migration rates below 8 microns h-1. By contrast, blocking antibodies (or Fabs) against L1, N-CAM, TAG-1 or beta 1 integrin, individually or in combination, did not reduce the rate of neuronal migration. By video-enhanced contrast differential interference contrast microscopy the effects of anti-astrotactin antibodies were seen to be rapid. Within fifteen minutes of antibody application, streaming of cytoplasmic organelles into the leading process arrested, the nucleus shifted from a caudal to a central position, and the extension of filopodia and lamellopodia along the leading process ceased. Correlated video and electron microscopy suggested that the mechanism of arrest by antiastrotactin antibodies involved the failure to form new adhesion sites along the leading process and the disorganization of cytoskeletal components. These results suggest astrotactin acts as a neuronal receptor for granule neuron migration along astroglial fibers.

Type IIa ('anti-Hu') antineuronal antibodies produce destruction of rat cerebellar granule neurons in vitro

Neurology ◽  
1993 ◽  
Vol 43 (10) ◽  
pp. 2049-2049 ◽  
Author(s):  
J. E. Greenlee ◽  
T. N. Parks ◽  
K. A. Jaeckle
Keyword(s):  
Cerebellar Granule Neurons ◽  
Granule Neurons ◽  
Cerebellar Granule ◽  
Antineuronal Antibodies

scholarly journals The GLUT3 glucose transporter is the predominant isoform in primary cultured neurons: assessment by biosynthetic and photoaffinity labelling

1994 ◽  
Vol 301 (2) ◽  
pp. 379-384 ◽  
Author(s):  
F Maher ◽  
I A Simpson
Keyword(s):  
Glucose Transporter ◽  
Dissociation Constants ◽  
Cerebellar Granule Neurons ◽  
Granule Neurons ◽  
Photoaffinity Labelling ◽  
Cerebellar Granule ◽  
Neuronal Membranes ◽  
Rat Brain Membranes ◽  
Surface Labelling

Cerebellar granule neurons in primary culture express increasing levels of two glucose transporter isoforms, GLUT1 and GLUT3, as they differentiate in vitro. We have determined the relative abundance of GLUT1 and GLUT3 in these neurons by three different labelling methods. (1) Photoaffinity cell surface labelling of neurons with an impermeant bis-mannose photolabel revealed 6-10-fold more GLUT3 than GLUT1 and dissociation constants (Kd) for the photolabel of 55-68 microM (GLUT3) and 146-169 microM (GLUT1). Binding to both transporters was inhibited by cytochalasin B. (2) Photoaffinity labelling of neuronal membranes with a permeant forskolin derivative showed 5.5-8-fold more GLUT3 than GLUT1, whereas in rat brain membranes containing both neuronal and glial membranes, GLUT3 and GLUT1 were detected in similar proportions. (3) Biosynthetic labelling of neurons with [35S]methionine and [35S]cysteine showed GLUT3 to be 6-10-fold more abundant than GLUT1. Thus GLUT3 is quantitatively the predominant glucose-transport isoform in cultured cerebellar granule neurons.

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