scholarly journals Regulatory connection between the expression level of classical protein kinase C and pruning of climbing fibers from cerebellar Purkinje cells

2017 ◽  
Vol 143 (6) ◽  
pp. 660-670 ◽  
Author(s):  
Nobutaka Takahashi ◽  
Anton N. Shuvaev ◽  
Ayumu Konno ◽  
Yasunori Matsuzaki ◽  
Masashi Watanave ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Purkinje Cells ◽  
Climbing Fibers ◽  
Expression Level ◽  
Kinase C ◽  
Cerebellar Purkinje Cells ◽  
Regulatory Connection

Potentiation of NMDA receptor-mediated transmission in turtle cerebellar granule cells by activation of metabotropic glutamate receptors

1993 ◽  
Vol 69 (2) ◽  
pp. 585-594 ◽  
Author(s):  
G. A. Kinney ◽  
N. T. Slater
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase C ◽  
Nmda Receptor ◽  
Protein Kinase ◽  
Adenylate Cyclase ◽  
Purkinje Cells ◽  
Granule Cells ◽  
Metabotropic Glutamate ◽  
Kinase C ◽  
Cell Synapse

1. The effects of metabotropic glutamate receptor (mGluR) agonists on excitatory postsynaptic potentials (EPSPs) evoked by stimulation of mossy fibers (MF) and parallel fibers (PF) were examined in turtle cerebellar Purkinje cells. 2. The mGluR agonist 1S,3R-ACPD (1-25 microM) reversibly potentiated the amplitude of the MF-evoked EPSPs, but was without effect on PF-evoked EPSPs. The potentiation of MF-evoked EPSPs was dose-dependent, with a median effective dose (ED50) of approximately 4.4 microM. At higher doses (15-25 microM) 1S,3R-ACPD produced a direct depolarization of Purkinje cells in 58% of cells examined. 3. The enhancement of MF EPSPs by 1S,3R-ACPD was mimicked by 1S,3S-ACPD (50 microM) and blocked by the N-methyl-D-aspartate (NMDA) receptor antagonist D-2-amino-5-phosphonovalerate (D-AP5), but not by the mGluR antagonist L-2-amino-3-phosphonopionic acid (L-AP3; 1 mM), or the 1R,3S isomer of ACPD (25-500 microM). 4. Quisqualate (1 microM) produced a biphasic effect on MF EPSPs, producing an initial blockade of the EPSP followed by a D-AP5-sensitive potentiation. 5. The potentiation of MF EPSPs by 1S,3R-ACPD was not blocked by prior exposure to the protein kinase C activator phorbol 12-myristate 13-acetate (10 microM), the protein kinase C inhibitor calphostin C (1 microM), the adenylate cyclase activator forskolin (25 microM), or the nitric oxide donator sodium nitroprusside (1 mM). Preincubation of the tissue for 24-48 h in pertussis toxin also failed to prevent the ability of 1S,3R-ACPD to potentiate the NMDA receptor-mediated component of the MF EPSP. PF EPSPs were also not significantly affected by these agents. 6. The results demonstrate that the mGluR agonists 1S,3R-ACPD, 1S,3S-ACPD, and quisqualate produce a potent, stereospecific potentiation of NMDA receptor-mediated transmission at the MF-granule cell synapse. Agents that modulate the intracellular messengers protein kinase C, adenylate cyclase, nitric oxide, or pertussis toxin-sensitive G proteins failed to mimic or block this effect. This would suggest that the potentiation of NMDA receptor-mediated transmission at this synapse is not mediated via these systems, and reflects a different site of action of mGluR agonists on the NMDA receptor. The observed interaction between mGluR and NMDA receptors in granule cells provides a means for activity-dependent modulation of synaptic transmission, which may play a role in synaptic integration at the MF-granule cell synapse.

scholarly journals Electron microscopic localization of type I protein kinase C in rat Purkinje cells

1988 ◽  
Vol 8 (11) ◽  
pp. 4262-4268 ◽  
Author(s):  
A Kose ◽  
N Saito ◽  
H Ito ◽  
U Kikkawa ◽  
Y Nishizuka ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Purkinje Cells ◽  
Type I ◽  
Electron Microscopic ◽  
Microscopic Localization ◽  
Kinase C ◽  
Electron Microscopic Localization

scholarly journals Translation information processing is regulated by protein kinase C-dependent mechanism in Purkinje cells in murine posterior vermis

2020 ◽  
Vol 117 (29) ◽  
pp. 17348-17358
Author(s):  
Rosendo G. Hernández ◽  
Chris I. De Zeeuw ◽  
Ruyan Zhang ◽  
Tatyana A. Yakusheva ◽  
Pablo M. Blazquez
Keyword(s):  
Protein Kinase C ◽  
Information Processing ◽  
Protein Kinase ◽  
Purkinje Cell ◽  
Purkinje Cells ◽  
Semicircular Canals ◽  
Theoretical Work ◽  
Otolith Organs ◽  
Cell Responses ◽  
Kinase C

The cerebellar posterior vermis generates an estimation of our motion (translation) and orientation (tilt) in space using cues originating from semicircular canals and otolith organs. Theoretical work has laid out the basic computations necessary for this signal transformation, but details on the cellular loci and mechanisms responsible are lacking. Using a multicomponent modeling approach, we show that canal and otolith information are spatially and temporally matched in mouse posterior vermis Purkinje cells and that Purkinje cell responses combine translation and tilt information. Purkinje cell-specific inhibition of protein kinase C decreased and phase-shifted the translation component of Purkinje cell responses, but did not affect the tilt component. Our findings suggest that translation and tilt signals reach Purkinje cells via separate information pathways and that protein kinase C-dependent mechanisms regulate translation information processing in cerebellar cortex output neurons.

Sign in / Sign up

Export Citation Format

Share Document