scholarly journals Consolidation of Memory After its Reactivation: Involvement of ß Noradrenergic Receptors in the Late Phase

1998 ◽  
Vol 6 (3) ◽  
pp. 63-68 ◽  
Author(s):  
Pascal Roullet ◽  
Susan Sara
Keyword(s):  
Late Phase ◽  
Long Term Memory ◽  
Control Groups ◽  
Camp Pathway ◽  
Noradrenergic Receptors ◽  
Element Binding Protein ◽  
Responsive Element ◽  
Camp Responsive Element Binding

Evidence is growing that the cAMP pathway through the cAMP responsive element binding protein (CREB) transcription factor plays an important role in long-term memory formation (LTM). To study the role of ß-noradrenergic receptors, positively linked to the cAMP secondmessenger system, in the dynamics of LTM processes, we used a memory-reactivation paradigm because recent studies in our laboratory confirmed that reactivated memory is labile and undergoes an extended reconsolidation process. In an eight-arm maze, rats were trained to choose the same three baited arms; 24 hr later, memory was reactivated and then the rats were injected intracerebroventricularly at 5 min, 30 min, 60 min, or 5 hr later with the ß-antagonist timolol or with saline. The results showed that injection of timolol induced amnesia only at the 60 min post-reactivation interval, whereas all control groups and groups that were timolol-injected at other post-reactivation intervals displayed optimal retention. The delayed amnesic action of timoloi suggests that ß noradrenergic receptors and the cAMP cascade are implicated in the late phase of reprocessing of a remembered event.

Deficient long-term memory in mice with a targeted mutation of the cAMP-responsive element-binding protein

Cell ◽  
1994 ◽  
Vol 79 (1) ◽  
pp. 59-68 ◽  
Author(s):  
Roussoudan Bourtchuladze ◽  
Bruno Frenguelli ◽  
Julie Blendy ◽  
Diana Cioffi ◽  
Gunther Schutz ◽  
...  
Keyword(s):  
Binding Protein ◽  
Long Term Memory ◽  
Term Memory ◽  
Targeted Mutation ◽  
Element Binding Protein ◽  
Responsive Element ◽  
Camp Responsive Element Binding

scholarly journals Long-Term Memory Deficits in Pavlovian Fear Conditioning in Ca2+/Calmodulin Kinase Kinase α-Deficient Mice

2006 ◽  
Vol 26 (23) ◽  
pp. 9105-9115 ◽  
Author(s):  
Frank Blaeser ◽  
Matthew J. Sanders ◽  
Nga Truong ◽  
Shanelle Ko ◽  
Long Jun Wu ◽  
...  
Keyword(s):  
Fear Conditioning ◽  
Long Term Potentiation ◽  
Long Term Memory ◽  
Term Memory ◽  
Calmodulin Kinase ◽  
Element Binding Protein ◽  
Long Term Follow Up ◽  
Responsive Element ◽  
Deficient Mice

ABSTRACT Signaling by the Ca2+/calmodulin kinase (CaMK) cascade has been implicated in neuronal gene transcription, synaptic plasticity, and long-term memory consolidation. The CaM kinase kinase α (CaMKKα) isoform is an upstream component of the CaMK cascade whose function in different behavioral and learning and memory paradigms was analyzed by targeted gene disruption in mice. CaMKKα mutants exhibited normal long-term spatial memory formation and cued fear conditioning but showed deficits in context fear during both conditioning and long-term follow-up testing. They also exhibited impaired activation of the downstream kinase CaMKIV/Gr and its substrate, the transcription factor cyclic AMP-responsive element binding protein (CREB) upon fear conditioning. Unlike CaMKIV/Gr-deficient mice, the CaMKKα mutants exhibited normal long-term potentiation and normal levels of anxiety-like behavior. These results demonstrate a selective role for CaMKKα in contextual fear memory and suggest that different combinations of upstream and downstream components of the CaMK cascade may serve distinct physiological functions.

scholarly journals Oiling the gears of memory: quercetin exposure during memory formation, consolidation, and recall enhances memory in Lymnaea stagnalis

2021 ◽  
Author(s):  
VERONICA RIVI ◽  
Anurada Batabyal ◽  
Cristina Benatti ◽  
Joan JMC Blom ◽  
Fabio Tascedda ◽  
...  
Keyword(s):  
Lymnaea Stagnalis ◽  
Memory Formation ◽  
Long Term Memory ◽  
Short Term ◽  
Extrinsic Factors ◽  
Element Binding Protein ◽  
Integral Process ◽  
Cyclic Amp Response Element

Memory formation (short-term, intermediate-term, and long-term) is an integral process of cognition which allows individuals to retain important information and is influenced by various intrinsic and extrinsic factors. A major extrinsic factor influencing cognition across taxa is diet, which may contain rich sources of molecular agents with antioxidant, anti-inflammatory, and memory enhancing properties that potentially enhance cognitive ability. A common and abundant flavonoid present in numerous food substances is quercetin (Q) which is also known to upregulate cyclic AMP response element binding protein (CREB) in several animals including our model system Lymnaea stagnalis. Since CREB is known to be involved in long term memory (LTM) formation, we investigated the role of Q-exposure on memory formation, consolidation, and recall during operant conditioning of aerial respiratory behaviour in Lymnaea. Snails were exposed to Q 3h before or after training to ascertain its effects on LTM. Additionally, we investigated the effect of the combined presentation of a single reinforcing stimulus (at 24h post-training or 24h before training) and Q-exposure on both LTM formation and reconsolidation. Our data indicate that Q-exposure acts on the different phases of memory formation, consolidation, and recall leading to enhanced LTM formation.

Role of CPEB-Family Proteins in Memory

2020 ◽  
Author(s):  
Kausik Si
Keyword(s):  
Molecular Mechanisms ◽  
Family Members ◽  
Long Term Memory ◽  
Cytoplasmic Polyadenylation ◽  
Element Binding Protein ◽  
The Face ◽  
Specific Mrnas ◽  
Over Time

A synapse-based mechanism of formation and persistence of long-term memory (LTM) entails some unique mechanistic challenges. It requires experience-dependent changes in synapse composition, function, and number. These changes must be specific to the synapse of interest, although all synapses in a neuron rely on the same genome. Finally, these changes must persist over time in the face of constant synaptic protein turnover. It has long been known that translation at the synapse is one of the fundamental requirements for LTM, and multiple mechanisms of synaptic translation have been characterized. Among these translation regulatory mechanisms, cytoplasmic polyadenylation element binding protein (CPEB) family members fulfill some of the unique needs of LTM and can even be considered as contributing to the biochemical substrates of memory. These proteins orchestrate a “synaptic mark” and regulate translation of specific mRNAs required for changes in synaptic composition, function, and number. Some CPEB family members also self-assemble and alter their function to maintain the altered synaptic state over time, contributing to persistence of memory. This chapter summarizes the known function of different CPEB family members in memory, their underlying molecular mechanisms, and important issues that remain to be resolved.

scholarly journals Degradation of Transcriptional Repressor ATF4 during Long-Term Synaptic Plasticity

2020 ◽  
Vol 21 (22) ◽  
pp. 8543
Author(s):  
Spencer G. Smith ◽  
Kathryn A. Haynes ◽  
Ashok N. Hegde
Keyword(s):  
Gene Expression ◽  
Synaptic Plasticity ◽  
Transcriptional Repressor ◽  
Long Term Potentiation ◽  
Long Term Memory ◽  
Activating Transcription Factor 4 ◽  
Element Binding Protein ◽  
Activating Transcription Factor ◽  
Responsive Element

Maintenance of long-term synaptic plasticity requires gene expression mediated by cAMP-responsive element binding protein (CREB). Gene expression driven by CREB can commence only if the inhibition by a transcriptional repressor activating transcription factor 4 (ATF4; also known as CREB2) is relieved. Previous research showed that the removal of ATF4 occurs through ubiquitin-proteasome-mediated proteolysis. Using chemically induced hippocampal long-term potentiation (cLTP) as a model system, we investigate the mechanisms that control ATF4 degradation. We observed that ATF4 phosphorylated at serine-219 increases upon induction of cLTP and decreases about 30 min thereafter. Proteasome inhibitor β-lactone prevents the decrease in ATF4. We found that the phosphorylation of ATF4 is mediated by cAMP-dependent protein kinase. Our initial experiments towards the identification of the ligase that mediates ubiquitination of ATF4 revealed a possible role for β-transducin repeat containing protein (β-TrCP). Regulation of ATF4 degradation is likely to be a mechanism for determining the threshold for gene expression underlying maintenance of long-term synaptic plasticity and by extension, long-term memory.

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