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Cited by 88Neuroscience and Neuropharmacology ResearchCalpain Protease Function and RegulationProtease and Inhibitor Mechanisms

Proteases involved in long-term potentiation

Tomimatsu, Yoshiro, Idemoto, Satoru, Moriguchi, Shigeki, Watanabe, Shigenori, Nakanishi, Hiroshi·2002·Life Sciences
DOI 10.1016/s0024-3205(02)02285-3
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Abstract

Much attention has been paid to proteases involved in long-term potentiation (LTP). Calpains, Ca-dependent cysteine proteases, have first been demonstrated to be the mediator of LTP by the proteolytic cleavage of fodrin, which allows glutamate receptors located deep in the postsynaptic membrane to move to the surface. It is now generally considered that calpain activation is necessary for LTP formation in the cleavage of substrates such as protein kinase Czeta, NMDA receptors, and the glutamate receptor-interacting protein. Recent studies have shown that serine proteases such as tissue-type plasminogen activator (tPA), thrombin, and neuropsin are involved in LTP. tPA contributes to LTP by both receptor-mediated activation of cAMP-dependent protein kinase and the cleavage of NMDA receptors. Thrombin induces a proteolytic activation of PAR-1, resulting in activation of protein kinase C, which reduces the voltage-dependent Mg2+ blockade of NMDA receptor-channels. On the other hand, neuropsin may act as a regulatory molecule in LTP via its proteolytic degradation of extracellular matrix protein such as fibronectin. In addition to such neuronal proteases, proteases secreted from microglia such as tPA may also contribute to LTP. The enzymatic activity of each protease is strictly regulated by endogenous inhibitors and other factors in the brain. Once activated, proteases can irreversibly cleave peptide bonds. After cleavage, some substrates are inactivated and others are activated to gain new functions. Therefore, the issue to identify substrates for each protease is very important to understand the molecular basis of LTP.

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Crossref · 10.1016/s0024-3205(02)02285-3

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  • TBS causes the breakdown of actin crosslinking proteins in the subsynaptic cytoskeleton.

    “TBS, in addition to its actions on kinases, causes the breakdown of actin crosslinking proteins in the subsynaptic cytoskeleton; the relevant proteases also cleave transmembrane adhesion receptors that play a critical role in LTP-related actin polymerization (40–42).”

    From Synaptic evidence for the efficacy of spaced learning (2012) · cites this paper as [41]

  • The relevant proteases cleave transmembrane adhesion receptors that play a critical role in LTP-related actin polymerization.

    “TBS, in addition to its actions on kinases, causes the breakdown of actin crosslinking proteins in the subsynaptic cytoskeleton; the relevant proteases also cleave transmembrane adhesion receptors that play a critical role in LTP-related actin polymerization (40–42).”

    From Synaptic evidence for the efficacy of spaced learning (2012) · cites this paper as [41]

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Authors
Tomimatsu, Y., Idemoto, S., Moriguchi, S., Watanabe, S., & Nakanishi, H.
Affiliations
Kyushu University (JP)
Corresponding author
Nakanishi, Hiroshi
ORCID
Venue
Life Sciences
Publisher
Elsevier BV
Published
2002-12
Volume
72
Issue
4-5
Pages
355-361
ISSN
0024-3205 (ISSN-L)
DOI
10.1016/s0024-3205(02)02285-3
OpenAlex
W2096531725
Cited by
88
References
23
Citations by year
2025: 1 · 2019: 1 · 2018: 1 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 7
FWCI
1.98
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Life Sciences (publishedVersion)
  • PubMed (publishedVersion)
Funders
Ministry of Education, Culture, Sports, Science and Technology
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
long-term potentiation, proteolytic enzymes, calpain, serine protease, tissue plasminogen activator, thrombin, neuropsin, protein kinase C, protease-activated receptor 1, protein kinase A, glutamate receptor trafficking, spectrin, fibronectin, extracellular matrix, protease inhibitors, synaptic plasticity
MeSH terms
Animals, Calpain, Cysteine Endopeptidases, Humans, Kallikreins, Multienzyme Complexes, Endopeptidases, Tissue Plasminogen Activator, Serine Endopeptidases, Thrombin, Long-Term Potentiation, Proteasome Endopeptidase Complex

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