PMID- 10085414
OWN - NLM
STAT- MEDLINE
DCOM- 19990430
LR  - 20190516
IS  - 1107-3756 (Print)
IS  - 1107-3756 (Linking)
VI  - 3
IP  - 4
DP  - 1999 Apr
TI  - Plasticity-related serine proteases in the brain (review).
PG  - 405-9
AB  - Serine proteases exert a variety of functions in the body; food digestion,
      regulation of other proteins and modification of extracellular matrix. Cumulative
      evidence has shown the importance of serine proteases in the nervous system as
      well. It has been shown that three serine proteases, thrombin, plasminogen
      activators and neuropsin, have functional roles in neural plasticity. Most of the
      actions of thrombin are thought to be mediated by its specific receptors.
      Thrombin reverses neurite outgrowth of serum-deprived neuroblastoma cells, and
      induces protective and apoptotic effects on neurons and glial cells depending on 
      concentration and time. Tissue-type and urokinase-type plasminogen activators
      (tPA and uPA) distribute broadly in the brain. tPA and uPA exert a variety of
      functions during development. These proteases also function in long-term
      potentiation and kindling formation. Furthermore, tPA is essential to excitotoxic
      neuronal cell death. Neuropsin is a serine protease expressed in the limbic
      system of the brain. Kindling induced neuropsin mRNA and protein expression and
      anti-neuropsin antibody ameliorates kindling epilepsy. The possible roles of
      these proteases in neural plasticity are reviewed here.
FAU - Yoshida, S
AU  - Yoshida S
AD  - Division of Structural Cell Biology, Nara Institute of Science and Technology,
      Ikoma, Nara 630-0101, Japan.
FAU - Shiosaka, S
AU  - Shiosaka S
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Greece
TA  - Int J Mol Med
JT  - International journal of molecular medicine
JID - 9810955
RN  - 0 (Receptors, Thrombin)
RN  - 0 (protease-activated receptor 3)
RN  - 9001-91-6 (Plasminogen)
RN  - EC 3.4.21.- (KLK8 protein, human)
RN  - EC 3.4.21.- (Kallikreins)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.5 (Thrombin)
RN  - EC 3.4.21.68 (Tissue Plasminogen Activator)
RN  - EC 3.4.21.73 (Urokinase-Type Plasminogen Activator)
SB  - IM
MH  - Animals
MH  - Brain/*physiology
MH  - Humans
MH  - *Kallikreins
MH  - Neuronal Plasticity/*physiology
MH  - Plasminogen/physiology
MH  - Receptors, Thrombin/metabolism
MH  - Serine Endopeptidases/*physiology
MH  - Thrombin/physiology
MH  - Tissue Plasminogen Activator/metabolism
MH  - Urokinase-Type Plasminogen Activator/metabolism
RF  - 55
EDAT- 1999/03/23 00:00
MHDA- 1999/03/23 00:01
CRDT- 1999/03/23 00:00
PHST- 1999/03/23 00:00 [pubmed]
PHST- 1999/03/23 00:01 [medline]
PHST- 1999/03/23 00:00 [entrez]
AID - 10.3892/ijmm.3.4.405 [doi]
PST - ppublish
SO  - Int J Mol Med. 1999 Apr;3(4):405-9. doi: 10.3892/ijmm.3.4.405.