Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions

Research output: Contribution to journalReview article

90 Citations (Scopus)

Abstract

Several serine proteases including thrombin, tissue-type plasminogen activator and urokinase-type plasminogen activator have been well characterized in the brain. In this article, we review the brain-related trypsin and trypsin-like serine proteases. Accumulating evidence demonstrates that trypsin and trypsin-like serine proteases play very important roles in neural development, plasticity, neurodegeneration and neuroregeneration in the brain. Neuropsin is able to hydrolyze the extracellular matrix components by its active site serine, and regulates learning and memory in normal brain. The mutant neurotrypsin contributes to mental retardation in children. Neurosin seems to be involved in the pathogenesis of neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease or multiple sclerosis. Although mesotrypsin/trypsin IV is also implicated in neurodegeneration, its functional significance still remains largely unknown. Particularly, mesotrypsin/trypsin IV, P22 and neurosin exert their physiological and pathological functions through activation of certain protease-activated receptors (PARs). In the brain, the presence of serpins controls the activity of serine proteases. Therefore, understanding the interaction among brain trypsin, serpins and PARs will provide invaluable tools for regulating normal brain functions and for the clinical treatment of neural disorders.

Original languageEnglish (US)
Pages (from-to)237-252
Number of pages16
JournalCellular and Molecular Life Sciences
Volume65
Issue number2
DOIs
StatePublished - Jan 1 2008

Fingerprint

Trypsin
Proteolysis
Peptide Hydrolases
Brain
Proteinase-Activated Receptors
Serpins
Serine Proteases
Neuronal Plasticity
Urokinase-Type Plasminogen Activator
Tissue Plasminogen Activator
Thrombin
Intellectual Disability
Neurodegenerative Diseases
Serine
Multiple Sclerosis
Extracellular Matrix
Parkinson Disease
Catalytic Domain
Alzheimer Disease
Learning

Keywords

  • Central nervous system
  • Neurodegeneration
  • Plasticity
  • Proteolytic activity
  • Serine protease

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

Cite this

Trypsin and trypsin-like proteases in the brain : Proteolysis and cellular functions. / Wang, Yingfei; Luo, Weibo; Reiser, G.

In: Cellular and Molecular Life Sciences, Vol. 65, No. 2, 01.01.2008, p. 237-252.

Research output: Contribution to journalReview article

@article{b61a7b94f6134eeda40775bcb2a2c4fa,
title = "Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions",
abstract = "Several serine proteases including thrombin, tissue-type plasminogen activator and urokinase-type plasminogen activator have been well characterized in the brain. In this article, we review the brain-related trypsin and trypsin-like serine proteases. Accumulating evidence demonstrates that trypsin and trypsin-like serine proteases play very important roles in neural development, plasticity, neurodegeneration and neuroregeneration in the brain. Neuropsin is able to hydrolyze the extracellular matrix components by its active site serine, and regulates learning and memory in normal brain. The mutant neurotrypsin contributes to mental retardation in children. Neurosin seems to be involved in the pathogenesis of neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease or multiple sclerosis. Although mesotrypsin/trypsin IV is also implicated in neurodegeneration, its functional significance still remains largely unknown. Particularly, mesotrypsin/trypsin IV, P22 and neurosin exert their physiological and pathological functions through activation of certain protease-activated receptors (PARs). In the brain, the presence of serpins controls the activity of serine proteases. Therefore, understanding the interaction among brain trypsin, serpins and PARs will provide invaluable tools for regulating normal brain functions and for the clinical treatment of neural disorders.",
keywords = "Central nervous system, Neurodegeneration, Plasticity, Proteolytic activity, Serine protease",
author = "Yingfei Wang and Weibo Luo and G. Reiser",
year = "2008",
month = "1",
day = "1",
doi = "10.1007/s00018-007-7288-3",
language = "English (US)",
volume = "65",
pages = "237--252",
journal = "Cellular and Molecular Life Sciences",
issn = "1420-682X",
publisher = "Birkhauser Verlag Basel",
number = "2",

}

TY - JOUR

T1 - Trypsin and trypsin-like proteases in the brain

T2 - Proteolysis and cellular functions

AU - Wang, Yingfei

AU - Luo, Weibo

AU - Reiser, G.

PY - 2008/1/1

Y1 - 2008/1/1

N2 - Several serine proteases including thrombin, tissue-type plasminogen activator and urokinase-type plasminogen activator have been well characterized in the brain. In this article, we review the brain-related trypsin and trypsin-like serine proteases. Accumulating evidence demonstrates that trypsin and trypsin-like serine proteases play very important roles in neural development, plasticity, neurodegeneration and neuroregeneration in the brain. Neuropsin is able to hydrolyze the extracellular matrix components by its active site serine, and regulates learning and memory in normal brain. The mutant neurotrypsin contributes to mental retardation in children. Neurosin seems to be involved in the pathogenesis of neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease or multiple sclerosis. Although mesotrypsin/trypsin IV is also implicated in neurodegeneration, its functional significance still remains largely unknown. Particularly, mesotrypsin/trypsin IV, P22 and neurosin exert their physiological and pathological functions through activation of certain protease-activated receptors (PARs). In the brain, the presence of serpins controls the activity of serine proteases. Therefore, understanding the interaction among brain trypsin, serpins and PARs will provide invaluable tools for regulating normal brain functions and for the clinical treatment of neural disorders.

AB - Several serine proteases including thrombin, tissue-type plasminogen activator and urokinase-type plasminogen activator have been well characterized in the brain. In this article, we review the brain-related trypsin and trypsin-like serine proteases. Accumulating evidence demonstrates that trypsin and trypsin-like serine proteases play very important roles in neural development, plasticity, neurodegeneration and neuroregeneration in the brain. Neuropsin is able to hydrolyze the extracellular matrix components by its active site serine, and regulates learning and memory in normal brain. The mutant neurotrypsin contributes to mental retardation in children. Neurosin seems to be involved in the pathogenesis of neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease or multiple sclerosis. Although mesotrypsin/trypsin IV is also implicated in neurodegeneration, its functional significance still remains largely unknown. Particularly, mesotrypsin/trypsin IV, P22 and neurosin exert their physiological and pathological functions through activation of certain protease-activated receptors (PARs). In the brain, the presence of serpins controls the activity of serine proteases. Therefore, understanding the interaction among brain trypsin, serpins and PARs will provide invaluable tools for regulating normal brain functions and for the clinical treatment of neural disorders.

KW - Central nervous system

KW - Neurodegeneration

KW - Plasticity

KW - Proteolytic activity

KW - Serine protease

UR - http://www.scopus.com/inward/record.url?scp=38549103718&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=38549103718&partnerID=8YFLogxK

U2 - 10.1007/s00018-007-7288-3

DO - 10.1007/s00018-007-7288-3

M3 - Review article

C2 - 17965832

AN - SCOPUS:38549103718

VL - 65

SP - 237

EP - 252

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-682X

IS - 2

ER -