Cathepsin E: An Aspartic Protease with Diverse Functions and Biomedical Implications

Kenji Yamamoto; Kuniaki Okamoto; Takayuki Tsukuba

doi:10.1016/B978-0-12-821618-7.00206-6

Cathepsin E: An Aspartic Protease with Diverse Functions and Biomedical Implications

Kenji Yamamoto, Kuniaki Okamoto, Takayuki Tsukuba

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Aspartic peptidases are widely distributed among vertebrates, yeast, plants, fungi, bacteria, and viruses. Of these, the A1 family members, including cathepsin E and ß-secretase, are involved in specific and/or nonspecific degradation of proteins and peptides in intra- and/or extracellular spaces. Since the 2000s, cathepsin E and ß-secretase have received enormous interest because of their involvement in important biological processes and the close association of their abnormal expression and uncontrolled activity with human diseases. This review summarizes the current knowledge on biochemical properties and functions of cathepsin E and highlights the pathophysiological conditions caused by its deficiency.

Original language	English
Title of host publication	Encyclopedia of Cell Biology
Subtitle of host publication	Volume 1-6, Second Edition
Publisher	Elsevier
Pages	865-873
Number of pages	9
Volume	1
ISBN (Electronic)	9780128216248
DOIs	https://doi.org/10.1016/B978-0-12-821618-7.00206-6
Publication status	Published - Jan 1 2022

Keywords

Activation
Angiogenesis
Apoptosis
Aspartic peptidases
Cancer
Cathepsin E
Drugs
Endosomal/lysosomal system
Inhibitors
Neurodegeneration
Pathogenesis
Pepsin subfamily
Processing and trafficking
Proliferation and Signaling

ASJC Scopus subject areas

General Biochemistry,Genetics and Molecular Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/B978-0-12-821618-7.00206-6

Cite this

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title = "Cathepsin E: An Aspartic Protease with Diverse Functions and Biomedical Implications",

abstract = "Aspartic peptidases are widely distributed among vertebrates, yeast, plants, fungi, bacteria, and viruses. Of these, the A1 family members, including cathepsin E and {\ss}-secretase, are involved in specific and/or nonspecific degradation of proteins and peptides in intra- and/or extracellular spaces. Since the 2000s, cathepsin E and {\ss}-secretase have received enormous interest because of their involvement in important biological processes and the close association of their abnormal expression and uncontrolled activity with human diseases. This review summarizes the current knowledge on biochemical properties and functions of cathepsin E and highlights the pathophysiological conditions caused by its deficiency.",

keywords = "Activation, Angiogenesis, Apoptosis, Aspartic peptidases, Cancer, Cathepsin E, Drugs, Endosomal/lysosomal system, Inhibitors, Neurodegeneration, Pathogenesis, Pepsin subfamily, Processing and trafficking, Proliferation and Signaling",

author = "Kenji Yamamoto and Kuniaki Okamoto and Takayuki Tsukuba",

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T2 - An Aspartic Protease with Diverse Functions and Biomedical Implications

AU - Yamamoto, Kenji

AU - Okamoto, Kuniaki

AU - Tsukuba, Takayuki

PY - 2022/1/1

Y1 - 2022/1/1

N2 - Aspartic peptidases are widely distributed among vertebrates, yeast, plants, fungi, bacteria, and viruses. Of these, the A1 family members, including cathepsin E and ß-secretase, are involved in specific and/or nonspecific degradation of proteins and peptides in intra- and/or extracellular spaces. Since the 2000s, cathepsin E and ß-secretase have received enormous interest because of their involvement in important biological processes and the close association of their abnormal expression and uncontrolled activity with human diseases. This review summarizes the current knowledge on biochemical properties and functions of cathepsin E and highlights the pathophysiological conditions caused by its deficiency.

AB - Aspartic peptidases are widely distributed among vertebrates, yeast, plants, fungi, bacteria, and viruses. Of these, the A1 family members, including cathepsin E and ß-secretase, are involved in specific and/or nonspecific degradation of proteins and peptides in intra- and/or extracellular spaces. Since the 2000s, cathepsin E and ß-secretase have received enormous interest because of their involvement in important biological processes and the close association of their abnormal expression and uncontrolled activity with human diseases. This review summarizes the current knowledge on biochemical properties and functions of cathepsin E and highlights the pathophysiological conditions caused by its deficiency.

KW - Activation

KW - Angiogenesis

KW - Apoptosis

KW - Aspartic peptidases

KW - Cancer

KW - Cathepsin E

KW - Drugs

KW - Endosomal/lysosomal system

KW - Inhibitors

KW - Neurodegeneration

KW - Pathogenesis

KW - Pepsin subfamily

KW - Processing and trafficking

KW - Proliferation and Signaling

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DO - 10.1016/B978-0-12-821618-7.00206-6

M3 - Chapter

AN - SCOPUS:85158943453

VL - 1

SP - 865

EP - 873

BT - Encyclopedia of Cell Biology

PB - Elsevier

ER -

Cathepsin E: An Aspartic Protease with Diverse Functions and Biomedical Implications

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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