Circulating Peptidome and Tumor-Resident Proteolysis

Jia Fan, Bo Ning, Christopher J. Lyon, Ye Hu

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Citations (Scopus)

Abstract

Mammalian proteases segregate into several distinct protein families that employ different functional domains to hydrolyze peptides bonds with different specificities and affinities. These enzymes play central roles in critical cellular and systemic processes, including regulation of cell growth, differentiation, homeostasis, and apoptosis; and cancer initiation, progression, and metastasis. Human proteases segregate into five distinct catalytic classes; the metalloprotease, serine protease, and cysteine protease families have the most members, while the aspartic and threonine peptidase families have relatively few examples. Section 1 discusses the five different types of human proteases and summarizes some of their known functions during tumorigenesis, migration, and metastasis. Section 2 focuses on how cancer degradomes, defined as all the proteases, protease inhibitors, and protease substrates regulated by a given cancer, affect cancer promotion and suppression, and current approaches for degradome profiling. Protein degradation products generated during cancer progression, invasion, and metastasis alter the tumor microenvironment to influence these processes. These cancer-associated protein degradation profiles (aka tumor peptidomes) represent a potentially rich pool of candidates for cancer biomarker discovery. Section 3 focuses on the benefits and challenges associated with peptidome studies, and methods employed to conduct them. Section 4 discusses recent studies that use circulating peptides as cancer biomarkers, and how the abundance of peptides reflects the activity of their source proteases during cancer progression. We hope this chapter will convey a good sense of current research on how cancer-associated proteases, degradomes, and their resulting peptidomes can improve our knowledge of cancer biology, improve diagnosis and evaluation, and inspire new ideas in this and related research areas.

Original languageEnglish (US)
Title of host publicationEnzymes
PublisherAcademic Press
Pages1-25
Number of pages25
DOIs
StatePublished - Jan 1 2017

Publication series

NameEnzymes
Volume42
ISSN (Print)1874-6047

Fingerprint

Proteolysis
Tumors
Peptide Hydrolases
Neoplasms
Tumor Biomarkers
Peptides
Neoplasm Metastasis
Degradation
Proteins
Cysteine Proteases
Cell growth
Metalloproteases
Serine Proteases
Threonine
Protease Inhibitors
Tumor Microenvironment
Research
Apoptosis
Cell Differentiation
Carcinogenesis

Keywords

  • Cancer
  • Degradome
  • Mass spectrometry
  • Nanopore
  • Peptidome
  • Protease
  • Proteolysis

ASJC Scopus subject areas

  • Biotechnology
  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Fan, J., Ning, B., Lyon, C. J., & Hu, Y. (2017). Circulating Peptidome and Tumor-Resident Proteolysis. In Enzymes (pp. 1-25). (Enzymes; Vol. 42). Academic Press. https://doi.org/10.1016/bs.enz.2017.08.001

Circulating Peptidome and Tumor-Resident Proteolysis. / Fan, Jia; Ning, Bo; Lyon, Christopher J.; Hu, Ye.

Enzymes. Academic Press, 2017. p. 1-25 (Enzymes; Vol. 42).

Research output: Chapter in Book/Report/Conference proceedingChapter

Fan, Jia ; Ning, Bo ; Lyon, Christopher J. ; Hu, Ye. / Circulating Peptidome and Tumor-Resident Proteolysis. Enzymes. Academic Press, 2017. pp. 1-25 (Enzymes).
@inbook{ed18fd86863344b48b9c3126075ac504,
title = "Circulating Peptidome and Tumor-Resident Proteolysis",
abstract = "Mammalian proteases segregate into several distinct protein families that employ different functional domains to hydrolyze peptides bonds with different specificities and affinities. These enzymes play central roles in critical cellular and systemic processes, including regulation of cell growth, differentiation, homeostasis, and apoptosis; and cancer initiation, progression, and metastasis. Human proteases segregate into five distinct catalytic classes; the metalloprotease, serine protease, and cysteine protease families have the most members, while the aspartic and threonine peptidase families have relatively few examples. Section 1 discusses the five different types of human proteases and summarizes some of their known functions during tumorigenesis, migration, and metastasis. Section 2 focuses on how cancer degradomes, defined as all the proteases, protease inhibitors, and protease substrates regulated by a given cancer, affect cancer promotion and suppression, and current approaches for degradome profiling. Protein degradation products generated during cancer progression, invasion, and metastasis alter the tumor microenvironment to influence these processes. These cancer-associated protein degradation profiles (aka tumor peptidomes) represent a potentially rich pool of candidates for cancer biomarker discovery. Section 3 focuses on the benefits and challenges associated with peptidome studies, and methods employed to conduct them. Section 4 discusses recent studies that use circulating peptides as cancer biomarkers, and how the abundance of peptides reflects the activity of their source proteases during cancer progression. We hope this chapter will convey a good sense of current research on how cancer-associated proteases, degradomes, and their resulting peptidomes can improve our knowledge of cancer biology, improve diagnosis and evaluation, and inspire new ideas in this and related research areas.",
keywords = "Cancer, Degradome, Mass spectrometry, Nanopore, Peptidome, Protease, Proteolysis",
author = "Jia Fan and Bo Ning and Lyon, {Christopher J.} and Ye Hu",
year = "2017",
month = "1",
day = "1",
doi = "10.1016/bs.enz.2017.08.001",
language = "English (US)",
series = "Enzymes",
publisher = "Academic Press",
pages = "1--25",
booktitle = "Enzymes",

}

TY - CHAP

T1 - Circulating Peptidome and Tumor-Resident Proteolysis

AU - Fan, Jia

AU - Ning, Bo

AU - Lyon, Christopher J.

AU - Hu, Ye

PY - 2017/1/1

Y1 - 2017/1/1

N2 - Mammalian proteases segregate into several distinct protein families that employ different functional domains to hydrolyze peptides bonds with different specificities and affinities. These enzymes play central roles in critical cellular and systemic processes, including regulation of cell growth, differentiation, homeostasis, and apoptosis; and cancer initiation, progression, and metastasis. Human proteases segregate into five distinct catalytic classes; the metalloprotease, serine protease, and cysteine protease families have the most members, while the aspartic and threonine peptidase families have relatively few examples. Section 1 discusses the five different types of human proteases and summarizes some of their known functions during tumorigenesis, migration, and metastasis. Section 2 focuses on how cancer degradomes, defined as all the proteases, protease inhibitors, and protease substrates regulated by a given cancer, affect cancer promotion and suppression, and current approaches for degradome profiling. Protein degradation products generated during cancer progression, invasion, and metastasis alter the tumor microenvironment to influence these processes. These cancer-associated protein degradation profiles (aka tumor peptidomes) represent a potentially rich pool of candidates for cancer biomarker discovery. Section 3 focuses on the benefits and challenges associated with peptidome studies, and methods employed to conduct them. Section 4 discusses recent studies that use circulating peptides as cancer biomarkers, and how the abundance of peptides reflects the activity of their source proteases during cancer progression. We hope this chapter will convey a good sense of current research on how cancer-associated proteases, degradomes, and their resulting peptidomes can improve our knowledge of cancer biology, improve diagnosis and evaluation, and inspire new ideas in this and related research areas.

AB - Mammalian proteases segregate into several distinct protein families that employ different functional domains to hydrolyze peptides bonds with different specificities and affinities. These enzymes play central roles in critical cellular and systemic processes, including regulation of cell growth, differentiation, homeostasis, and apoptosis; and cancer initiation, progression, and metastasis. Human proteases segregate into five distinct catalytic classes; the metalloprotease, serine protease, and cysteine protease families have the most members, while the aspartic and threonine peptidase families have relatively few examples. Section 1 discusses the five different types of human proteases and summarizes some of their known functions during tumorigenesis, migration, and metastasis. Section 2 focuses on how cancer degradomes, defined as all the proteases, protease inhibitors, and protease substrates regulated by a given cancer, affect cancer promotion and suppression, and current approaches for degradome profiling. Protein degradation products generated during cancer progression, invasion, and metastasis alter the tumor microenvironment to influence these processes. These cancer-associated protein degradation profiles (aka tumor peptidomes) represent a potentially rich pool of candidates for cancer biomarker discovery. Section 3 focuses on the benefits and challenges associated with peptidome studies, and methods employed to conduct them. Section 4 discusses recent studies that use circulating peptides as cancer biomarkers, and how the abundance of peptides reflects the activity of their source proteases during cancer progression. We hope this chapter will convey a good sense of current research on how cancer-associated proteases, degradomes, and their resulting peptidomes can improve our knowledge of cancer biology, improve diagnosis and evaluation, and inspire new ideas in this and related research areas.

KW - Cancer

KW - Degradome

KW - Mass spectrometry

KW - Nanopore

KW - Peptidome

KW - Protease

KW - Proteolysis

UR - http://www.scopus.com/inward/record.url?scp=85030848611&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85030848611&partnerID=8YFLogxK

U2 - 10.1016/bs.enz.2017.08.001

DO - 10.1016/bs.enz.2017.08.001

M3 - Chapter

T3 - Enzymes

SP - 1

EP - 25

BT - Enzymes

PB - Academic Press

ER -