Apoptosis and the response to anticancer therapy

Benjamin M F Mow, April L. Blajeski, Joya Chandra, Scott H Kaufmann

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

Apoptosis is a distinctive form of cell death that reflects cleavage of a subset of intracellular polypeptides by proteases known as caspases. Two major intracellular caspase cascades, one activated predominately by death receptor ligands and the other triggered by various cellular stresses, including DNA damage and microtubule disruption, have been delineated. Activation of these protease cascades is tightly regulated by a number of polypeptides, including Bcl-2 family members, inhibitor of apoptosis proteins, and several protein kinases. The demonstration that many antineoplastic agents induce apoptosis in susceptible cells raises the possibility that factors affecting caspase activation and activity might be important determinants of anticancer drug sensitivity. Here, we review recent studies describing the regulation of apoptotic pathways and identify potential implications of these findings for resistance to antineoplastic agents.

Original languageEnglish (US)
Pages (from-to)453-462
Number of pages10
JournalCurrent Opinion in Oncology
Volume13
Issue number6
DOIs
StatePublished - 2001

Fingerprint

Caspases
Apoptosis
Neoplasm Drug Resistance
Peptide Hydrolases
Inhibitor of Apoptosis Proteins
Death Domain Receptors
Peptides
Microtubules
Antineoplastic Agents
Protein Kinases
DNA Damage
Cell Death
Therapeutics
Ligands
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Cancer Research

Cite this

Apoptosis and the response to anticancer therapy. / Mow, Benjamin M F; Blajeski, April L.; Chandra, Joya; Kaufmann, Scott H.

In: Current Opinion in Oncology, Vol. 13, No. 6, 2001, p. 453-462.

Research output: Contribution to journalArticle

Mow, Benjamin M F ; Blajeski, April L. ; Chandra, Joya ; Kaufmann, Scott H. / Apoptosis and the response to anticancer therapy. In: Current Opinion in Oncology. 2001 ; Vol. 13, No. 6. pp. 453-462.
@article{9cc353463a9041c0ae3768220fb2d555,
title = "Apoptosis and the response to anticancer therapy",
abstract = "Apoptosis is a distinctive form of cell death that reflects cleavage of a subset of intracellular polypeptides by proteases known as caspases. Two major intracellular caspase cascades, one activated predominately by death receptor ligands and the other triggered by various cellular stresses, including DNA damage and microtubule disruption, have been delineated. Activation of these protease cascades is tightly regulated by a number of polypeptides, including Bcl-2 family members, inhibitor of apoptosis proteins, and several protein kinases. The demonstration that many antineoplastic agents induce apoptosis in susceptible cells raises the possibility that factors affecting caspase activation and activity might be important determinants of anticancer drug sensitivity. Here, we review recent studies describing the regulation of apoptotic pathways and identify potential implications of these findings for resistance to antineoplastic agents.",
author = "Mow, {Benjamin M F} and Blajeski, {April L.} and Joya Chandra and Kaufmann, {Scott H}",
year = "2001",
doi = "10.1097/00001622-200111000-00007",
language = "English (US)",
volume = "13",
pages = "453--462",
journal = "Current Opinion in Oncology",
issn = "1040-8746",
publisher = "Lippincott Williams and Wilkins",
number = "6",

}

TY - JOUR

T1 - Apoptosis and the response to anticancer therapy

AU - Mow, Benjamin M F

AU - Blajeski, April L.

AU - Chandra, Joya

AU - Kaufmann, Scott H

PY - 2001

Y1 - 2001

N2 - Apoptosis is a distinctive form of cell death that reflects cleavage of a subset of intracellular polypeptides by proteases known as caspases. Two major intracellular caspase cascades, one activated predominately by death receptor ligands and the other triggered by various cellular stresses, including DNA damage and microtubule disruption, have been delineated. Activation of these protease cascades is tightly regulated by a number of polypeptides, including Bcl-2 family members, inhibitor of apoptosis proteins, and several protein kinases. The demonstration that many antineoplastic agents induce apoptosis in susceptible cells raises the possibility that factors affecting caspase activation and activity might be important determinants of anticancer drug sensitivity. Here, we review recent studies describing the regulation of apoptotic pathways and identify potential implications of these findings for resistance to antineoplastic agents.

AB - Apoptosis is a distinctive form of cell death that reflects cleavage of a subset of intracellular polypeptides by proteases known as caspases. Two major intracellular caspase cascades, one activated predominately by death receptor ligands and the other triggered by various cellular stresses, including DNA damage and microtubule disruption, have been delineated. Activation of these protease cascades is tightly regulated by a number of polypeptides, including Bcl-2 family members, inhibitor of apoptosis proteins, and several protein kinases. The demonstration that many antineoplastic agents induce apoptosis in susceptible cells raises the possibility that factors affecting caspase activation and activity might be important determinants of anticancer drug sensitivity. Here, we review recent studies describing the regulation of apoptotic pathways and identify potential implications of these findings for resistance to antineoplastic agents.

UR - http://www.scopus.com/inward/record.url?scp=0034765627&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034765627&partnerID=8YFLogxK

U2 - 10.1097/00001622-200111000-00007

DO - 10.1097/00001622-200111000-00007

M3 - Article

C2 - 11673685

AN - SCOPUS:0034765627

VL - 13

SP - 453

EP - 462

JO - Current Opinion in Oncology

JF - Current Opinion in Oncology

SN - 1040-8746

IS - 6

ER -