Role of hsp70 in cancer growth and survival

Marcus P D Hatfield, Sándor Lovas

Research output: Contribution to journalReview article

16 Citations (Scopus)

Abstract

Hsp70 is a highly conserved protein that refolds misfolded proteins and has numerous housekeeping functions which regulate apoptosis and other cell activities. Hsp70 consists of a nucleotide binding domain which binds ATP and a substrate binding domain that binds misfolded proteins. The substrate binding domain contains a peptide binding pocket which is covered by a helical lid. In humans, there are three major cytosolic Hsp70 isotypes, Hsp70-8, Hsp70-1 and Hsp70-2. Leukemic and numerous other cancer cells have a greater amount of Hsp70-1 and -2, which help the cancer cells inhibit apoptosis in response to stress. This review summarizes the structure and role of Hsp70 proteins in cancer survival.

Original languageEnglish
Pages (from-to)616-624
Number of pages9
JournalProtein and Peptide Letters
Volume19
Issue number6
StatePublished - Jun 2012

Fingerprint

Survival
Growth
Protein Refolding
Apoptosis
Housekeeping
Neoplasms
Proteins
Cells
Substrates
Nucleotides
Adenosine Triphosphate
Peptides

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Structural Biology

Cite this

Role of hsp70 in cancer growth and survival. / Hatfield, Marcus P D; Lovas, Sándor.

In: Protein and Peptide Letters, Vol. 19, No. 6, 06.2012, p. 616-624.

Research output: Contribution to journalReview article

Hatfield, MPD & Lovas, S 2012, 'Role of hsp70 in cancer growth and survival', Protein and Peptide Letters, vol. 19, no. 6, pp. 616-624.
Hatfield, Marcus P D ; Lovas, Sándor. / Role of hsp70 in cancer growth and survival. In: Protein and Peptide Letters. 2012 ; Vol. 19, No. 6. pp. 616-624.
@article{a233735350694d38a3ba2d8a403a7ac0,
title = "Role of hsp70 in cancer growth and survival",
abstract = "Hsp70 is a highly conserved protein that refolds misfolded proteins and has numerous housekeeping functions which regulate apoptosis and other cell activities. Hsp70 consists of a nucleotide binding domain which binds ATP and a substrate binding domain that binds misfolded proteins. The substrate binding domain contains a peptide binding pocket which is covered by a helical lid. In humans, there are three major cytosolic Hsp70 isotypes, Hsp70-8, Hsp70-1 and Hsp70-2. Leukemic and numerous other cancer cells have a greater amount of Hsp70-1 and -2, which help the cancer cells inhibit apoptosis in response to stress. This review summarizes the structure and role of Hsp70 proteins in cancer survival.",
author = "Hatfield, {Marcus P D} and S{\'a}ndor Lovas",
year = "2012",
month = "6",
language = "English",
volume = "19",
pages = "616--624",
journal = "Protein and Peptide Letters",
issn = "0929-8665",
publisher = "Bentham Science Publishers B.V.",
number = "6",

}

TY - JOUR

T1 - Role of hsp70 in cancer growth and survival

AU - Hatfield, Marcus P D

AU - Lovas, Sándor

PY - 2012/6

Y1 - 2012/6

N2 - Hsp70 is a highly conserved protein that refolds misfolded proteins and has numerous housekeeping functions which regulate apoptosis and other cell activities. Hsp70 consists of a nucleotide binding domain which binds ATP and a substrate binding domain that binds misfolded proteins. The substrate binding domain contains a peptide binding pocket which is covered by a helical lid. In humans, there are three major cytosolic Hsp70 isotypes, Hsp70-8, Hsp70-1 and Hsp70-2. Leukemic and numerous other cancer cells have a greater amount of Hsp70-1 and -2, which help the cancer cells inhibit apoptosis in response to stress. This review summarizes the structure and role of Hsp70 proteins in cancer survival.

AB - Hsp70 is a highly conserved protein that refolds misfolded proteins and has numerous housekeeping functions which regulate apoptosis and other cell activities. Hsp70 consists of a nucleotide binding domain which binds ATP and a substrate binding domain that binds misfolded proteins. The substrate binding domain contains a peptide binding pocket which is covered by a helical lid. In humans, there are three major cytosolic Hsp70 isotypes, Hsp70-8, Hsp70-1 and Hsp70-2. Leukemic and numerous other cancer cells have a greater amount of Hsp70-1 and -2, which help the cancer cells inhibit apoptosis in response to stress. This review summarizes the structure and role of Hsp70 proteins in cancer survival.

UR - http://www.scopus.com/inward/record.url?scp=84861942110&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84861942110&partnerID=8YFLogxK

M3 - Review article

VL - 19

SP - 616

EP - 624

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

SN - 0929-8665

IS - 6

ER -