HSP16.2 in cancers

S. Bellyei, Eva Pozsgai, B. Sümegi

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Homology of HSP16.2 to αB-crystallin, the induction of its synthesis to heat stress and its ATP-independent chaperone activity suggested that HSP16.2 is a novel small Heat Shock Protein. Suppression of HSP16.2 sensitized cells to apoptotic stimuli, while the over-expressing of HSP16.2 protected cells against H2O2 and taxol-induced cell death. Under stress conditions, HSP16.2 inhibited the release of cytochrome c from the mitochondria, nuclear translocation of AIF and endonuclease G, and caspase-3 activation by protecting the integrity of the mitochondrial membrane system. It was demonstrated that HSP16.2 interacts with HSP90, and that the presence of functionally active HSP90 is a prerequisite of the cytoprotective action of HSP16.2. HSP16.2 also facilitated lipid rafts formation, which could serves as scaffolds for the activation of Akt. The inhibition of PI-3-kinase-Akt pathway by LY-294002, or wortmannin, significantly decreased the cytoprotective effect of HSP16.2. These data indicate that one of the main mechanisms by which HSP16.2 inhibits apoptosis is through its interaction with functionally active HSP90, promoting lipid raft formation and the activation of PI-3-kinase-Akt cytoprotective pathway. Expression of HSP16.2 varies in different types of brain tumors and a positive correlation can be found between the tumor grade and the quantity of HSP16.2 in the tumor cells' cytoplasm. Thus, HSP16.2 may become a valuable marker for brain cancer diagnosis, or a possible target of cancer therapy.

Original languageEnglish
Title of host publicationSmall Stress Proteins and Human Diseases
PublisherNova Science Publishers, Inc.
Pages379-385
Number of pages7
ISBN (Print)9781614706366
Publication statusPublished - 2011

Fingerprint

Tumors
Chemical activation
Phosphatidylinositol 3-Kinases
Brain Neoplasms
Brain
Small Heat-Shock Proteins
Lipids
Neoplasms
Crystallins
2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one
Mitochondria
Mitochondrial Membranes
Cell death
Paclitaxel
Cytochromes c
Scaffolds
Caspase 3
Cytoplasm
Cell Death
Hot Temperature

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Bellyei, S., Pozsgai, E., & Sümegi, B. (2011). HSP16.2 in cancers. In Small Stress Proteins and Human Diseases (pp. 379-385). Nova Science Publishers, Inc..

HSP16.2 in cancers. / Bellyei, S.; Pozsgai, Eva; Sümegi, B.

Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc., 2011. p. 379-385.

Research output: Chapter in Book/Report/Conference proceedingChapter

Bellyei, S, Pozsgai, E & Sümegi, B 2011, HSP16.2 in cancers. in Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc., pp. 379-385.
Bellyei S, Pozsgai E, Sümegi B. HSP16.2 in cancers. In Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc. 2011. p. 379-385
Bellyei, S. ; Pozsgai, Eva ; Sümegi, B. / HSP16.2 in cancers. Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc., 2011. pp. 379-385
@inbook{af36be97fad24e0aafc52b4be808adad,
title = "HSP16.2 in cancers",
abstract = "Homology of HSP16.2 to αB-crystallin, the induction of its synthesis to heat stress and its ATP-independent chaperone activity suggested that HSP16.2 is a novel small Heat Shock Protein. Suppression of HSP16.2 sensitized cells to apoptotic stimuli, while the over-expressing of HSP16.2 protected cells against H2O2 and taxol-induced cell death. Under stress conditions, HSP16.2 inhibited the release of cytochrome c from the mitochondria, nuclear translocation of AIF and endonuclease G, and caspase-3 activation by protecting the integrity of the mitochondrial membrane system. It was demonstrated that HSP16.2 interacts with HSP90, and that the presence of functionally active HSP90 is a prerequisite of the cytoprotective action of HSP16.2. HSP16.2 also facilitated lipid rafts formation, which could serves as scaffolds for the activation of Akt. The inhibition of PI-3-kinase-Akt pathway by LY-294002, or wortmannin, significantly decreased the cytoprotective effect of HSP16.2. These data indicate that one of the main mechanisms by which HSP16.2 inhibits apoptosis is through its interaction with functionally active HSP90, promoting lipid raft formation and the activation of PI-3-kinase-Akt cytoprotective pathway. Expression of HSP16.2 varies in different types of brain tumors and a positive correlation can be found between the tumor grade and the quantity of HSP16.2 in the tumor cells' cytoplasm. Thus, HSP16.2 may become a valuable marker for brain cancer diagnosis, or a possible target of cancer therapy.",
author = "S. Bellyei and Eva Pozsgai and B. S{\"u}megi",
year = "2011",
language = "English",
isbn = "9781614706366",
pages = "379--385",
booktitle = "Small Stress Proteins and Human Diseases",
publisher = "Nova Science Publishers, Inc.",

}

TY - CHAP

T1 - HSP16.2 in cancers

AU - Bellyei, S.

AU - Pozsgai, Eva

AU - Sümegi, B.

PY - 2011

Y1 - 2011

N2 - Homology of HSP16.2 to αB-crystallin, the induction of its synthesis to heat stress and its ATP-independent chaperone activity suggested that HSP16.2 is a novel small Heat Shock Protein. Suppression of HSP16.2 sensitized cells to apoptotic stimuli, while the over-expressing of HSP16.2 protected cells against H2O2 and taxol-induced cell death. Under stress conditions, HSP16.2 inhibited the release of cytochrome c from the mitochondria, nuclear translocation of AIF and endonuclease G, and caspase-3 activation by protecting the integrity of the mitochondrial membrane system. It was demonstrated that HSP16.2 interacts with HSP90, and that the presence of functionally active HSP90 is a prerequisite of the cytoprotective action of HSP16.2. HSP16.2 also facilitated lipid rafts formation, which could serves as scaffolds for the activation of Akt. The inhibition of PI-3-kinase-Akt pathway by LY-294002, or wortmannin, significantly decreased the cytoprotective effect of HSP16.2. These data indicate that one of the main mechanisms by which HSP16.2 inhibits apoptosis is through its interaction with functionally active HSP90, promoting lipid raft formation and the activation of PI-3-kinase-Akt cytoprotective pathway. Expression of HSP16.2 varies in different types of brain tumors and a positive correlation can be found between the tumor grade and the quantity of HSP16.2 in the tumor cells' cytoplasm. Thus, HSP16.2 may become a valuable marker for brain cancer diagnosis, or a possible target of cancer therapy.

AB - Homology of HSP16.2 to αB-crystallin, the induction of its synthesis to heat stress and its ATP-independent chaperone activity suggested that HSP16.2 is a novel small Heat Shock Protein. Suppression of HSP16.2 sensitized cells to apoptotic stimuli, while the over-expressing of HSP16.2 protected cells against H2O2 and taxol-induced cell death. Under stress conditions, HSP16.2 inhibited the release of cytochrome c from the mitochondria, nuclear translocation of AIF and endonuclease G, and caspase-3 activation by protecting the integrity of the mitochondrial membrane system. It was demonstrated that HSP16.2 interacts with HSP90, and that the presence of functionally active HSP90 is a prerequisite of the cytoprotective action of HSP16.2. HSP16.2 also facilitated lipid rafts formation, which could serves as scaffolds for the activation of Akt. The inhibition of PI-3-kinase-Akt pathway by LY-294002, or wortmannin, significantly decreased the cytoprotective effect of HSP16.2. These data indicate that one of the main mechanisms by which HSP16.2 inhibits apoptosis is through its interaction with functionally active HSP90, promoting lipid raft formation and the activation of PI-3-kinase-Akt cytoprotective pathway. Expression of HSP16.2 varies in different types of brain tumors and a positive correlation can be found between the tumor grade and the quantity of HSP16.2 in the tumor cells' cytoplasm. Thus, HSP16.2 may become a valuable marker for brain cancer diagnosis, or a possible target of cancer therapy.

UR - http://www.scopus.com/inward/record.url?scp=84895405704&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84895405704&partnerID=8YFLogxK

M3 - Chapter

SN - 9781614706366

SP - 379

EP - 385

BT - Small Stress Proteins and Human Diseases

PB - Nova Science Publishers, Inc.

ER -