Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity

Akihiro Ito, Takashi Uehara, Yasuyuki Nomura

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Members of the caspase family are essential executors of apoptosis. Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S. Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain. However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here, we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S. Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells. Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates. These results suggested that ISBP may be the mediator for the survival function of caspase-2S. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)360-364
Number of pages5
JournalFEBS Letters
Volume470
Issue number3
DOIs
Publication statusPublished - Mar 31 2000
Externally publishedYes

Fingerprint

Caspases
Carrier Proteins
Caspase 2
Calcium-Binding Proteins
Cell death
Cell Death
Cells
Apoptosis
EF Hand Motifs
Aptitude
Alternative Splicing
Glutathione Transferase
Integrins
Northern Blotting
Yeast
Anti-Idiotypic Antibodies
Cultured Cells
Brain
Cell Survival
Screening

Keywords

  • Apoptosis
  • Caspase-2
  • Caspase-2S
  • Ich-1S-binding protein

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity. / Ito, Akihiro; Uehara, Takashi; Nomura, Yasuyuki.

In: FEBS Letters, Vol. 470, No. 3, 31.03.2000, p. 360-364.

Research output: Contribution to journalArticle

@article{f1ea9fbdddc04aab870bbd8ed304dbc5,
title = "Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity",
abstract = "Members of the caspase family are essential executors of apoptosis. Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S. Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain. However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here, we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S. Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells. Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates. These results suggested that ISBP may be the mediator for the survival function of caspase-2S. Copyright (C) 2000 Federation of European Biochemical Societies.",
keywords = "Apoptosis, Caspase-2, Caspase-2S, Ich-1S-binding protein",
author = "Akihiro Ito and Takashi Uehara and Yasuyuki Nomura",
year = "2000",
month = "3",
day = "31",
doi = "10.1016/S0014-5793(00)01351-X",
language = "English",
volume = "470",
pages = "360--364",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity

AU - Ito, Akihiro

AU - Uehara, Takashi

AU - Nomura, Yasuyuki

PY - 2000/3/31

Y1 - 2000/3/31

N2 - Members of the caspase family are essential executors of apoptosis. Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S. Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain. However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here, we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S. Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells. Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates. These results suggested that ISBP may be the mediator for the survival function of caspase-2S. Copyright (C) 2000 Federation of European Biochemical Societies.

AB - Members of the caspase family are essential executors of apoptosis. Caspase-2 has two messenger RNAs generated by alternative splicing, which encode caspase-2L and caspase-2S. Although caspase-2L induces apoptosis, caspase-2S also has the ability to antagonize cell death. Experiments in caspase-2-deficient mice showed that caspase-2 functions to delay cell death in some neuronal populations, suggesting that caspase-2S dominantly acts for cell survival in the brain. However, the mechanism of caspase-2S-mediated anti-apoptotic effect is still unclear. Here, we isolated a protein that interacts with caspase-2S, designated as Ich-1S (caspase-2S)-binding protein (ISBP), by yeast two-hybrid screening using full-length caspase-2S cDNA as a bait. ISBP is identical to the recently isolated calcium and integrin-binding protein, and a small molecule calcium-binding protein with two EF-hand motifs of its C-terminus. In vitro transcribed and translated ISBP interacts specifically with glutathione-S-transferase-fused caspase-2S. Moreover, the interaction between ISBP and caspase-2S was observed in cultured cells. Northern blot analysis indicated that ISBP may be a ubiquitous protein. Interestingly, ISBP can partially inhibit the processing of pro-caspase-2L induced by anti-Fas antibody-treated Jurkat cytosolic lysates. These results suggested that ISBP may be the mediator for the survival function of caspase-2S. Copyright (C) 2000 Federation of European Biochemical Societies.

KW - Apoptosis

KW - Caspase-2

KW - Caspase-2S

KW - Ich-1S-binding protein

UR - http://www.scopus.com/inward/record.url?scp=0034737397&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034737397&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(00)01351-X

DO - 10.1016/S0014-5793(00)01351-X

M3 - Article

C2 - 10745097

AN - SCOPUS:0034737397

VL - 470

SP - 360

EP - 364

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -