NDLI: Large complex formation of the inhibitor of caspase-activated DNase

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Apoptosis : Volume 10, Issue 2, March 2005

Apoptosis : Volume 10, Issue 1, January 2005

Large complex formation of the inhibitor of caspase-activated DNase

Content Provider	Springer Nature Link
Author	Kauchi, H. Nishizaki, H. Minatogawa, Y. Toné, S.
Copyright Year	2005
Abstract	Inhibitor of caspase-activated DNase (ICAD) is required for correctly folding of CAD and inhibits nuclease activity of CAD in non-apoptotic cells. From proteomic analysis of the ICAD binding proteins, we revealed that over-expressed flag-ICAD bound other ICAD molecules}. Purified recombinant ICAD protein showed three bands, 66 KDa, 132 KDa and 450 KDa, by native-PAGE. ICAD fused with glutathione-S-transferase (GST) was immunoprecipitated with anti-flag antibody from Jurkat cell lysates cotransfected with ICAD fused with either GST or flag expression vectors. When purified recombinant ICAD protein was separated by gel chromatography, the molecular weight of ICAD was detected at ∼440 and 45 K. ICAD in extracts of wild type Jurkat cells also existed at ∼440 and 45 K as measured by gel chromatography; so that fractions of CAD coincided with fractions of ∼440 K of ICAD. These results indicate that ICAD and/or CAD appeared to form large complexes in Jurkat cells.
Starting Page	651
Ending Page	656
Page Count	6
File Format	PDF
ISSN	13608185
Journal	Apoptosis
Volume Number	10
Issue Number	3
e-ISSN	1573675X
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	apoptosis CAD homooligomerization ICAD proteomic analysis Cancer Research Virology Oncology Biochemistry Cell Biology
Content Type	Text
Resource Type	Article
Subject	Pharmaceutical Science Biochemistry (medical) Cell Biology Clinical Biochemistry Cancer Research Pharmacology

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