Murine Ortholog of ASC, a CARD-Containing Protein, Self-Associates and Exhibits Restricted Distribution in Developing Mouse Embryos

ASC (apoptosis-associated speck-like protein containing a CARD) was first identified as a cytosolic soluble protein that forms insoluble aggregates and enhances etoposide-induced apoptosis. We have cloned a murine ortholog of ASC (mASC) comprising 193 amino acids with a well-conserved pyrin N-termin...

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Bibliographic Details
Published in:Experimental cell research 2001-01, Vol.262 (2), p.128-133
Main Authors: Masumoto, Junya, Taniguchi, Shun'ichiro, Nakayama, Kohzo, Ayukawa, Koichi, Sagara, Junji
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Apaf-1
apoptosis
Apoptosis Regulatory Proteins
ASC
Base Sequence
Blotting, Northern
Brain - metabolism
CARD Signaling Adaptor Proteins
Cloning, Molecular
COS Cells
CRAD
Cytoskeletal Proteins - genetics
distribution
Embryo, Mammalian
embryos
Gene Expression Regulation, Developmental
In Situ Hybridization
Liver - metabolism
Mice
Mice, Inbred BALB C
Molecular Sequence Data
mouse
Myocardium - metabolism
oligomerization
Organ Specificity
Protein Binding
Sequence Homology, Amino Acid
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Summary:ASC (apoptosis-associated speck-like protein containing a CARD) was first identified as a cytosolic soluble protein that forms insoluble aggregates and enhances etoposide-induced apoptosis. We have cloned a murine ortholog of ASC (mASC) comprising 193 amino acids with a well-conserved pyrin N-terminal homology domain and caspase recruitment domain (CARD). mASC fused with green fluorescent protein appeared as a speck in transfected COS-7 cells and showed self-association. We analyzed mASC gene expression in developing embryos by in situ hybridization and found it to have a restricted distribution in mouse embryos. At E9.5, mASC was strongly expressed in the telencephalon, thalamic areas of the diencephalon, heart, and liver. Northern blotting analysis revealed that the mASC gene was expressed ubiquitously in multiple organs in adult mice. These findings indicate that mASC shows conservation of not only the primary structure of human ASC but also the ability to aggregate and has some similarity in its distribution to other CARD-containing molecules, including the apoptosis regulator Apaf-1.
ISSN:0014-4827
1090-2422
DOI:10.1006/excr.2000.5078