@article{oai:soar-ir.repo.nii.ac.jp:00003906,
 author = {Matsushita,  Kazuhiko and Takeoka,  Michiko and Sagara,  Junji and Itano,  Naoki and Kurose,  Yuka and Nakamura,  Akihiro and Taniguchi,  Shun'ichiro},
 journal = {Mediators of Inflammation},
 month = {},
 note = {Copyright (c) 2009 Kazuhiko Matsushita et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited., The apoptosis-associated speck-like protein containing a caspase recruit domain (ASC) is involved in apoptosis and innate immunity and is a major adaptor molecule responsible for procaspase-1 activation. ASC mRNA is encoded by three exons: exons 1 and 3 encode a pyrin domain (PYD) and caspase recruit domain (CARD), respectively, and exon 2 encodes a proline and glycine-rich (PGR) domain. Here, we identified a variant ASC protein (vASC) lacking the PGR domain that was smaller than full length ASC (fASC) derived from fully transcribed mRNA and searched for differences in biochemical and biological nature. Both fASC and vASC were found to activate procaspase-1 to a similar degree, but the efficiency of IL-1 beta excretion was significantly higher for vASC. There was also a marked structural difference observed in the fibrous aggregates formed by fASC and vASC. These results suggest that although the PGR domain is dispensable for procaspase-1 activation, it plays an important role in the regulation of the molecular structure and activity of ASC., Article, Mediators of Inflammation. 2009:287387 (2009)},
 title = {A Splice Variant of ASC Regulates IL-1 beta Release and Aggregates Differently from Intact ASC},
 volume = {2009},
 year = {2009}
}