| Literature DB >> 16503113 |
Fumihiko Osuka1, Yuichi Endo, Mitsunori Higuchi, Hiroyuki Suzuki, Yutaka Shio, Koichi Fujiu, Ryuzo Kanno, Akio Oishi, Masanori Terashima, Teizo Fujita, Mitsukazu Gotoh.
Abstract
Decay-accelerating factor (DAF) is one of the complement regulatory proteins. Two isoforms of DAF have been identified in humans. In this study, we isolated novel cDNAs encoding five isoforms of DAF from the human lung, which were generated by insertion of new exonic sequences. RT-PCR revealed that all isoforms were expressed in almost all tissues tested, although the expression patterns and levels differed among the tissues. Transfection of isoform vDAF1, 2, and 3 cDNAs into CHO cells showed that these molecules are soluble forms secreted after glycosylation. Isoform vDAF4 and vDAF5 cDNAs included a part of and the entire intron 7 sequence, respectively, and the transfection of vDAF4 cDNA produced a large, glycosylated, membrane-bound form. These results suggest that more than seven isoforms of human DAF are involved in the regulation of complement activation under physiological conditions through their specific structures and localization.Entities:
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Year: 2006 PMID： 16503113 DOI： 10.1016/j.ygeno.2006.01.006
Source DB: PubMed Journal: Genomics ISSN： 0888-7543 Impact factor: 5.736