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2004 | 51 | 4 | 1051-1058
Article title

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI.

Content
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Languages of publication
EN
Abstracts
EN
Peptidylarginine deiminase (PAD) catalyzes the post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Human, similar to rodents, has four isoforms of PAD (type I, II, III and IV/V), each of which is distinct in substrate specificity and tissue specific expression. In our large-scale sequencing project, we identified a new human PAD cDNA from a human fetal brain cDNA library. The putative protein encoded by this cDNA is designated hPADVI. Expression analysis of hPADVI showed that it is mainly expressed in adult human ovary and peripheral blood leukocytes. We conclude that hPADVI may be orthologous to mouse ePAD, basing on sequence comparison, chromosome localization and exon-intron structure analysis. PAD-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development. This study describes a new important member of the human PAD family.
Keywords
Publisher

Year
Volume
51
Issue
4
Pages
1051-1058
Physical description
Dates
published
2004
received
2004-01-13
revised
2004-10-26
accepted
2004-11-26
Contributors
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
author
  • State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, P. R. China
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv51i4p1051kz
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