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

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Zhang J., Dai J., Zhao E., Lin Y., Zeng L., Chen J., Zheng H., Wang Y., Li X., Ying K., Xie Y., Mao Y.

vol. 51

issue 4

1051-1058

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.

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1 Acta Biochimica Polonica

1 2004

1 Chen J.

1 Dai J.

1 Li X.

1 Lin Y.

1 Mao Y.

1 Wang Y.

1 Xie Y.

1 Ying K.

1 Zeng L.

1 Zhang J.

1 Zhao E.

1 Zheng H.

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