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

• Autorzy: Zhang J. , Dai J. , Zhao E. , Lin Y. , Zeng L. , Chen J. , Zheng H. , Wang Y. , Li X. , Ying K. , Xie Y. , Mao Y.
• Języki publikacji: EN

Abstrakty

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.

Słowa kluczowe

EN

man; gene expression; cDNA cloning; gene organization; peptidylarginine deiminase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 4
• Opis fizyczny: p.1051-1058,fig.,ref.

Twórcy

autor

Zhang J.

• Fudan University, Shanghai 200433, P.R.China

autor

Dai J.

autor

Zhao E.

autor

Lin Y.

autor

Zeng L.

autor

Chen J.

autor

Zheng H.

autor

Wang Y.

autor

Li X.

autor

Ying K.

autor

Xie Y.

autor

Mao Y.

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