Yamakoshi A, Ono H, Nishijyo T, Shiraiwa M, Takahara H
Department of Applied Biological Resource Sciences, School of Agriculture, Ibaraki University, Ami-machi, Inashiki-gun, Ibaraki 300-0393, Japan.
Biochim Biophys Acta. 1998 Jul 28;1386(1):227-32. doi: 10.1016/s0167-4838(98)00084-3.
We isolated a new clone that showed structural similarities with the rat peptidylarginine deiminase (PAD) types II and III. The full-length cDNA sequence of this novel PAD comprised 1998 bp encoding a sequence for 666 amino acid residues (Mr 74467), a 3'-non-coding region of 115 bp and a 5'-non-coding region of 16 bp. The derived amino acid sequence of the PAD showed 51.1 and 54.0% identities with the sequences of types II and III, respectively. Semi-quantitative reverse transcription-polymerase chain reaction (RT-PCR) assays of mRNAs from several tissues of rat indicated that the PAD message is highly expressed in the pancreas, spleen, and ovary and, less strongly expressed in the liver, lung, stomach, kidney, uterus, and dermis, and weakly expressed in the brain, heart and epidermis. Since this expression pattern was quite different from those of the previously reported PAD types I, II, and III, we designated this novel PAD as type IV.
