PMID- 10092850
OWN - NLM
STAT- MEDLINE
DCOM- 19990422
LR  - 20191210
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 259
IP  - 3
DP  - 1999 Feb
TI  - Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III
      and type IV, and the expression pattern of type I in mouse.
PG  - 660-9
AB  - Peptidylarginine deiminases (PADs), a group of post-translational enzymes,
      catalyze the conversion of protein-bound arginine residues to citrulline residues
      in a calcium ion-dependent manner and are widely distributed in various organs of
      vertebrates. Although the existence of four isoforms of PAD (types I, II, III,
      and IV) is reported in rodents, the relative functions of the isoforms with
      respect to their colocation in the tissues have yet to be explored. In this
      study, we cloned the full-length cDNA encoding mouse PAD type I by screening a
      uterine cDNA library and using the RACE method. This cDNA consists of an open
      reading frame of 1989 bases encoding 662 amino acids (73,823 Da), a
      5'-untranslated region of 127 bases and a 3'-untranslated region of 1639 bases.
      Comparative reverse transcription-PCR and Northern-blot analyses detected PAD
      type I mRNA only in the epidermis and uterus. Administration of estrogen to adult
      ovariectomized mice increased the content of PAD type I mRNA in the uterus,
      providing evidence that its expression is under the control of the sex steroid
      hormone. We also cloned the full-length cDNAs of mouse PAD type III and type IV
      by the reverse transcription-PCR and RACE methods. The primary structure of PAD
      type III contains 664 amino acids (75,098 Da) deduced from the coding region of
      1995 bases, and the primary structure of PAD type IV consists of 666 amino acids 
      (74,475 Da) deduced from the coding region of 2001 bases. Comparison of the
      deduced amino acid sequences of all four isoforms of PAD showed about 50%
      identity with each other, the 3' regions being highly homologous compared with
      the 5' regions.
FAU - Rus'd, A A
AU  - Rus'd AA
AD  - Department of Applied Biological Resource Sciences, School of Agriculture,
      Ibaraki University, Japan.
FAU - Ikejiri, Y
AU  - Ikejiri Y
FAU - Ono, H
AU  - Ono H
FAU - Yonekawa, T
AU  - Yonekawa T
FAU - Shiraiwa, M
AU  - Shiraiwa M
FAU - Kawada, A
AU  - Kawada A
FAU - Takahara, H
AU  - Takahara H
LA  - eng
SI  - GENBANK/AB013848
SI  - GENBANK/AB013849
SI  - GENBANK/AB013850
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Estrogens)
RN  - 0 (Isoenzymes)
RN  - 0 (RNA, Messenger)
RN  - EC 3.- (Hydrolases)
RN  - EC 3.5.3.15 (Protein-Arginine Deiminase Type 1)
RN  - EC 3.5.3.15 (Protein-Arginine Deiminase Type 3)
RN  - EC 3.5.3.15 (Protein-Arginine Deiminase Type 4)
RN  - EC 3.5.3.15 (Protein-Arginine Deiminases)
RN  - EC 3.5.3.15 (peptidylarginine deiminase 4, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Epidermis/enzymology
MH  - Estrogens/pharmacology
MH  - Female
MH  - Gene Expression/genetics
MH  - Hydrolases/biosynthesis/chemistry/*genetics
MH  - Isoenzymes/biosynthesis/genetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - Ovariectomy
MH  - Protein-Arginine Deiminase Type 1
MH  - Protein-Arginine Deiminase Type 3
MH  - Protein-Arginine Deiminase Type 4
MH  - Protein-Arginine Deiminases
MH  - RNA, Messenger/metabolism
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Uterus/enzymology
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
AID - 10.1046/j.1432-1327.1999.00083.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1999 Feb;259(3):660-9. doi: 10.1046/j.1432-1327.1999.00083.x.