PMID- 10488123
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20191210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 39
DP  - 1999 Sep 24
TI  - Molecular characterization of peptidylarginine deiminase in HL-60 cells induced
      by retinoic acid and 1alpha,25-dihydroxyvitamin D(3).
PG  - 27786-92
AB  - Three types of peptidylarginine deiminase (PAD), which converts a protein
      arginine residue to a citrulline residue, are widely distributed in animal
      tissues. Little is known about PAD of hemopoietic cells. We found that PAD
      activity in human myeloid leukemia HL-60 cells was induced with the
      granulocyte-inducing agents retinoic acid and dimethyl sulfoxide and with the
      monocyte-inducing agent 1alpha,25-dihydroxyvitamin D(3). We cloned and
      characterized a PAD cDNA from retinoic acid-induced cells. The cDNA was 2,238
      base pairs long and encoded a 663-amino acid polypeptide. The HL-60 PAD had
      50-55% amino acid sequence identities with the three known enzymes and 73%
      identity with the recently cloned keratinocyte PAD. The recombinant enzyme
      differs in kinetic properties from the known enzymes. Immunoblotting and Northern
      blotting with an antiserum against the enzyme and the cDNA, respectively, showed 
      that a protein of approximately 67 kDa increased concomitantly with increase of
      mRNA of approximately 2.6 kilobases during granulocyte differentiation. During
      monocyte differentiation the same mRNA and protein increased as in granulocyte
      differentiation. Neither the enzyme activity nor the protein was found in
      macrophage-induced cells. These results suggested that expression of the PAD gene
      is tightly linked to myeloid differentiation.
FAU - Nakashima, K
AU  - Nakashima K
AD  - Graduate School of Integrated Science, Yokohama City University, 22-2, Seto,
      Kanazawa-ku, Yokohama 236-0027, Japan.
FAU - Hagiwara, T
AU  - Hagiwara T
FAU - Ishigami, A
AU  - Ishigami A
FAU - Nagata, S
AU  - Nagata S
FAU - Asaga, H
AU  - Asaga H
FAU - Kuramoto, M
AU  - Kuramoto M
FAU - Senshu, T
AU  - Senshu T
FAU - Yamada, M
AU  - Yamada M
LA  - eng
SI  - GENBANK/AB017919
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA Primers)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Sulfuric Acid Esters)
RN  - 5688UTC01R (Tretinoin)
RN  - EC 3.- (Hydrolases)
RN  - EC 3.5.3.15 (PADI4 protein, human)
RN  - EC 3.5.3.15 (Protein-Arginine Deiminase Type 4)
RN  - EC 3.5.3.15 (Protein-Arginine Deiminases)
RN  - FXC9231JVH (Calcitriol)
RN  - JW5CW40Z50 (dimethyl sulfate)
RN  - NI40JAQ945 (Tetradecanoylphorbol Acetate)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Calcitriol/*pharmacology
MH  - Cell Differentiation/drug effects
MH  - DNA Primers
MH  - Enzyme Induction
MH  - Gene Library
MH  - Granulocytes/cytology/enzymology
MH  - HL-60 Cells
MH  - Humans
MH  - Hydrolases/*biosynthesis/*genetics/metabolism
MH  - Keratinocytes/enzymology
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Protein-Arginine Deiminase Type 4
MH  - Protein-Arginine Deiminases
MH  - Recombinant Fusion Proteins/biosynthesis/metabolism
MH  - Sequence Alignment
MH  - Sulfuric Acid Esters/pharmacology
MH  - Tetradecanoylphorbol Acetate/pharmacology
MH  - Tretinoin/*pharmacology
EDAT- 1999/09/17 00:00
MHDA- 1999/09/17 00:01
CRDT- 1999/09/17 00:00
PHST- 1999/09/17 00:00 [pubmed]
PHST- 1999/09/17 00:01 [medline]
PHST- 1999/09/17 00:00 [entrez]
AID - 10.1074/jbc.274.39.27786 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 24;274(39):27786-92. doi: 10.1074/jbc.274.39.27786.