Molecular cloning of two novel types of peptidylarginine deiminase cDNAs from retinoic acid-treated culture of a newborn rat keratinocyte cell line

FEBS Lett. 1998 Aug 14;433(1-2):113-8. doi: 10.1016/s0014-5793(98)00893-x.

Abstract

Peptidylarginine deiminases (PADs) are a group of enzymes which convert protein arginine residues to citrulline residues. Using rat muscle PAD cDNA as a probe, we obtained two novel cDNAs, PAD-R11 and PAD-R4, from immortalized rat keratinocytes treated with all-trans retinoic acid. Comparison of the deduced amino acid sequences with those of muscle and hair follicle enzymes showed high conservation in the C-terminal region. Recombinant proteins encoded by both PAD-R11 and PAD-R4 showed the enzyme activities. That of PAD-R11 showed a characteristic feature of the enzyme found in the epidermis.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Animals, Newborn*
  • Base Sequence
  • Blotting, Northern
  • Cell Line
  • Cloning, Molecular*
  • Conserved Sequence
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics*
  • Hair Follicle / enzymology
  • Hydrolases / chemistry
  • Hydrolases / genetics*
  • Keratinocytes / enzymology*
  • Molecular Sequence Data
  • Muscles / enzymology
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases
  • RNA, Messenger / analysis
  • Rats
  • Recombinant Proteins / metabolism
  • Sequence Homology
  • Tretinoin / pharmacology*

Substances

  • DNA, Complementary
  • RNA, Messenger
  • Recombinant Proteins
  • Tretinoin
  • Hydrolases
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases

Associated data

  • GENBANK/AB010998
  • GENBANK/AB010999