Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture

Biochem Biophys Res Commun. 1991 Mar 29;175(3):906-13. doi: 10.1016/0006-291x(91)91651-r.

Abstract

We have isolated a cDNA encoding human epidermal transglutaminase, a key enzyme of terminal differentiation of keratinocytes. A cDNA library from cultured human keratinocytes was screened by a PCR-amplified partial cDNA fragment of the enzyme with oligonucleotide primers based on the homology of the transglutaminase family. The cDNA is 2734 bp coding a protein of 817 amino acids. The several regions including the active site cysteine residue are highly conserved among the transglutaminase family. However, the charged N-terminal domain is unique to the epidermal transglutaminse, suggesting that the region is involved in the function of the enzyme in keratinocytes.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Cells, Cultured
  • Cloning, Molecular
  • DNA / genetics
  • DNA / isolation & purification
  • Epidermis / enzymology*
  • Humans
  • Keratinocytes / enzymology*
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Polymerase Chain Reaction / methods
  • Protein Conformation
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid
  • Transglutaminases / genetics*

Substances

  • Oligonucleotide Probes
  • DNA
  • Transglutaminases

Associated data

  • GENBANK/D00690
  • GENBANK/D00691
  • GENBANK/D90287
  • GENBANK/M62476
  • GENBANK/M62477
  • GENBANK/M62478
  • GENBANK/M62479
  • GENBANK/M62480
  • GENBANK/M62481
  • GENBANK/M62482