Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture.
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.
Yamanishi
K
K
Department of Dermatology, Kyoto Prefectural University of Medicine, Japan.
Liew
F M
FM
Konishi
K
K
Yasuno
H
H
Doi
H
H
Hirano
J
J
Fukushima
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D004817:Epidermis / Q000201:enzymology*; D006801:Humans; D015603:Keratinocytes / Q000201:enzymology*; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D016133:Polymerase Chain Reaction / Q000379:methods; D011487:Protein Conformation; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D011503:Transglutaminases / Q000235:genetics*
D015345:Oligonucleotide Probes; D004247:DNA; D011503:Transglutaminases