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.
Department of Dermatology, Kyoto Prefectural University of Medicine, Japan.
K
K
Yamanishi
F M
FM
Liew
K
K
Konishi
H
H
Yasuno
H
H
Doi
J
J
Hirano
S
S
Fukushima
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