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

FEBS Letters

Ishigami, Akihito¹  Yamada, Michiyuki²  Senshu, Tatsuo¹  Watanabe, Kazutada³  Kuramoto, Masashi² 

[1] Department of Cell Chemistry, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, Japan;Graduate School of Integrated Science, Yokohama City University, 3-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan;Department of Experimental Biology, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, Japan

关键词: Peptidylarginine deiminase;    All-trans retinoic acid;    Keratinocyte differentiation;    PAD;    peptidylarginine deiminase;    RA;    all-trans retinoic acid;    PCR;    polymerase chain reaction;    RACE;    rapid amplification of cDNA ends;    GST;    glutathione S-transferase;    BAEE;    benzoyl-l-arginine ethyl ester;    Bz-L-Arg;    benzoyl-l-arginine;   

DOI  :  10.1016/S0014-5793(98)00893-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown