1998 Fiscal Year Final Research Report Summary
Biological roles of peptidylarginine deiminase in the pathogenic mechanisms of keratin deseases : molecular biological approach
| Project/Area Number |
09670896
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Dermatology
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| Research Institution | AKITA UNIVERSITY (1998)
Juntendo University (1997) |
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Principal Investigator |
MANABE Motomu Akita University School of Medicine Department of Dermatology, Professor, 医学部, 教授 (30138309)
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| Co-Investigator(Kenkyū-buntansha) |
DEMITSU Toshio Akita University School of Medicine Department of Dermatology, Associate Profess, 医学部, 助教授 (20237027)
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| Project Period (FY) |
1997 – 1998
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| Keywords | peptidylarginine deiminase / keratins / apoptosis |
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| Research Abstract |
Peptidylarginine deiminase (PAD) is the enzyme responsible for converting protein-bound arginine residues to citrulline. It has recently been shown that a number of epidermal proteins including filaggrin, trichohyalin and keratins are deiminated by the action of PAD, suggesting a possible role for protein deiminatjon during the final stages of epidermal differentiation. We report here a novel PAD substrate found during the course of identifying deiminated proteins in cultured rat epidermal keratinocytes. We found that a 70 kD protein localized to the periphery of the nucleus was preferentially deiminated after ionomycin treatment in the presence of 2 mM calcium and was associated with apoptotic events in these cells. Furthermore, it was discovered that the deimination of nuclear protein could be induced by the transfection of a PAD cDNA into rat epidermal keratinocytes. These data suggest that PAD may act on the 70 kD nuclear protein to induce disassembly of the nuclear lamina and promote apoptosis during terminal epidermal differentiation.
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