课题基金 / 基金详情

Studies on the structure and biological function of human hair follicle peptidylarginine deiminase

Studies on the structure and biological function of human hair follicle peptidylarginine deiminase
人毛囊肽基精氨酸脱亚胺酶的结构及生物学功能研究
批准号:
13670904
负责人:
KAWADA Aklira
金额:
$2.3万
依托单位:
依托单位国家:
日本
项目类别:
Grant-in-Aid for Scientific Research (C)
财政年份:
2001
资助国家:
日本
项目状态:
已结题
起止时间:
2001 至 2003

项目摘要

项目成果

相似基金

相关文献

中文摘要
翻译
点击翻译按钮获取中文摘要
英文摘要
The hair is composed of inner and root sheath, cuticle, and medulla cells which are differentiated from hair mother cell. The terminal differentiation of hair mother cell is common in tracing epidermal basal cells, but the biochemical study regarding the process of hair differentiation is very few.Peptidylarginine deiminase(PAD) is a post-translational modification enzyme which gives the electrostatic change by converting basic region of the target protein into the radio valence, causing the different interaction between target proteins and another protein. Since the first finding of G.E Rogers in 1977, that enzymatic activity converts arginine residue of the protein to the citrulline residue in extract of guinea pig hair follicle, biochemical studies of PADs were advanced in the various tissues. However the research on the PAD of the hair follicle is seldom carried out. In this study, we prepared the human hair cells by the primary culture method, and the RNA, and then cloned the enti … More re cDNA of the human hairy cell PAD(PAD T4) by homologue polymerase chain reaction. The complete amino acid sequence was clarified by the nucleotide sequence analysis. We constructed the human PAD T4 expression plasmid in an Echerichia coli and purification and enzymatic properties of the recombinant enzyme were clarified. Especially, the role of which the hairy cell peculiar protein(trichohyalin) is important for the regulation of the hair construct and the citrulline residues were found in the trichohyalin, that the trichohyalin is a candidate target for PAD T4. In this study we proved that PAD T4 modified the trichohyalin effectively. Next, we made a monoclonal antibody against specific for PAD T4 is and we examined the cellular distribution of PAD T4 in the hair follicle. The immunohistochemisty showed that the PAD T4 specifically localized in the inner root sheath in the hairy cells. The knowledge which proved that the above-mentioned trichohyalin also exists in this organization locally and that this enzyme has made the trichohyalin to be a target. Less
期刊论文(3)
专著(0)
科研奖励(0)
会议论文
S.Chavanas, M.C.Mechin, H.Takahara, K.Kawada, R.Nachat, G.Serre, M.Simon: "Comparative analysis of the mouse and human peptidylarginine deiminase(PADI)clusters reveals high conserved non-coding"Gene. 印刷中.
S.Chavanas、M.C.Mechin、H.Takahara、K.Kawada、R.Nachat、G.Serre、M.Simon:“对小鼠和人类肽基精氨酸脱亚胺酶 (PADI) 簇的比较分析揭示了高度保守的非编码”基因。正在打印。
DOI: --
发表时间:
期刊:
影响因子: --
作者: []
通讯作者:
S.Chavanas, M.C.Mechin, H.Takahara, A.Kawada, R.Nachat, G.Serre, M.Simon: "Comparative analysis of the mouse and human peptidylarginine deiminase(PADI) clusters reveals highly conserved non-coding segments and a new human gene, PADI6"Gene. (印刷中).
S.Chavanas、M.C.Mechin、H.Takahara、A.Kawada、R.Nachat、G.Serre、M.Simon:“对小鼠和人肽基精氨酸脱亚氨酶 (PADI) 簇的比较分析揭示了高度保守的非编码片段和新的人类基因,PADI6“基因。(正在印刷中)。
DOI: --
发表时间:
期刊:
影响因子: --
作者: []
通讯作者:
S.Chavanas, M.C.Mehi, H.Takahara, A.Kawada, R.Nachat, G.Serre, M.Simon: "Comparative analysis of the mouse and human peptidylarginine deiminase(PADI) clusters reveals high conserved non-conding segments and new human gene, PADI6"Gene. (in press).
S.Chavanas、M.C.Mehi、H.Takahara、A.Kawada、R.Nachat、G.Serre、M.Simon:“对小鼠和人肽基精氨酸脱亚胺酶 (PADI) 簇的比较分析揭示了高度保守的非条件片段和新的片段
DOI: --
发表时间:
期刊:
影响因子: --
作者: []
通讯作者:
海外基金