Mutations in Homocysteine Metabolism Genes Increase Keratin N-Homocysteinylation and Damage in Mice
作者: Kamila BorowczykJacek WróblewskiJoanna SuliburskaNoriyuki AkahoshiIsao IshiiHieronim Jakubowski
作者单位: 1epartment of Microbiology, Biochemistry and Molecular Genetics, Rutgers-New Jersey Medical School, International Center for Public Health, Newark, NJ 07103, USA
2Institute of Bioorganic Chemistry, 71-704 Poznań, Poland
3Institute of Human Nutrition and Dietetics, Poznań University of Life Sciences, 60-632 Poznań, Poland
4Department of Health Chemistry, Showa Pharmaceutical University, Tokyo 194-8543, Japan
5Department of
刊名: International Journal of Genomics, 2018, Vol.2018
来源数据库: Directory of Open Access Journals
DOI: 10.1155/2018/7570850
原始语种摘要: Genetic or nutritional deficiencies in homocysteine (Hcy) metabolism increase Hcy-thiolactone, which causes protein damage by forming isopetide bonds with lysine residues, generating N-Hcy-protein. In the present work, we studied the prevalence and genetic determinants of keratin damage caused by homocysteinylation. We found that in mammals and birds, 35 to 98% of Hcy was bound to hair keratin via amide or isopeptide bond (Hcy-keratin), while 2 to 65% was S-Hcy-keratin. A major fraction of hair Hcy-keratin (56% to 93%), significantly higher in birds than in mammals, was sodium dodecyl sulfate-insoluble. Genetic hyperhomocysteinemia significantly increased N-Hcy-keratin levels in the mouse pelage. N-Hcy-keratin was elevated 3.5-, 6.3-, and 11.7-fold in hair from Mthfr−/−, Cse−/−, or Cbs−/−...
全文获取路径: DOAJ  (合作)

  • Keratin 角蛋白
  • keratin 角朊
  • pelage 毛发
  • sulfate 硫酸盐
  • protein 蛋白质
  • mouse 小鼠
  • birds 鸟类
  • causes 白内障的原因
  • solubility 溶度
  • sodium