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High-throughput profiling of histone post-translational modifications and chromatin modifying proteins by reverse phase protein array.
Wang, Xuan; Shi, Zhongcheng; Lu, Hsin-Yi; Kim, Jean J; Bu, Wen; Villalobos, Jose A; Perera, Dimuthu N; Jung, Sung Yun; Wang, Tao; Grimm, Sandra L; Taylor, Bethany C; Rajapakshe, Kimal; Park, Hyekyung; Wulfkuhle, Julia; Young, Nicolas L; Li, Yi; Coarfa, Cristian; Edwards, Dean P; Huang, Shixia.
Afiliación
  • Wang X; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
  • Shi Z; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
  • Lu HY; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
  • Kim JJ; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA; Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.
  • Bu W; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA; Lester & Sue Smith Breast Center, Baylor College of Medicine, Houston, TX, USA.
  • Villalobos JA; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
  • Perera DN; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
  • Jung SY; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
  • Wang T; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
  • Grimm SL; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA; Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.
  • Taylor BC; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
  • Rajapakshe K; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.
  • Park H; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
  • Wulfkuhle J; Center for Applied Proteomics and Molecular Medicine, George Mason University, Fairfax, VA, USA.
  • Young NL; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA; Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
  • Li Y; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA; Lester & Sue Smith Breast Center, Baylor College of Medicine, Houston, TX, USA.
  • Coarfa C; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA; Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.
  • Edwards DP; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA; Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.
  • Huang S; Advanced Technology Cores, Baylor College of Medicine, Houston, TX, USA; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA; Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA; Department of Education, Innovation & Tech
J Proteomics ; 262: 104596, 2022 06 30.
Article en En | MEDLINE | ID: mdl-35489683
Epigenetic variation plays a significant role in normal development and human diseases including cancer, in part through post-translational modifications (PTMs) of histones. Identification and profiling of changes in histone PTMs, and in proteins regulating PTMs, are crucial to understanding diseases, and for discovery of epigenetic therapeutic agents. In this study, we have adapted and validated an antibody-based reverse phase protein array (RPPA) platform for profiling 20 histone PTMs and expression of 40 proteins that modify histones and other epigenomic regulators. The specificity of the RPPA assay for histone PTMs was validated with synthetic peptides corresponding to histone PTMs and by detection of histone PTM changes in response to inhibitors of histone modifier proteins in cell cultures. The useful application of the RPPA platform was demonstrated with two models: induction of pluripotent stem cells and a mouse mammary tumor progression model. Described here is a robust platform that includes a rapid microscale method for histone isolation and partially automated workflows for analysis of histone PTMs and histone modifiers that can be performed in a high-throughput manner with hundreds of samples. This RPPA platform has potential for translational applications through the discovery and validation of epigenetic states as therapeutic targets and biomarkers. SIGNIFICANCE: Our study has established an antibody-based reverse phase protein array platform for global profiling of a wide range of post-translational modifications of histones and histone modifier proteins. The high-throughput platform provides comprehensive analyses of epigenetics for biological research and disease studies and may serve as screening assay for diagnostic purpose or therapy development.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / Análisis por Matrices de Proteínas Límite: Animals Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / Análisis por Matrices de Proteínas Límite: Animals Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos