Histone H2

Abstract: Biologically active substance with standardizable hormonal activity, containing in a physiological medium at least one histone, particularly at least one histone H2 or an active area of said histone with immune system immunostimulating and/or endocrinological properties. Utilization of histones and/or segments of histones for producing such a preparation for medical purposes. Said histones may be extracted from biological starting materials, for example calf thymus. Since H2A and H2B histones of oxen and humans are identical, ox histones may also be used for such a preparation for human medical purposes. The preparation according to the present invention may also contain only the variable evolution segments or part of at least one H2 histone. The invention is based on the fact that the biologically active area of an immunostimulating or endocrinologically active histone is located in the variable evolution histone segment. The preparation according to the present invention may be used in immunotherapy.

Abstract: Understanding the mechanisms of cataract formation is important for age-related and hereditary cataracts caused by mutations in lens protein genes Lens proteins of the crystallin gene families α-, β-, and γ-crystallin are the most abundant proteins in the lens Single point mutations in crystallin genes cause autosomal dominant cataracts in multigenerational families Our previous proteomic and RNAseq studies identified genes and proteins altered in the early stages of cataract formation in mouse models Histones H2A, H2B, and H4 increase in abundance in αA- and αB-crystallin mutant mouse lenses and in cultured cells expressing the mutant form of αA-crystallin linked with hereditary cataracts In this study of histones in mutant lenses, we extracted histones from adult mouse lenses from cryaa-R49C and cryab-R120G mutant knock-in mice We characterized the histones using matrix-assisted laser desorption/ionization time of flight (MALDI-TOF)-mass spectrometric analysis and gel electrophoresis and characterized the lens nucleus morphology using electron microscopy (EM) The relative abundance of histone H3 protein decreased in lenses from cryaa-R49C mutant mice and the relative abundance of histone H2 increased in these lenses Electron microscopy of nuclei from cryaa-R49C-homozygous mutant mouse lenses revealed a pronounced alteration in the distribution of heterochromatin

Abstract: Epigenetics is a hot new research field, but it seems that the influenza virus already has it figured out. By mimicking epigenetic regulation in human cells, one flu strain suppresses the expression of antiviral genes. See Article p.428 Histone proteins are essential regulators of gene function. The amino-terminal domain of the histone H2, or the histone 'tail', can be post-translationally modified, and it acts as a scaffold for the assembly of protein complexes that control gene function. Ivan Marazzi and colleagues now show that the immunosuppressive NS1 protein of the influenza virus carries a histone-like sequence that mimics key features of histone H3, including binding to key transcriptional regulators, so that the virus can hijack the host transcriptional machinery. Interaction between NS1 and transcriptional elongation complex PAF1C is shown to be crucial to the host antiviral response, validating PAF1 protein as a candidate for anti-inflammatory therapy using synthetic PAF1 antagonists.