Disease relevance of Hist1h2bl

• ADP-ribosylation of nuclear proteins in vivo. Identification of histone H2B as a major acceptor for mono- and poly(ADP-ribose) in dimethyl sulfate-treated hepatoma AH 7974 cells [1].

High impact information on Hist1h2bl

• These receptors also showed diminished exogenous substrate kinase activity using histone H2b and angiotensin II as phosphoacceptors [2].
• In contrast to the latter enzyme, this new enzyme catalyzed the spliting of a linkage between ADP-ribose and a protein portion in mono ADP-ribosylated histone H2B but little, if any, of the glycosidic ribosyl(1"-2') ribose bonds within poly(ADP-ribose) [3].
• Histone H2B phosphorylation in mammalian apoptotic cells. An association with DNA fragmentation [4].
• Cardiolipin activation was most evident with autophosphorylation and histone H2B phosphorylation, but only marginally evident with the favored ribosomal S6-(229-239) peptide substrate for the protease-activated kinase activity [5].
• Insulin receptor tyrosine kinase activity solubilized from hind limb muscle of control and streptozocin-induced diabetic (STZ-D) rats (2-3 wk) was studied with the substrates histone H2B and poly glutamic acid-tyrosine (glu-tyr) (4:1) [6].

Biological context of Hist1h2bl

• Under similar assay conditions, Ap4A did not inhibit phosphorylation of histone H2b by cAMP- or cGMP-dependent protein kinases [7].
• The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis [8].
• In this study, analysis of purified histone fractions revealed the in vivo acetylation of histone H2B, the testis histone variant designated TH2B, and two or more of the histone H2A variants [9].
• Amino acid sequence of rat thymus histone H2B and identification of the in vitro phosphorylation sites [10].
• When the pattern of hydrolysis of poly(ADP-ribosyl)ated histones was analyzed it was found that poly(ADP-ribose) attached to histone H2B is more resistant than the polymer attached to histone H1 or H2A or protein A24 [11].

Anatomical context of Hist1h2bl

• The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis [12].
• Truncation, deamidation, and oxidation of histone H2B in cells cultured with nickel(II) [13].
• In the present study, Western blotting of histones isolated from rat and human cell lines, cultured for 3-5 days with 0.05-0.5 mM Ni(II), revealed time- and dose-dependent appearance of a new band of histone H2B [13].
• This sequence is identical to the sequence of calf thymus histone H2B [10].
• Cationic cofactors (e.g., polylysine or histone H2B) are necessary to observe phosphorylation of calmodulin in cell-free systems containing partially purified insulin receptors from a variety of tissues [14].

Associations of Hist1h2bl with chemical compounds

• Vanadate caused a 10-fold decrease in the Km for ATP, for tyrosine kinase, and enhanced the phosphorylation of histone H2B [15].
• ADP-ribosylation of histone H2B. Identification of glutamic acid residue 2 as the modification site [16].
• Perifusion of cells with histone H2A (30 muM) or histone H2B (30 muM), markedly stimulated LH release but failed to elicit any FSH response [17].
• Insulin receptor tyrosine kinase activity solubilized from liver of control and streptozotocin diabetic rats was studied using histone H2b and poly-Glu-Tyr (4:1) as phosphoacceptors [18].
• At both termini, the truncation occurred between lysine and alanine in the two identical -KAVTK- repeats of histone H2B [13].

Regulatory relationships of Hist1h2bl

• In this investigation, we demonstrate that calmodulin enhances insulin-stimulated phosphorylation of the beta subunit of the insulin receptor and histone H2b and that insulin also stimulates phosphorylation of calmodulin [19].

Other interactions of Hist1h2bl

• Calmodulin also induced an approximately 2-fold increase in both the rate and amount of insulin-mediated incorporation of 32P into histone H2b [19].
• Phosphorylation of substrates currently used for protein kinase assays (histone H2B and phosvitin) was not stimulated [20].
• To explore the relationship between postnatal renal development and the renin-angiotensin system, we examined the steady-state levels of messenger ribonucleic acid (mRNA) for renin, angiotensinogen, histone H2b (a marker of DNA synthesis) and the structural protein actin [21].
• Additionally, the gel reveals two protein bands, one ahead of histone H2B and another ahead of histone H4, that are diminished or missing from the inactive chromatin [22].

Analytical, diagnostic and therapeutic context of Hist1h2bl

• Autophosphorylation of the beta-subunit and receptor tyrosyl kinase activity toward histone H2b was stimulated by insulin in denervated muscles as in controls, although the biological response to insulin, in vitro and in vivo, was markedly impaired after denervation, suggesting a postreceptor defect [23].
• The genomic and sequence analysis of rat histone H2B genes [24].
• Isolation, purification, tryptic digestion, and peptide sequence analysis of the retinal approximately 20 kDa phosphoprotein suggest that it is histone H2B [25].

References