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Two histone H4 mRNA variants, H4-v.1 and histogranin mRNAs, were detected in the rat genome and measured in various tissues and isolated alveolar macrophages. Medium to high levels of both mRNAs were present in the liver, adrenal glands, thymus, bone marrow and alveolar macrophag-es. H4-v.1 cDNA contained an open reading frame that coded for unmodi-fied whole histone H4, whereas histogranin cDNA lacked the first ATG codon and contained an open reading frame that coded for modified (Thr89) H4-(84–102). . | ễFEBS Journal Characterization localization and possible anti-inflammatory function of rat histone H4 mRNA variants Rene Poirier Irma Lemaire and Simon Lemaire Department of Cellular and Molecular Medicine University of Ottawa Canada Keywords C-terminalH4 peptides extracellular function histogranin histone H4 mRNA variants H4-V.1 Correspondence S. Lemaire Department of Cellular and Molecular Medicine Faculty of Medicine University of Ottawa 451 Smyth Road Ottawa Ontario Canada K1H-8M5 Fax 1 613 562 5646 Tel 1 613 562 5800 ext. 8350 E-mail slemaire@uottawa.ca Received 7 July 2006 accepted 1 August 2006 doi 10.1111 j.1742-4658.2006.05444.x Two histone H4 mRNA variants H4-V.1 and histogranin mRNAs were detected in the rat genome and measured in various tissues and isolated alveolar macrophages. Medium to high levels of both mRNAs were present in the liver adrenal glands thymus bone marrow and alveolar macrophages. H4-v.1 cDNA contained an open reading frame that coded for unmodified whole histone H4 whereas histogranin cDNA lacked the first ATG codon and contained an open reading frame that coded for modified Thr89 H4- 84-102 . The two genes displayed a sequence homologous 80 to the open reading frame of core H4 somatic H4s and H4 germinal H4g and their variant nature was supported by the absence of histone consensus palindromic and purine-rich sequences in the proximal 3 UTR and the presence of a polyadenylation signal in the distal 3 UTR and of specific upstream transcription factor-binding sites. H4-v.1 and his-togranin transcripts but not H4s transcript were selectively induced by lipopolysaccharide and or interferon gamma in alveolar macrophages. In vitro transcription translation experiments with H4-v.1 and histogranin cDNA pCMV constructs produced peptides with the molecular mass 2 kDa of the alternative histone H4 translation product which like synthetic H4- 86-100 and Thr89 H4- 86-100 or rat histogranin inhibited lipopolysaccharide-induced prostaglandin E2 .
