Lemaire, Simon,Bonhomme, Andreanne2013-11-072013-11-0720032003Source: Masters Abstracts International, Volume: 42-06, page: 2112.http://hdl.handle.net/10393/26449http://dx.doi.org/10.20381/ruor-9634Rat alveolar macrophages express specific binding sites for C-terminal fragments of histone H4. The present study was aimed at identifying and characterizing the receptor for the C-terminal fragment 86 to 100 of histone H4, an antinociceptive peptide structurally similar to histogranin. The inhibitory effect of GTP analogs (GTP-gamma-S and Gpp(NH)p) and pertussis toxin on membrane preparations and the finding that H4-(86--100) potently (10--8 M) inhibited forskolin-stimulated cAMP levels in cultured alveolar macrophages suggest the involvement of a GiPCR. Gel electrophoresis of cross-linked bound radiolabelled ligand revealed two binding proteins, 30 kDa and 54 kDa, whose detection was increased by stimulation of macrophages with interferon gamma (IFNgamma). Affinity chromatography and SDS-PAGE gel electrophoresis revealed a major protein band identified as beta-actin trypsin digests. (Abstract shortened by UMI.)92 p.enBiology, Molecular.Thesis