title: Murine GBP-5, a new member of the murine guanylate-binding protein family, is coordinately regulated with other GBPs in vivo and in vitro.
abstract: A new murine member of the interferon (IFN)-inducible guanylate-binding protein (GBP) family was cloned in a search for glucocorticoid-attenuated response genes induced in the lung during endotoxemia. The full-length MuGBP-5 cDNA encodes a 590 amino acid residue protein with GTP binding motifs identical to those in human GBP-1 (HuGBP-1) and a similar isoprenylation sequence at the C-terminus. An alternatively spliced form of MuGBP-5 that lacks the second GTP binding motif and differs at the C-terminus was also identified. The MuGBP-5 gene is located on chromosome 3, near MuGBP-3 and MuGBP-2, and has a genomic organization similar to other GBP genes. To facilitate the evaluation of GBP family message expression, we constructed RNase protection assay probes for MuGBP-1, MuGBP-2, MuGBP-3, MuGBP-4/Mag-2 (macrophage activation gene-2), and MuGBP-5 and validated their use in Swiss Webster, BALB/c, and C57BL/6 mice. In BALB/c mice, all five MuGBPs were induced in multiple organs during endotoxemia, and all had a similar pattern of expression in different tissues. With minor quantitative differences, the MuGBPs also had similar patterns of response to IFN-gamma, lipopolysaccharide (LPS), interleukin-1beta (IL-1beta), and tumor necrosis factor-alpha (TNF-alpha) in RAW 264.7 and Swiss 3T3 cells. The coordinate expression of the MuGBPs suggests that they share common mechanisms of regulation.
authors.affiliation: Department of Pediatrics, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
authors.forename: Tam Thuan
authors.initials: TT
authors.lastname: Nguyen
authors.forename: Yan
authors.initials: Y
authors.lastname: Hu
authors.forename: Daniel P
authors.initials: DP
authors.lastname: Widney
authors.forename: Rebecca A
authors.initials: RA
authors.lastname: Mar
authors.forename: Jeffrey B
authors.initials: JB
authors.lastname: Smith
mesh_terms: D016475:3T3 Cells / Q000187:drug effects / Q000378:metabolism; D000315:Adrenalectomy; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis / Q000235:genetics; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000235:genetics; D019446:Endotoxemia / Q000235:genetics / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000096:biosynthesis* / Q000235:genetics; D005786:Gene Expression Regulation / Q000187:drug effects; D006801:Humans; D007371:Interferon-gamma / Q000494:pharmacology; D007375:Interleukin-1 / Q000494:pharmacology; D008070:Lipopolysaccharides / Q000494:pharmacology; D008168:Lung / Q000378:metabolism; D008264:Macrophages / Q000187:drug effects / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D005810:Multigene Family; D009928:Organ Specificity; D010802:Phylogeny; D051381:Rats; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013047:Specific Pathogen-Free Organisms; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology
chemical_list: D002352:Carrier Proteins; D018076:DNA, Complementary; D004268:DNA-Binding Proteins; C490287:GBP1 protein, human; C113264:GBP3 protein, human; C490288:Gbp2b protein, mouse; C485134:Gbp3 protein, mouse; D007375:Interleukin-1; D008070:Lipopolysaccharides; D014409:Tumor Necrosis Factor-alpha; D007371:Interferon-gamma; D019204:GTP-Binding Proteins; C452200:Gbp2 protein, mouse; C472531:Gbp5 protein, mouse; C472530:Mpa2 protein, mouse