Disease relevance of Aif1

• Antibody responses to Four Corners hantavirus (FCV) infections in the deer mouse (Peromyscus maniculatus) were characterized by using FCV nucleocapsid protein (N), glycoprotein 1 (G1), and glycoprotein 2 (G2) recombinant polypeptides in Western immunoblot assays [1].
• Expression of allograft inflammatory factor-1 in mouse uterus and poly(I:C)-induced fetal resorption [2].
• Viruses causing hemorrhagic fever with renal syndrome (HFRS) encode two glycoproteins, G1 and G2 [3].
• Neutralizing monoclonal antibody (MAb) escape mutants of Hantaan virus were generated using MAbs to envelope protein G1 (16D2) and G2 (11E10) [4].
• Invasion is blocked by pertussis toxin (PT), which adenosine diphosphate (ADP)-ribosylates G1-proteins, and we have provided evidence that the PT-sensitive signal stimulates leukocyte function-associated antigen-1 (LFA-1)-mediated adhesion required for invasion [5].

High impact information on Aif1

• Thus, when B cells were stimulated with mitogenic and nonmitogenic anti-IgD antibodies, both of which induce entry of cells into G1 and early calcium transients of comparable magnitude, persistent low-level calcium elevations were only detected in cells stimulated with the mitogenic antibody [6].
• These data suggest that the rapid and large increases of [Ca2+]i seen in lymphocytes within seconds after antigen receptor ligation may be associated with entry in G1, whereas low-level but persistent elevations may be the hallmark of a cell destined to synthesize DNA [6].
• We conclude that G1-proteins play an important role in T-cell hybridoma metastasis [5].
• Although immunostaining and 32P RT-PCR assays showed no differences in the mononuclear cell infiltration and T cell activation between IL-4(-/-) and wild-type tolerant recipients, some monokines (IL-12, TNF-alpha, and allograft inflammatory factor-1) were up-regulated in grafts from IL-4(-/-) recipients [7].
• Whereas anti-Ig antibody-stimulated entry of G0 B cells to the G1 and S phase of the cell cycle was markedly suppressed by dexamethasone, phorbol myristate acetate/A23187 stimulation of these events was resistant to dexamethasone [8].

Chemical compound and disease context of Aif1

• Allograft inflammatory factor-1 regulates trinitrobenzene sulphonic acid-induced colitis [9].
• This [Ca2+]i increase was completely blocked by the tyrosine kinase inhibitor, tyrphostin A48, and by the inactivator of G1 proteins, pertussis toxin [10].

Biological context of Aif1

• The mouse AIF-1 was highly conserved among all reported AIF-1 from a variety of species, from invertebrates to mammals, and the cloned cDNA was in good accordance with putative expressed regions of genomic sequences in the mouse major histocompatibility complex (MHC) class III region [11].
• Mouse allograft inflammatory factor-1 (AIF-1) cDNA was cloned and the AIF-1-specific monoclonal antibodies were established to examine its tissue distribution [11].
• After the insemination, the expression of AIF-1 mRNA diminished gradually and again increased in the pre-implantation or implantation period in allogeneic or syngeneic pregnancy, respectively [2].
• RESULTS: The expression of AIF-1 varied during the estrous cycle with a peak at estrus [2].
• Histocompatibility reaction in tissue and cells of the marine sponge Suberites domuncula in vitro and in vivo: central role of the allograft inflammatory factor 1 [12].

Anatomical context of Aif1

• Immunohistological examination revealed that differentiating germ cells in the testis and presumably macrophages in the red pulp of the spleen were positive for AIF-1 [11].
• To analyse the function of the AIF-1, a macrophage cell line, RAW 264.7, was transfected with mouse AIF-1 cDNA [11].
• The messages of mouse AIF-1 were abundantly expressed in the testis, moderately in the spleen and lymph nodes and slightly in the liver and thymus of normal BALB/c mice [11].
• These results suggest that AIF-1 plays an important role in cells of a monocyte/macrophage lineage upon stimulation with inflammatory stimuli by augmenting particular cytokine production [11].
• CONCLUSIONS: This study demonstrated for the first time that AIF-1 was expressed in uterus [2].

Associations of Aif1 with chemical compounds

• Upon stimulation with bacterial lipopolysaccharide, the transfectants that overexpressed AIF-1 showed marked morphological changes and produced significantly large amounts of interleukin (IL)-6, IL-10 and IL-12p40 but not IL-12p70 compared with control cells [11].
• By using purified proteins, direct binding of Iba1 to L-fimbrin was demonstrated by immunoprecipitation, glutathione S-transferase pull-down assays and ligand overlay assays [13].
• X-ray Structures of the Microglia/Macrophage-specific Protein Iba1 from Human and Mouse Demonstrate Novel Molecular Conformation Change Induced by Calcium binding [14].
• Immunohistochemical analysis for 4-hydroxy-2-nonenal (HNE), 8-hydroxy-deoxyguanosine (8-OHdG), ionized calcium-binding adapter molecule 1 (Iba-1), inducible NO synthase (iNOS), and nitrotyrosine were performed at 24 hours, 72 hours, or 7 days after reperfusion [15].

Physical interactions of Aif1

• In addition, retardation in morphological transformation from activated to amoeboid microglia in response to sciatic nerve injury, differential expressions of some cytokines in the lumbar cord segments and induction of Iba-1 (ionized calcium-binding adaptor molecule-1) expression in microglia were observed in NFL-/- mice [16].

Co-localisations of Aif1

• In response to stimulation, L-fimbrin accumulated and co-localized with Iba1 in membrane ruffles induced by M-CSF-stimulation and phagocytic cups formed by IgG-opsonized beads in microglial cell line MG5 [13].

Other interactions of Aif1

• Allograft inflammatory factor-1 augments production of interleukin-6, -10 and -12 by a mouse macrophage line [11].
• The augmented expression of AIF-I with concomitant expressions of TNF-alpha and NOS2 mRNA in poly(I:C)-injected mice suggests a correlation between AIF-1 production and fetal resorption [2].
• The G1/G2 protein of PVM is probably a haemagglutinin since a monoclonal antibody directed against it has a high haemagglutination inhibition titre [17].

Analytical, diagnostic and therapeutic context of Aif1

• METHOD OF STUDY: AIF-1 expression was examined in uteri of non-pregnant and pregnant mice by Northern blot analysis, RT-PCR and immunohistochemistry [2].
• Tryptic peptide mapping showed that the two major glycosylated polypeptides G1 and G2 were different forms of the same protein [17].
• Stereotaxic microinjection of recombinant IFN-gamma triggered microglial transformation in IL-18-/- mice and upregulated Iba1 expression, leading to effective eradication of virally infected neurons [18].
• Double immunofluorescence was used to confirm that Iba1 is not expressed in astrocytes which stained for glial fibrillary acidic protein [19].
• At 7 days after reperfusion, sections double-immunostained for EGFP and Iba-1 showed less activation and migration of EGFP-positive bone marrow-derived macrophages in FcgammaR-/- chimera mice than in WT mice [20].

References