Disease relevance of AIF1

• VSMCs stably transduced with AIF-1 retrovirus migrate 2.6-fold more rapidly (85.1+/-2.9 versus 225.5+/-16.6; P<0.001) in response to platelet-derived growth factor versus control cells [1].
• We recently mapped the retention signal for Golgi localization in one Bunyaviridae member (Uukuniemi virus) to the cytoplasmic tail of G1 [2].
• Targeting of a short peptide derived from the cytoplasmic tail of the G1 membrane glycoprotein of Uukuniemi virus (Bunyaviridae) to the Golgi complex [2].
• The attachment protein G of respiratory syncytial virus (RSV) has a modular architecture [3].
• A single epitope, recognized by NV MAbs NV3901, NV3912, and NV2461 was found to occur in the majority of genogroup 1 (G1) but not genogroup 2 (G2) "Norwalk-like viruses" (NLVs) [4].

Psychiatry related information on AIF1

• The allograft inflammatory factor-1 in Creutzfeldt-Jakob disease brains [5].

High impact information on AIF1

• Here we measure the relative propensity for beta-sheet formation of the twenty naturally occurring amino acids in a variant of the small, monomeric, beta-sheet-rich, IgG-binding domain from protein G. Amino-acid substitutions were made at a guest site on the solvent-exposed surface of the beta-sheet [6].
• The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints [7].
• Upregulation of AIF-1 in the setting of T cell activation suggests that it may play a role in macrophage activation and function [8].
• Expression of the G1 cDNA in Chinese hamster ovary cells produced ALAD protein with little activity; the G2 cDNA produced the enzyme with approximately 50% normal activity [9].
• Pulse-labeling studies demonstrated that the G1 enzyme had a normal half life, while the G2 enzyme had a markedly decreased half life [9].

Chemical compound and disease context of AIF1

• Reperfusion arrhythmia (in sec) was significantly (all p < 0.05) shorter in GGA (115 +/- 33) vs G1 (315 +/- 29) and G2 (273 +/- 33), and also in GL (161 +/- 26) vs G1 [10].
• IgGs purified by protein-G immunoaffinity were similarly screened for inhibition of ACTH-stimulated cortisol secretion; samples from 5 controls and 5 patients with Graves' disease were without effect, and IgGs from only 2 of 25 patients with Addison's disease decreased ACTH bioactivity (by < 12%) [11].
• A few applications of diffusion-edited HSQC to an E. coli cell lysate containing the (15)N-labeled B domain of streptococcal protein G (GB1), and to a (15)N-labeled N-acetylglycine/apomyoglobin mixture are presented [12].
• The expression pattern of AIF-1 mRNA and protein in the kidneys of normal and diseased rats, such as anti-GBM nephritis and puromycin aminonucleoside nephrosis, was investigated by in situ hybridization, immunohistochemistry, and immunoelectron microscopy [13].
• Increased binding to heparin of the HCV fraction that was not retained by a protein G column suggested that antibodies complexed to the virions partially inhibited the interaction [14].

Biological context of AIF1

• Taken together, modification of the wild-type EF-hand domain and native calcium-binding activity results in a loss of AIF-1 function [15].
• We sequenced the AIF-1 gene region and detected three novel polymorphisms, all of which were diallelic and localized at introns [16].
• AIF-1 is not present in cultured human VSMCs but is induced by cytokines, and overexpression of AIF-1 results in increased VSMC growth and cell-cycle gene expression [1].
• AIF-1 is an actin-polymerizing and Rac1-activating protein that promotes vascular smooth muscle cell migration [1].
• Overexpression of AIF-1 in these cells led to a 238% increase in cell number compared to empty vector controls [17].

Anatomical context of AIF1

• The ability of AIF-1 to activate human vascular smooth muscle cells is lost by mutations in the EF-hand calcium-binding region [15].
• In unstimulated VSMCs, AIF-1 colocalizes with F-actin but translocates to lamellipodia on stimulation with platelet-derived growth factor [1].
• AIF-1 is constitutively expressed in monocytes/macrophages, but its expression in human lymphocytes has not been described [17].
• Expression of allograft inflammatory factor-1 in T lymphocytes: a role in T-lymphocyte activation and proliferative arteriopathies [17].
• Allograft inflammatory factor (AIF)-1 is a cytoplasmic, calcium-binding protein whose expression in transplanted human hearts correlates with rejection and development of coronary artery vasculopathy (CAV) [17].

Associations of AIF1 with chemical compounds

• To characterize AIF-1 modulatory effects in primary human VSMCs, AIF-1-interacting proteins were identified by an AIF-1/glutathione S transferase fusion protein affinity assay [1].
• Morphological analyses of hypoxic microglia using the microglial marker Iba1 revealed that treatment with MINO and DOXY caused a higher percentage of microglia to remain in a non-activated state [18].
• A portion of the G1 glycoprotein of ELMC that is homologous to an important linear epitope of FC differs from the FC epitope by 10 of 31 residues [19].
• Isolated rat hearts were perfused with modified Krebs-Henseleit buffer containing either (in mM): glucose 11 (G1), glucose 22 (G2), or glucose 11 with either xylitol 11 (GX), mannitol 11 (GM), L-leucine 1 (GL), or L-glutamic acid 2 (GGA), respectively [10].
• CONCLUSIONS: The effect of progesterone is seen only on proliferation in low-grade (G1 and G2) tumors [20].

Physical interactions of AIF1

• These data indicate that AIF-1 binds and polymerizes F actin and also regulates Rac1 activity and VSMC migration [1].
• Their effects are mediated via different protein G-coupled melanocortin (MC) receptors that are capable to bind one or more POMC-derived peptides [21].
• Heavy and light chains of FVIII were detected in plasma-derived immune complexes extracted by using protein G Sepharose [22].
• Immunoblot analysis indicated that the molecular weight of the binding protein was 150-160K, and the IL-1 alpha binding activity was removed and recovered from NHS by Protein-G affinity chromatography; indicating that the binding protein was IL-1 alpha-specific IgG [23].
• The structure of a peptide antigen corresponding to the subtype P1.7 variant of the porin PorA from the human pathogen Neisseria meningitidis was determined by solution of the X-ray crystal structure of the ternary complex of the peptide (ANGGASGQVK) in complex with a Fab fragment and a domain from streptococcal protein G to 1.95 A resolution [24].

Co-localisations of AIF1

• AIF-1 colocalizes with Rac1, and AIF-1-transduced VSMCs show a constitutive and enhanced activation of Rac1, providing a mechanism for the increased migration [1].

Regulatory relationships of AIF1

• CONCLUSIONS: This study indicates that AIF-1 enhances VSMC growth by autocrine production of G-CSF, and AIF-1 expression may influence VSMC-inflammatory cell communication [25].
• Inhibitory mutant Iba1 that suppresses M-CSF-induced membrane ruffling had lost the actin-cross-linking activity, and it inhibited the cross-linking activity of intact Iba1 [26].

Other interactions of AIF1

• TNF, TNF receptor type 1, and allograft inflammatory factor-1 gene polymorphisms in Japanese patients with type 1 diabetes [16].
• Further, it was unable to activate Rac1, or induce G-CSF expression to the degree as wild-type AIF-1 [15].
• To determine if calcium binding plays a functional role in AIF-1 activity, a single site-specific mutation was made in the EF-hand calcium-binding domain to abrogate binding of calcium (AIF-1DeltaA), which was confirmed by calcium overlay [15].
• In this report, we describe IRT-1, a novel mRNA transcript constitutively expressed in a number of human tissues, but expressed in human VSMCs only when they are stimulated with IFN-gamma [27].
• This study suggests that IRT-1 is an IFN-gamma-inducible factor that may regulate the progression of vascular proliferative diseases [27].

Analytical, diagnostic and therapeutic context of AIF1

• Allograft inflammatory factor-1 (AIF-1) is a cytoplasmic, calcium-binding protein that is expressed in VSMCs by allograft and balloon angioplasty injury [1].
• Allograft inflammatory factor-1 (AIF-1), a cytokine-responsive macrophage molecule, was originally identified and cloned from rat cardiac allografts with chronic cardiac rejection [28].
• AIF-1 gene transcripts were identified by the reverse-transcriptase polymerase chain reaction in endomyocardial biopsy specimens from human heart transplants and in macrophage cell lines [28].
• Western blotting confirmed more prominent AIF-1 immunoreactive bands of approximately 50 kDa in four CJD patients compared to three controls [5].
• We used immunohistochemistry double labelling experiments to analyse the spatial distribution and cell-type-specific localization of AIF-1 in the brains of patients who died as a result of sporadic Creutzfeldt-Jakob disease (CJD) and neuropathologically unaltered controls [5].

References