Disease relevance of LOC396260

• Hen egg-white avidin shows clear structural homology to streptavidin, from Streptomyces avidinii, but significant deviations can be observed in some regions [1].
• Biochemical characterization and crystal structure of a recombinant hen avidin and its acidic mutant expressed in Escherichia coli [2].
• Induction of chicken avidin and related mRNAs after bacterial infection [3].
• We have used atomic force microscopy on the calyx-type nerve terminal of the chick ciliary ganglion to localize single calcium channels tagged via biotinylated omega-conotoxin GVIA to avidin-coated 30 nm gold particles [4].
• Synthesis and secretion of avidin was studied in cultured chicken embryo fibroblasts infected with transforming retroviruses (Rous sarcoma virus, its mutants temperature-sensitive for transformation, OK-10 virus) or a nontransforming retrovirus (RAV-1) [5].

Psychiatry related information on LOC396260

• Food deprivation for 2 and 6 h reduced the avidin resistance to 54% and 30%, respectively [6].
• The time response curve of the avidin mRNA induction by progesterone was also determined [7].

High impact information on LOC396260

• Avidin was detectable in both transformed and untransformed cultures, and was identical to chicken egg white avidin by several criteria: biotin-binding, heat-induced biotin exchange, subunit size (mol. wt. 15 600), immunoprecipitation of metabolically labeled proteins and immunoblotting [5].
• Avidin is induced in chicken embryo fibroblasts by viral transformation and cell damage [5].
• The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin (which are missing in streptavidin) may account for its higher affinity constant [8].
• Unexpectedly, a residual N-acetylglucosamine moiety was detected in the deglycosylated avidin monomer by difference Fourier synthesis [8].
• Alternatively, avidin conjugated to rhodamine or avidin complexed to biotinated peroxidase has been used for mRNA detection [9].

Chemical compound and disease context of LOC396260

• Thus, the binding properties of chicken liver galectin (CG-16) to glycoproteins (gps) and Streptococcus pneumoniae type 14 polysaccharide were studied by the biotin/avidin-mediated microtitre-plate lectin-binding assay and by the inhibition of lectin-glycan interactions with sugar ligands [10].
• Actinomycin D (200 microgram/kg) caused ascites and subcutaneous oedema in 40--60% of the chicks, and avidin was found only in the tissues of these inflamed animals [11].

Biological context of LOC396260

• Differences were found in some physico-chemical properties of the AVRs as compared with avidin, including lowered pI, increased glycosylation and, most notably, reversible biotin binding for two AVRs (AVR1 and AVR2) [12].
• Despite the numerous amino acid substitutions in the subunit interface regions, the AVRs form extremely stable tetramers similar to those of avidin [12].
• The Avd gene, as well as the cDNA, encodes a Gln residue at position 53 of the mature protein, which is in contrast to the previously determined amino-acid sequence [13].
• The entire coding region of preavidin (pre-Avd) containing four exons was identified by comparing the Avd gene (1119 bp) with the cDNA [13].
• Interestingly, comparison of Avd with the Avr genes showed that the introns were better conserved (on average 97%) than the exons (90%) [13].

Anatomical context of LOC396260

• A cDNA for chicken avidin was identified in a chicken oviduct cDNA library by screening with antibodies and synthetic oligodeoxyribonucleotides [14].
• In developing chick embryos, immunohistochemistry revealed avidin in skeletal muscles and growth plate hypertrophic cartilage [15].
• Avidin expression during chick chondrocyte and myoblast development in vitro and in vivo: regulation of cell proliferation [15].
• This method also showed some avidin-positive ciliated epithelial cells in chicks treated with progesterone [16].
• The results obtained by immunoelectron microscopic peroxidase techniques with high resolution power indicated that progesterone stimulation in the DES-treated chicks resulted in avidin production in the goblet cells of the oviduct epithelium [16].

Associations of LOC396260 with chemical compounds

• Avidin binds the vitamin biotin with the highest affinity known for non-covalent interactions found in nature [12].
• In this novel recombinant avidin derivative, five out of the eight arginine residues were replaced with neutral amino acids, and two of the lysine residues were replaced by glutamic acid [17].
• An avidin mRNA, approximately 700 nucleotides in length, was induced by a single injection of progesterone over a period of twenty four hours [14].
• In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known [18].
• The object of this study was to define minimized biotin-binding fragments, or 'prorecognition sites', of either the egg-white glycoprotein avidin or its bacterial analogue streptavidin [19].

Physical interactions of LOC396260

• Chicken avidin-related proteins show altered biotin-binding and physico-chemical properties as compared with avidin [12].
• Avidin is a slow-binding inhibitor of pyruvate carboxylase [20].

Regulatory relationships of LOC396260

• Estrogen regulation of the biological activity of the avian oviduct progesterone receptor and its ability to induce avidin [21].
• Avidin as a probe of the conformational changes induced in pyruvate carboxylase by acetyl-CoA and pyruvate [22].

Other interactions of LOC396260

• The gene encoding avidin (AVD) has homologues in chicken, named avidin-related genes (AVRs) [12].
• A progestin-inducible protein, avidin, was found in part of the luminal and glandular epithelium cells but not in other PR-positive cell types [23].
• The crude egg white extract was passed through a cation exchanger Streamline trade mark SP and the bound lysozyme was eluted with 5% ammonium carbonate, pH 9.0, containing 1 M NaCl after elution of avidin [24].
• Thus, ovalbumin and avidin itself, containing a mixture of oligomannose and hybrid glycans at their single glycosylation sites, may well present they glycans to the processing enzymes in a display very similar to that of the avidin close complex observed here [25].
• Also, the structures form complexes with avidin and antibiotin antibody and thus, like pyruvate carboxylase, contain biotin [26].

Analytical, diagnostic and therapeutic context of LOC396260

• Molecular cloning of the chicken avidin cDNA [14].
• Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4 [18].
• 7. Rational design of the avidin mutants was based on known crystallographic data together with comparative sequence alignment of avidin, streptavidin and a set of avidin-related genes which occur in the chicken genome [27].
• In this study, we used fluorescence in situ hybridization on extended DNA fibers (fiber-FISH) to show that the number of the AVD and AVR genes differs between individuals [28].
• Inflammation-mediated avidin gene expression in the chicken was studied using hybridization analysis, polymerase chain reaction (RT-PCR) and sequencing [3].

References