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Gene Review

AVD  -  avidin

Gallus gallus

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Disease relevance of LOC396260


Psychiatry related information on LOC396260


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


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


Regulatory relationships of LOC396260


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


  1. Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 A resolution. Pugliese, L., Coda, A., Malcovati, M., Bolognesi, M. J. Mol. Biol. (1993) [Pubmed]
  2. Biochemical characterization and crystal structure of a recombinant hen avidin and its acidic mutant expressed in Escherichia coli. Nardone, E., Rosano, C., Santambrogio, P., Curnis, F., Corti, A., Magni, F., Siccardi, A.G., Paganelli, G., Losso, R., Apreda, B., Bolognesi, M., Sidoli, A., Arosio, P. Eur. J. Biochem. (1998) [Pubmed]
  3. Induction of chicken avidin and related mRNAs after bacterial infection. Kunnas, T.A., Wallén, M.J., Kulomaa, M.S. Biochim. Biophys. Acta (1993) [Pubmed]
  4. Localization of individual calcium channels at the release face of a presynaptic nerve terminal. Haydon, P.G., Henderson, E., Stanley, E.F. Neuron (1994) [Pubmed]
  5. Avidin is induced in chicken embryo fibroblasts by viral transformation and cell damage. Korpela, J., Kulomaa, M., Tuohimaa, P., Vaheri, A. EMBO J. (1983) [Pubmed]
  6. Polymer-protomer transition of acetyl-CoA carboxylase occurs in vivo and varies with nutritional conditions. Ashcraft, B.A., Fillers, W.S., Augustine, S.L., Clarke, S.D. J. Biol. Chem. (1980) [Pubmed]
  7. Induction of avidin messenger ribonucleic acid in the chick oviduct by progesterone and other steroids. Kunnas, T.A., Joensuu, T.K., Viitala, K.K., Sopanen, P., Tuohimaa, P., Kulomaa, M.S. Endocrinology (1992) [Pubmed]
  8. Three-dimensional structures of avidin and the avidin-biotin complex. Livnah, O., Bayer, E.A., Wilchek, M., Sussman, J.L. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  9. Actin gene expression visualized in chicken muscle tissue culture by using in situ hybridization with a biotinated nucleotide analog. Singer, R.H., Ward, D.C. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  10. Carbohydrate specificity of a galectin from chicken liver (CG-16). Wu, A.M., Wu, J.H., Tsai, M.S., Kaltner, H., Gabius, H.J. Biochem. J. (2001) [Pubmed]
  11. Progesterone-independent avidin induction in chick tissues caused by tissue injury and inflammation. Elo, H.A., Kulomaa, M.S., Tuohimaa, P.J. Acta Endocrinol. (1979) [Pubmed]
  12. Chicken avidin-related proteins show altered biotin-binding and physico-chemical properties as compared with avidin. Laitinen, O.H., Hytönen, V.P., Ahlroth, M.K., Pentikäinen, O.T., Gallagher, C., Nordlund, H.R., Ovod, V., Marttila, A.T., Porkka, E., Heino, S., Johnson, M.S., Airenne, K.J., Kulomaa, M.S. Biochem. J. (2002) [Pubmed]
  13. Cloning and sequencing of the chicken egg-white avidin-encoding gene and its relationship with the avidin-related genes Avr1-Avr5. Wallén, M.J., Laukkanen, M.O., Kulomaa, M.S. Gene (1995) [Pubmed]
  14. Molecular cloning of the chicken avidin cDNA. Gope, M.L., Keinänen, R.A., Kristo, P.A., Conneely, O.M., Beattie, W.G., Zarucki-Schulz, T., O'Malley, B.W., Kulomaa, M.S. Nucleic Acids Res. (1987) [Pubmed]
  15. Avidin expression during chick chondrocyte and myoblast development in vitro and in vivo: regulation of cell proliferation. Zerega, B., Camardella, L., Cermelli, S., Sala, R., Cancedda, R., Descalzi Cancedda, F. J. Cell. Sci. (2001) [Pubmed]
  16. Immunoelectron microscopic localization of a progesterone-inducible protein (avidin) in the chick oviduct mucosa. Rantala, I., Helin, H., Elo, H.A. Endocrinology (1982) [Pubmed]
  17. Recombinant NeutraLite avidin: a non-glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non-specific binding properties. Marttila, A.T., Laitinen, O.H., Airenne, K.J., Kulik, T., Bayer, E.A., Wilchek, M., Kulomaa, M.S. FEBS Lett. (2000) [Pubmed]
  18. Binding Properties of HABA-Type Azo Derivatives to Avidin and Avidin-Related Protein 4. Repo, S., Paldanius, T.A., Hyt??nen, V.P., Nyholm, T.K., Halling, K.K., Huuskonen, J., Pentik??inen, O.T., Rissanen, K., Slotte, J.P., Airenne, T.T., Salminen, T.A., Kulomaa, M.S., Johnson, M.S. Chem. Biol. (2006) [Pubmed]
  19. Studies on the biotin-binding site of avidin. Minimized fragments that bind biotin. Hiller, Y., Bayer, E.A., Wilchek, M. Biochem. J. (1991) [Pubmed]
  20. Avidin is a slow-binding inhibitor of pyruvate carboxylase. Duggleby, R.G., Attwood, P.V., Wallace, J.C., Keech, D.B. Biochemistry (1982) [Pubmed]
  21. Estrogen regulation of the biological activity of the avian oviduct progesterone receptor and its ability to induce avidin. Hora, J., Gosse, B., Rasmussen, K., Spelsberg, T.C. Endocrinology (1986) [Pubmed]
  22. Avidin as a probe of the conformational changes induced in pyruvate carboxylase by acetyl-CoA and pyruvate. Attwood, P.V., Mayer, F., Wallace, J.C. FEBS Lett. (1986) [Pubmed]
  23. Distribution of estrogen and progesterone receptors and steroid-regulated gene products in the chick oviduct. Isola, J.J. Mol. Cell. Endocrinol. (1990) [Pubmed]
  24. An integrated process for purification of lysozyme, ovalbumin, and ovomucoid from hen egg white. Roy, I., Rao, M.V., Gupta, M.N. Appl. Biochem. Biotechnol. (2003) [Pubmed]
  25. The effect of the protein matrix on glycoprotein processing by oviduct Golgi enzymes. Shao, M.C., Wold, F. J. Biol. Chem. (1989) [Pubmed]
  26. A re-examination of the electron microscopic appearance of pyruvate carboxylase from chicken liver. Cohen, N.D., Beegen, H., Utter, M.F., Wrigley, N.G. J. Biol. Chem. (1979) [Pubmed]
  27. Engineering of chicken avidin: a progressive series of reduced charge mutants. Marttila, A.T., Airenne, K.J., Laitinen, O.H., Kulik, T., Bayer, E.A., Wilchek, M., Kulomaa, M.S. FEBS Lett. (1998) [Pubmed]
  28. Copy-number fluctuation by unequal crossing-over in the chicken avidin gene family. Ahlroth, M.K., Ahlroth, P., Kulomaa, M.S. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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