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Olfactory function varies by several orders of magnitude among healthy individuals, who may exhibit a reduced sensitivity (hyposmia), a high sensitivity (hyperosmia), or an olfactory blindness (anosmia). Environmental and genetic factors seem to account for this variability. Most of odorant molecules are hydrophobic and it has been suggested that odorants are transported to the olfactory receptors by means of odorant binding proteins (OBPs). Aim of this study was to evaluate the presence of a relationship between the olfactory performance of healthy subjects and the polymorphism in the odor binding-protein (OBPIIa) gene, the only OBP found in the olfactory epithelium of humans. Using the "Sniffin' Sticks" Extended Test we assessed the olfactory performance in 69 subjects, who were genotyped for the rs2590498 polymorphism of the OBPIIa gene, whose major allele A has been associated with a higher retronasal perception as compared to the minor allele G. We found that subjects homozygous for the A-allele exhibited threshold scores higher than subjects homozous for the G-allele or heterozygous. In addition, subjects classified as normosmic and hyposmic differed on the basis of genotype distribution and allelic frequencies. In fact, a normosmic condition was associated with genotype AA and allele A and a hyposmic condition was associated with genotype GG and allele G. In conclusion, our results show that a relationship exists between the physiological variations of olfactory performance and the OBPIIa gene polymorphism.
This article was published in the following journal.
Name: Behavioural brain research
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Proteins, usually projecting from the cilia of olfactory receptor neurons, that specifically bind odorant molecules and trigger responses in the neurons. The large number of different odorant receptors appears to arise from several gene families or subfamilies rather than from DNA rearrangement.
An ATP-binding cassette, sub-family B protein (ATP BINDING CASSETTE TRANSPORTER, SUB-FAMILY B) that functions in the transport of ANTIGENS from the CYTOPLASM to the ENDOPLASMIC RETICULUM for association with HISTOCOMPATIBILITY ANTIGENS CLASS I peptides. It also acts as a molecular scaffold for the final stage of MHC class I PROTEIN FOLDING.
GTP-BINDING PROTEINS that contain three non-identical subunits. They are found associated with members of the seven transmembrane domain superfamily of G-PROTEIN-COUPLED RECEPTORS. Upon activation the GTP-BINDING PROTEIN ALPHA SUBUNIT of the complex dissociates leaving a dimer of a GTP-BINDING PROTEIN BETA SUBUNIT bound to a GTP-BINDING PROTEIN GAMMA SUBUNIT.
A poly(A) binding protein that has a variety of functions such as mRNA stabilization and protection of RNA from nuclease activity. Although poly(A) binding protein I is considered a major cytoplasmic RNA-binding protein it is also found in the CELL NUCLEUS and may be involved in transport of mRNP particles.
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