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Kagatani, Seiya; Inaba, Noriko; Fukui, Muneo; Sonobe, Takashi

doi:10.1023/a:1011952804479

Cited by 11 publications

(2 citation statements)

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“…for azetirelin [35] and secretin [36] in rats and insulin in dogs [37]. For dairy products in which volatile fatty acids are important flavor compounds, the pH of the aqueous phase influences perception by affecting the dissociation equilibria of these acids [38].…”

Section: Introductionmentioning

confidence: 99%

Loss of the V-ATPase B1 Subunit Isoform Expressed in Non-Neuronal Cells of the Mouse Olfactory Epithelium Impairs Olfactory Function

et al. 2012

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The vacuolar proton-pumping ATPase (V-ATPase) is the main mediator of intracellular organelle acidification and also regulates transmembrane proton (H+) secretion, which is necessary for an array of physiological functions fulfilled by organs such as the kidney, male reproductive tract, lung, bone, and ear. In this study we characterize expression of the V-ATPase in the main olfactory epithelium of the mouse, as well as a functional role for the V-ATPase in odor detection. We report that the V-ATPase localizes to the apical membrane microvilli of olfactory sustentacular cells and to the basolateral membrane of microvillar cells. Plasma membrane V-ATPases containing the B1 subunit isoform are not detected in olfactory sensory neurons or in the olfactory bulb. This precise localization of expression affords the opportunity to ascertain the functional relevance of V-ATPase expression upon innate, odor-evoked behaviors in B1-deficient mice. This animal model exhibits diminished innate avoidance behavior (revealed as a decrease in freezing time and an increase in the number of sniffs in the presence of trimethyl-thiazoline) and diminished innate appetitive behavior (a decrease in time spent investigating the urine of the opposite sex). We conclude that V-ATPase-mediated H+ secretion in the olfactory epithelium is required for optimal olfactory function.

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Section: Introductionmentioning

confidence: 99%

Loss of the V-ATPase B1 Subunit Isoform Expressed in Non-Neuronal Cells of the Mouse Olfactory Epithelium Impairs Olfactory Function

et al. 2012

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“…[69,70] Recently, dynamic covalent disulfide bond exchange at the cell surface has emerged as an innovative concept to improve the cell penetration of the nanoparticles. [71,72] In this thesis, the lipoamido-dPEG8-acid with a high tension cyclic disulfide (CDs) ring is coupled to the surface amino of SiNPs through EDC/NHS coupling reaction to equip the SiNPs with CDs. When the grafted CDs approached the cell surface, the CDs will have a disulfide exchange with thiols at the cell membrane, then the towed SiNPs are readily transported into the cells, effectively avoiding the endocytosis path (Figure 2.13 a).…”

Section: Cds-assisted Intracellular Internalizationmentioning

confidence: 99%