Leveraging virtual reality for vestibular testing: Clinical outcomes from tests of dynamic visual acuity.

BACKGROUND: Virtual reality (VR) use as a platform for vestibular rehabilitation is widespread. However, the utility of VR based vestibular assessments remains unknown. OBJECTIVE: To compare dynamic visual acuity (DVA) scores, perceived balance, and perceived dizziness when using traditional versus VR environments for DVA testing among healthy individuals. METHODS: DVA testing occurred for both a traditional clinical protocol and in a VR variant. Horizontal, vertical, and no head motion conditions were conducted for both clinical and VR test protocols. DVA scores, balance ratings, and dizziness ratings were obtained per condition. Two-way ANOVAs with repeated measures were used to assess differences in DVA scores, balance, and dizziness ratings. RESULTS: No differences in DVA results, balance or dizziness ratings were observed when comparing traditional clinical protocol versus the VR variant. Differences across head motion conditions were observed, with no motion trials exhibiting significantly higher DVA scores and perceived balance, and lower perceived dizziness compared to vertical and horizontal head motion. Vertical head motion exhibited this same trend compared to horizontal. CONCLUSION: DVA testing conducted in VR demonstrated clinical utility for each measure. Effects of head motion were similar across test variants, indicating DVA testing in VR produces similar effects on vestibular function than traditional clinical testing. Additional research should be conducted to assess the feasibility of VR assessment in individuals with vestibular disorder.

Methyl farnesoate synthesis in the lobster mandibular organ: the roles of HMG-CoA reductase and farnesoic acid O-methyltransferase.

Eyestalk ablation (ESA) increases crustacean production of methyl farnesoate (MF), a juvenile hormone-like compound, but the biochemical steps involved are not completely understood. We measured the activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR) and farnesoic acid O-methyl transferase (FAOMeT), an early step and the last step in MF synthesis. ESA elevated hemolymph levels of MF in male lobsters. Enzyme activity suggested that increased MF production on day one was due largely to elevated HMGR activity while changes in FAOMeT activity closely paralleled changes in MF levels on day 14. Transcript levels for HMGR and FAOMeT changed little on day one, but both increased substantially on day 14. We treated ESA males with a partially purified mandibular organ-inhibiting hormone (MOIH) and observed a significant decline in MF levels, FAOMeT activity, and FAOMeT-mRNA levels after 5h. However, no effect was observed on HMGR activity or its mRNA indicating that they must be regulated by a separate sinus gland peptide. We confirmed that lobster HMGR was not a phosphoprotein and was not regulated by reversible phosphorylation, an important mechanism for regulating other HMGRs. Nevertheless, molecular modeling indicated that the catalytic mechanisms of lobster and mammalian HMGR were similar.

Purification and characterization of a mandibular organ protein from the American lobster, Homarus americanus: a putative farnesoic acid O-methyltransferase.

Methyl farnesoate (MF) appears to have important roles in the development, morphogenesis, and reproduction of crustaceans. To better understand the regulation of MF synthesis, we studied farnesoic acid O-methyltransferase (FAOMeT, the final enzyme in the MF biosynthetic pathway) in the American lobster (Homarus americanus). FAOMeT purified from mandibular organ (MO) homogenates had a MW of approximately 38,000. The sequences of trypsin fragments of purified FAOMeT were used to design PCR primers to amplify a cDNA fragment, which was used to isolate a full-length cDNA containing a single open reading frame (ORF) of 828 bp encoding a protein of 276 amino acids. The deduced amino acid sequence of this putative FAOMeT protein contained two copies of a conserved approximately 135 amino acid domain we term the CF (CPAMD8/FAOMeT) domain; single copies of this domain also occur in the human CPAMD8 protein (a member of the alpha-2 macroglobulin family) and an uncharacterized Drosophila protein. The recombinant protein had no FAOMeT activity. However, its addition to MO homogenates from eyestalk ablated (ESA) lobsters increased enzyme activity by up to 75%, suggesting that FAOMeT may require an additional factor or modification (e.g., phosphorylation) for its activation. The mRNA for the putative FAOMeT was primarily found in the proximal region of the MO, the predominant site of MF synthesis. FAOMeT transcripts were found in muscle tissue from ESA animals, but not in green gland, hepatopancreas, or in muscle tissue from intact animals. FAOMeT mRNA was also detected in embryos and larval stages. This is the first comprehensive report of this protein in the lobster, and is an important step in elucidating the functions of MF in these animals.