Posterior nasal neurectomy in treatment of intractable rhinitis: A preliminary series

Objective@#To evaluate the efficacy and safety of posterior nasal neurectomy on the treatment of nasal congestion, rhinorrhea, sneezing, and post-nasal discharge in intractable rhinitis patients.@*Methods@#Design: Preliminary case series. Setting: Tertiary University Medical Center. Participant: Ten (10) patients with intractable rhinitis underwent endoscopic posterior nasal neurectomy in both sides. Symptoms were compared pre- and post-operatively one month and one year after surgery using Visual Analog Scale (VAS) scores. Endoscopic pre- and one-month post-operative Lund-Mackay scores were also compared.@*Results@#All four mean nasal symptom scores were reduced significantly at 1-month follow-up for nasal congestion (1.5 ± 1.08 vs 4.1 ± 0.5687, p = .00001), rhinorrhea (0.7 ± 0.823 vs 3.4 ± 0.966, p = .00001) post-nasal discharge (0.9 ± 0.994 vs 2.4 ± 1.5, p = .03), and sneezing (1.1 ± 0.738 vs 3 ± 0.943, p = .02). Mean endoscopic scores were also reduced significantly at one month, from 12.9 ± 2.55 to 4.2 ± 3, p = 0.0001.In the 6 patients that followed up at 1-year, post-operative mean nasal symptoms were still significantly better for congestion (0.6667 ± 0.8165 vs 4 ± 0.632, p = 0.00001), rhinorrhea (0.6667 ± 0.5164 vs 3.67 ± 1.033, p = .001), post-nasal discharge (0.1667 ± 0.40825 vs 2.17 ± 1.835, p = .033), sneezing (0.5 ± 0.54772 vs 3.17 ± 0.983, p = 0.0001). Mean post-operative VAS nasal scores and endoscopic scores were well associated (Correlation Coefficient -.648, p = .048).@*Conclusion@#Posterior nasal neurectomy could be considered as a safety and effective way to treat intractable rhinitis patients in Vietnam.

Chemical Synthesis of Glycoproteins with the Specific Installation of Gradient-Enriched 15 N-Labeled Amino Acids for Getting Insights into Glycoprotein Behavior.

Elucidating the effects of oligosaccharides on glycoprotein properties, such as local conformational changes, stability, and dynamics, has still been challenging. In this paper, a novel partial 15 N-labeling method for the amide backbone of a synthetic glycoprotein is proposed. Using solid-phase peptide synthesis (SPPS) and native chemical ligation (NCL), thirteen 15 N-labeled amino acids were inserted at specific positions of the protein backbone, while intentionally varying the enrichment of 15 N atoms. This idea discriminated even the same type of amino acid based on the intensities of 1 H-15 N HSQC signals, combined with classic homonuclear TOCSY and NOESY methods, thus allowing for understanding the dynamics of the local conformation of a synthetic homogeneous glycoprotein. Results suggested that the attachment of an oligosaccharide of either a bi-antennary complex-type or a high-mannose-type did not disturb protein conformation. However, T1 values suggested that the oligosaccharide influenced dynamics at the local conformation. Temperature-varied circular dichroism (CD) spectra and T1 values clearly indicated that oligosaccharides appeared to inhibit protein fluctuation or, in other words, stabilize protein structure. This insight into oligosaccharide behavior suggests some further effects on binding affinity between a glycoprotein and its receptor.