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We demonstrate the capability of using immunotargeted gold nanoshells as contrast agents for in vitro two-photon microscopy. The two-photon luminescence properties of different-sized gold nanoshells are first validated using near-infrared excitation at 780 nm. The utility of two-photon microscopy as a tool for imaging live HER2-overexpressing breast cancer cells labeled with anti-HER2-conjugated nanoshells is then explored and imaging results are compared to normal breast cells. Five different imaging channels are simultaneously examined within the emission wavelength range of 451-644 nm. Our results indicate that under near-infrared excitation, superior contrast of SK-BR-3 cancer cells labeled with immunotargeted nanoshells occurs at an emission wavelength ranging from 590 to 644 nm. Luminescence from labeled normal breast cells and autofluorescence from unlabeled cancer and normal cells remain imperceptible under the same conditions.

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Objectives/Hypothesis VT is often considered the preferred treatment for vocal feminization in transgender patients. However, Wendler glottoplasty offers a surgical option for increasing fundamental frequency and perception of vocal femininity. We aimed to determine whether the addition of glottoplasty to VT results in greater fundamental frequency elevation and improvement in quality‐of‐life measures. Study Design Retrospective case series. Methods Forty‐eight trans female patients were treated for vocal feminization. Twenty‐seven patients underwent VT, and 21 patients underwent VT with additional glottoplasty (VTWG). Pre‐ and posttreatment acoustic measures, Trans Woman Voice Questionnaire (TWVQ), and Voice Handicap Index‐10 (VHI‐10) data were compared. Results Glottoplasty in combination with VT elevated average speaking fundamental frequency (SF0) to a greater extent than VT alone (P < .0001). The VTWG group achieved a 42‐Hz increase in SF0, whereas the VT group achieved a 15‐Hz increase in SF0. In both the VT and VTWG groups, the lower bound of physiologic range increased by 18 Hz (P = .0008 and P = .016, respectively). The addition of glottoplasty also resulted in greater improvement in voice‐related quality of life. Improvement in TWVQ and VHI‐10 was significantly greater in the VTWG group than the VT group (P = .007 and P = .029, respectively). TWVQ showed statistically significant improvement in the VTWG group only. Conclusions VT results in SF0 elevation and improvement in VHI‐10. The addition of glottoplasty to VT results in further improvements in SF0 and VHI‐10 and statistically significant improvement in TWVQ. Level of Evidence 4 Laryngoscope, 131:1588–1593, 2021

A soluble sialidase that can degrade recombinant glycoproteins expressed in Chinese hamster ovary (CHO) cells has been isolated and purified to near homogeneity from the cell culture fluid of this host. Purification of approximately 34,000-fold was carried out using conventional purification techniques including sequential DEAE-Sepharose and S-Sepharose ion-exchange chromatography, followed by hydrophobic interaction chromatography with Phenyl-Toyopearl. Final purification was achieved by heparin-agarose and chromatofocusing chromatography. The minimum molecular weight of the sialidase on SDS-PAGE was approximately 43,000 Da. When the final preparation was examined under non-denaturing conditions, two major (pI = 6.8 and 7.0) and five minor electrophoretic forms with different isoelectric points were identified. The basis for the electrophoretic heterogeneity is not known, but it was not due to carbohydrate diversity since no carbohydrates were detected on the purified protein. The enzyme degraded a variety of sialyl-conjugate substrates, at a pH optimum of 5.9, including intact glycoproteins, oligosaccharides and gangliosides with a 4-fold preference for 2,3- versus 2,6-linked sialic acid residues. With ganglioside substrates, internally linked sialic acid residues were not cleaved by the enzyme. Delineation of this enzyme from the lysosomal and plasma membrane sialidases was made using inhibition studies with C-9 substituted 5-acetamido-2,6-anhydro-3,5-dideoxy-D-glycero-D-galacto-non-2- enonic acid derivatives. The enzyme was identified in several CHO cell lines by immunoblotting using antiserum raised against a synthetic peptide based on amino acid sequence of a fragment derived by trypsin digestion of the purified sialidase.(ABSTRACT TRUNCATED AT 250 WORDS)