65 research outputs found
Randomized Clinical Trial on the Efficacy and Side Effects of Tropicamide and Phenylephrine in Mydriasis for Ophthalmoscopy
Purpose: To compare the efficacy and side effects of two combinations of tropicamide and phenylephrine as mydriatics for ophthalmoscopy.
Methods: In this prospective randomized controlled trial, 51 Chinese outpatients were randomized to receive topical tropicamide 1.0% and phenylephrine 2.5% (Regime A), and 50 to receive a fixed combination of tropicamide 0.5% and phenylephrine 0.5% (Regime B). The change in horizontal pupillary diameter, subject discomfort upon instillation and the time elapsed between instillation and recovery from glare and near blur were studied.
Results: After 60 minutes, the mean increase in pupillary diameter was 3.56±0.65 mm with Regime A, and 3.04±0.62 mm with Regime B (P<0.01), but there was no difference in the proportion of subjects having a post-mydriatic pupillary diameter of 6 mm or larger (P=0.54). No subjects required additional instillation. Regime B was better tolerated (P<0.001). The median times elapsed between instillation and recovery from glare or near blur was 7 hours, without a significant difference between the two regimes (P=0.5).
Conclusions: Both regimes were effective and safe for ophthalmoscopy. However, Regime B was better tolerated. Subjects may be reassured that the side effects of glare and near blur are likely to disappear by the following day
Effects of Differential Glycosylation of Glycodelins on Lymphocyte Survival*S⃞
Glycodelin is a human glycoprotein with four reported glycoforms, namely
glycodelin-A (GdA), glycodelin-F (GdF), glycodelin-C (GdC), and glycodelin-S
(GdS). These glycoforms have the same protein core and appear to differ in
their N-glycosylation. The glycosylation of GdA is completely
different from that of GdS. GdA inhibits proliferation and induces cell death
of T cells. However, the glycosylation and immunomodulating activities of GdF
and GdC are not known. This study aimed to use ultra-high sensitivity mass
spectrometry to compare the glycomes of GdA, GdC, and GdF and to study the
relationship between the immunological activity and glycosylation pattern
among glycodelin glycoforms. Using MALDI-TOF strategies, the glycoforms were
shown to contain an enormous diversity of bi-, tri-, and tetra-antennary
complex-type glycans carrying Galβ1–4GlcNAc (lacNAc) and/or
GalNAcβ1–4GlcNAc (lacdiNAc) antennae backbones with varying levels
of fucose and sialic acid substitution. Interestingly, they all carried a
family of Sda (NeuAcα2–3(GalNAcβ1–4)Gal)-containing
glycans, which were not identified in the earlier study because of less
sensitive methodologies used. Among the three glycodelins, GdA is the most
heavily sialylated. Virtually all the sialic acid on GdC is located on the Sda
antennae. With the exception of the Sda epitope, the GdC N-glycome
appears to be the asialylated counterpart of the GdA/GdF glycomes. Sialidase
activity, which may be responsible for transforming GdA/GdF to GdC, was
detected in cumulus cells. Both GdA and GdF inhibited the proliferation,
induced cell death, and suppressed interleukin-2 secretion of Jurkat cells and
peripheral blood mononuclear cells. In contrast, no immunosuppressive effect
was observed for GdS and GdC
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