Dacryolithiasis is one of the causes of acquired nasolacrimal duct obstruction, although its origin is unclear. The purpose of this study was to investigate the differences in tear constituents between patients with nasolacrimal duct obstruction with dacryoliths and those without dacryoliths. In a prospective case-control study, undiluted tears were collected from 30 eyes from 30 patients with partial acquired nasolacrimal duct obstruction (PANDO) consisting of 17 PANDO patients with dacryoliths and 13 PANDO patients without dacryoliths. The pH, and the Na⁺, K⁺, Cl^–, total calcium and total protein concentrations were determined. The composition of the tear proteins was assessed by cellulose acetate electrophoresis. In the tear samples from 17 eyes with PANDO/dacryoliths, the mean ± SD K⁺ level was 15.6 ± 3.1 mEq/l. In the tear samples from 13 PANDO controls, the mean ± SD K⁺ level was 19.8 ± 4.9 mEq/l. The difference between the two groups was statistically significant (p = 0.02). In the tear samples from PANDO/dacryolith patients, the mean ± SD total protein level was 129.0 ± 72.9 mg/dl. In the tear samples from the PANDO controls the mean ± SD total protein level was 261.6 ± 132.5 mg/dl. The difference between the two groups was statistically significant (p = 0.00). In the tear protein fractions from electrophoresis, a low level of lysozyme was observed in the PANDO/dacryolith samples compared with the PANDO control samples (p = 0.03). The tears from patients with PANDO due to dacryoliths showed a change in the concentrations of electrolytes and protein, particularly lysozyme, compared with that of the patients with PANDO without dacryoliths, which may be related to the pathogenesis of dacryoliths.

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Purpose: To compare inferior orbital wall morphology between isolated inferior and medial orbital wall fracture patients. Methods: The morphologic properties of patients with isolated blow-out fractures involving the medial wall or inferior wall treated from August 2004 to August 2009 were reviewed. The cross-sectional area, thickness, gradient, and curvature of the inferior wall were measured via orbital CT in the opposite non-traumatized eye. Results: Patients with isolated inferior wall fractures (n = 77) and isolated medial wall fractures (n = 78) evidenced no differences in sex, age, etiology of trauma, laterality of trauma, and associated concomitant intraocular injuries. The cross-sectional area, thickness, and gradient of the inferior wall did not differ significantly between the 2 groups. However, the coefficient of curvature was significantly greater in patients with inferior wall fracture than in patients with medial wall fracture (0.016 ± 0.006 vs. 0.006 ± 0.002, respectively; p = 0.000). Conclusion: Patients with more convex and steep inferior walls are more likely to incur isolated inferior wall fractures than isolated medial wall fractures.

Tropomyosin-related kinase A (TrkA) is a receptor-type protein tyrosine kinase and exploits pleiotypic roles via nerve growth factor (NGF)-dependent or NGF-independent mechanisms in various cell types. Here, we showed that the inhibition of TrkA activity by GW441756 resulted in the suppression of tyrosine phosphorylation of cellular proteins including extracellular signal-regulated protein kinase (ERK) and c-Jun N-terminal kinase (JNK). To find novel targets associated with TrkA-mediated tyrosine phosphorylation signaling pathways, we investigated GW441756 effects on TrkA-dependent targets in SK-N-MC neuroblastoma cells by proteomic analysis. The major TrkA-dependent protein spots controlled by GW441756 were determined by PDQuest image analysis, identified by MALDI-TOF MS and MALDI-TOF/TOF MS/MS, and verified by 2DE/Western blot analysis. Thus, we found that most of the identified protein spots were modified forms in a normal condition, and their modifications were regulated by TrkA activity. Especially, our results demonstrated that the modifications of α-tubulin and heterogeneous nuclear ribonucleoproteins C1/C2 (hnRNP C1/C2) were significantly upregulated by TrkA, whereas α-enolase modification was downregulated by TrkA, and it was suppressed by GW441756, indicating that TrkA activity is required for their modifications. Taken together, we suggest here that the major novel TrkA-dependent targets such as α-tubulin, hnRNP C1/C2, and α-enolase could play an essential role in TrkA-mediated tyrosine phosphorylation signaling pathways via regulation of their posttranslational modifications.