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1.
Sci Rep ; 11(1): 6950, 2021 03 26.
Article in English | MEDLINE | ID: mdl-33772040

ABSTRACT

Qualitative analysis of fundus photographs enables straightforward pattern recognition of advanced pathologic myopia. However, it has limitations in defining the classification of the degree or extent of early disease, such that it may be biased by subjective interpretation. In this study, we used the fovea, optic disc, and deepest point of the eye (DPE) as the three major markers (i.e., key indicators) of the posterior globe to quantify the relative tomographic elevation of the posterior sclera (TEPS). Using this quantitative index from eyes of 860 myopic patients, support vector machine based machine learning classifier predicted pathologic myopia an AUROC of 0.828, with 77.5% sensitivity and 88.07% specificity. Axial length and choroidal thickness, the existing quantitative indicator of pathologic myopia only reached an AUROC of 0.758, with 75.0% sensitivity and 76.61% specificity. When all six indices were applied (four TEPS, AxL, and SCT), the discriminative ability of the SVM model was excellent, demonstrating an AUROC of 0.868, with 80.0% sensitivity and 93.58% specificity. Our model provides an accurate modality for identification of patients with pathologic myopia and may help prioritize these patients for further treatment.


Subject(s)
Axial Length, Eye/pathology , Fovea Centralis/pathology , Myopia, Degenerative/pathology , Optic Disk/pathology , Support Vector Machine , Biomarkers/analysis , Female , Fundus Oculi , Humans , Male , Middle Aged , Myopia, Degenerative/diagnosis , Retrospective Studies , Sclera/pathology , Tomography, Optical Coherence/methods
2.
Invest Ophthalmol Vis Sci ; 54(10): 6982-90, 2013 Oct 23.
Article in English | MEDLINE | ID: mdl-24030460

ABSTRACT

PURPOSE: To investigate the patterns of retinal nerve fiber layer (RNFL) defects in mean deviation-matched early glaucomatous eyes with either superior or inferior visual hemifield loss. METHODS: Seventy-five open-angle glaucoma patients with isolated parafoveal scotoma (PFS) within a central 10° of fixation, and 62 patients with isolated peripheral nasal scotoma (PNS) in the nasal periphery outside 10° of fixation were enrolled if the scotoma involved only one hemifield. The relationship between the mean threshold sensitivity (MS) of each corresponding VF sector and optical coherence tomography-measured RNFL thickness was assessed by logarithmic regression analysis. The angular widths and locations of the RNFL defects were measured from red-free fundus photographs. RESULTS: Eyes with superior PFS showed a significant relationship between RNFL thickness and corresponding MS at clock-hours 7 and 8 while eyes with inferior PFS had significant relationship at clock-hours 9, 10, and 11. Eyes with superior PNS displayed a significant relationship between RNFL thickness and MS at clock-hour 7 while eyes with inferior PNS showed significant relationship at clock-hours 11 and 12. Overall, fundus photographs-measured RNFL defect associated with inferior hemifield loss (inferior PFS + PNS) was significantly wider and closer to the horizontal meridian than those with superior hemifield loss (superior PFS + PNS) (P = 0.032 and 0.009, angular width and location, respectively). CONCLUSIONS: A superior RNFL defect associated with inferior hemifield loss was wider and was located closer to the horizontal meridian of the optic disc than an inferior defect with superior field loss, particularly in patients with central VF loss.


Subject(s)
Glaucoma, Open-Angle/pathology , Glaucoma, Open-Angle/physiopathology , Nerve Fibers/pathology , Sensory Thresholds/physiology , Adult , Aged , Female , Fundus Oculi , Humans , Male , Middle Aged , Regression Analysis , Tomography, Optical Coherence , Visual Fields/physiology
3.
Immune Netw ; 9(4): 138-46, 2009 Aug.
Article in English | MEDLINE | ID: mdl-20157601

ABSTRACT

BACKGROUND: The MHC region of the chromosome contains a lot of genes involved in immune responses. Here we have investigated the mouse NG29/Cd320 gene in the centrometrically extended MHC region of chromosome 17. METHODS: We cloned the NG29 gene by RT-PCR and confirmed the tissue distribution of its gene expression by northern blot hybridization. We generated the NG29 gene expression constructs and polyclonal antibody against the NG29 protein to perform the immunofluorescence, immunoprecipitation and flow cytometric analysis. RESULTS: The murine NG29 gene and its human homologue, the CD320/8D6 gene, were similar in the gene structure and tissue expression patterns. We cloned the NG29 gene and confirmed its expression in plasma membrane and intracellular compartments by transfecting its expresssion constructs into HEK 293T cells. The immunoprecipitation studies with rabbit polyclonal antibody raised against the NG29-NusA fusion protein indicated that NG29 protein was a glycoprotein of about 45 kDa size. A flow cytometric analysis also showed the NG29 expression on the surface of Raw 264.7 macrophage cell line. CONCLUSION: These findings suggested that NG29 gene in mouse extended MHC class II region was the orthologue of human CD320 gene even though human CD320/8D6 gene was located in non-MHC region, chromosome 19p13.

4.
Exp Mol Med ; 35(4): 310-6, 2003 Aug 31.
Article in English | MEDLINE | ID: mdl-14508072

ABSTRACT

We have used a surface plasmon resonance biosensor (SPR, BIACORE 2000) to detect antibodies against glucose 6-phosphate isomerase (GPI) in synovial fluids of rheumatoid arthritis (RA) and osteoarthritis (OA). Recombinant human GPI proteins fused with or without NusA were expressed in E. coli, purified to homogeneity and immobilized in flow cells of CM5 sensor chips. The flow cells immobilized with NusA protein or bovine serum albumin were used to monitor non-specific binding. Synovial fluid samples from RA patients showed a significantly higher level of binding to recombinant GPI proteins than samples from OA patients. Proteins which bound to the recombinant GPI proteins were confirmed to be immunoglobulin through the administration of anti-human immunoglobulin. NusA fusion protein was excellent for this assay because of a low background binding activity in the SPR analysis and its advantage of increased solubility in recombinant protein production. These results suggested a useful utilization of recombinant NusA-GPI fusion protein for the detection of autoantibodies against GPI in RA patients.


Subject(s)
Antibodies/immunology , Arthritis, Rheumatoid/immunology , Glucose-6-Phosphate Isomerase/immunology , Synovial Fluid/immunology , Aged , Escherichia coli Proteins , Female , Glucose-6-Phosphate Isomerase/genetics , Glucose-6-Phosphate Isomerase/metabolism , Humans , Male , Middle Aged , Osteoarthritis/immunology , Peptide Elongation Factors/genetics , Peptide Elongation Factors/metabolism , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Surface Plasmon Resonance , Transcription Factors/genetics , Transcription Factors/metabolism , Transcriptional Elongation Factors
5.
FEBS Lett ; 540(1-3): 217-22, 2003 Apr 10.
Article in English | MEDLINE | ID: mdl-12681511

ABSTRACT

We studied the role of lipid rafts and actin cytoskeleton in CD99-mediated signaling to elucidate the mechanism of protein transport upon CD99 engagement. CD99 engagement in Jurkat cells elicited the exocytic transport of GM1 as well as several surface molecules closely related with CD99 functions. In addition, CD99 molecules were rapidly incorporated into lipid rafts and appeared to rearrange the actin cytoskeleton upon CD99 stimulation. Association of CD99 with actin cytoskeleton was inhibited by methyl-beta-cyclodextrin, while CD99-mediated GM1 clustering was inhibited by cytochalasin D. Therefore, we suggest that CD99 may play a role in the vesicular transport of transmembrane proteins and lipid rafts from the intracellular location to the cell surface, possibly by effecting actin cytoskeleton reorganization.


Subject(s)
Actins/metabolism , Antigens, CD/metabolism , Cell Adhesion Molecules/metabolism , Cytoskeleton/metabolism , Exocytosis , G(M1) Ganglioside/metabolism , 12E7 Antigen , Biological Transport , Humans , Jurkat Cells
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