No abstract available.
Granuloma* ; Intubation*

The pancreas is formed from dorsal and ventral parts which normally fuse in the second month of intrauterine life. Pancreas divisum occurs when the ventral and dorsal elements fail to fuse; as a result, the main bulk of the pancreas drains through the accessory papilla. It is a congenital variait of pancreatic ductal fusion and drainage anomalies. Since the accessoy papilla and Santorinis duct are too all to accept total pancreatic secretion, obstructive pain and pancreatitis may result. Between March 1983 and February 1988, 631 patients underwent endoscopic retrograde cholangiopancreatography(ERCP) in our hospital. We experiericed one case of pancreas divisum. And then, we report it with brief review of literatures.
Drainage ; Humans ; Pancreas* ; Pancreatic Ducts ; Pancreatitis

No abstract available.
Lung*

No abstract available.
Choriocarcinoma* ; Female ; Lung Neoplasms* ; Lung* ; Pregnancy

Fibrolipoma is a rare variant of lipomas which shows distinct pathologic findings with both component of mature adipose cells and broad bands of dense fibrous connective tissue. A 52-year-old woman presented with 2X2cm sized, indurated, slightly elevated and slightly tender subcutaneous mass which slowly enlarged during the last four to five years accompanied by slight tenderness on the right upper back. The laboratory examination showed non-specific findings. Histopathologic findings revealed a well-defined mass composed of eosinophilic dense connective tissue bands with mature adipose cells scattered throughout the mass. The lesion was totally excised and she showed no evidence of recurrence after 6 months of follow-up.
Connective Tissue ; Eosinophils ; Female ; Follow-Up Studies ; Humans ; Lipoma ; Middle Aged ; Recurrence

No abstract available.
Arrhythmias, Cardiac* ; Humans ; Mitral Valve*

Plasmodium falciparum can invade all stages of red blood cells, while Plasmodium vivax can invade only reticulocytes. Although many P. vivax proteins have been discovered, their functions are largely unknown. Among them, P. vivax reticulocyte binding proteins (PvRBP1 and PvRBP2) recognize and bind to reticulocytes. Both proteins possess a C-terminal hydrophobic transmembrane domain, which drives adhesion to reticulocytes. PvRBP1 and PvRBP2 are large (> 326 kDa), which hinders identification of the functional domains. In this study, the complete genome information of the P. vivax RBP family was thoroughly analyzed using a prediction server with bioinformatics data to predict B-cell epitope domains. Eleven pvrbp family genes that included 2 pseudogenes and 9 full or partial length genes were selected and used to express recombinant proteins in a wheat germ cell-free system. The expressed proteins were used to evaluate the humoral immune response with vivax malaria patients and healthy individual serum samples by protein microarray. The recombinant fragments of 9 PvRBP proteins were successfully expressed; the soluble proteins ranged in molecular weight from 16 to 34 kDa. Evaluation of the humoral immune response to each recombinant PvRBP protein indicated a high antigenicity, with 38-88% sensitivity and 100% specificity. Of them, N-terminal parts of PvRBP2c (PVX_090325-1) and PvRBP2 like partial A (PVX_090330-1) elicited high antigenicity. In addition, the PvRBP2-like homologue B (PVX_116930) fragment was newly identified as high antigenicity and may be exploited as a potential antigenic candidate among the PvRBP family. The functional activity of the PvRBP family on merozoite invasion remains unknown.
Epitopes, B-Lymphocyte/*chemistry/genetics/*immunology ; Female ; Humans ; Immunodominant Epitopes/chemistry/genetics/*immunology ; Malaria, Vivax/immunology/*parasitology ; Middle Aged ; Plasmodium vivax/chemistry/genetics/*immunology ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry/genetics/*immunology ; Reticulocytes/*parasitology

BACKGROUND: The purpose of this retrospective study was to evaluate the clinical utility of an implant with a sandblasted, large-grit, acid-etched (SLA) surface and internal connection. METHODS: Six patients who received dental implants in the Department of Oral and Maxillofacial Surgery, Chonnam National University Dental Hospital, were analyzed by factors influencing the success rate and marginal bone loss. Factors included patient’s age, sex, implant installation site, whether bone graft was done, type of bone graft materials, approaching method if sinus lift was done, and the size of the fixture. In addition, the marginal bone loss was analyzed by using a radiograph. RESULTS: All implants were successful, and the cumulative survival rate was 100 %. Average marginal bone loss of 6 months after the installation was 0.52 mm and 20 months after the functional loading was 1.06 mm. Total marginal bone resorption was 1.58 mm on average. There was no statistically significant difference in mesial and distal marginal bone loss. CONCLUSIONS: The short-term clinical success rate of the implant with an SLA surface and internal connection was satisfactory. Moreover, the marginal bone loss was also consistent with the implant success criteria.
Bone Resorption ; Clinical Study* ; Dental Implants ; Humans ; Jeollanam-do ; Methods ; Retrospective Studies* ; Surgery, Oral ; Survival Rate ; Transplants

The discovery and understanding of antigenic proteins are essential for development of a vaccine against malaria. In Plasmodium falciparum, Pf92 have been characterized as a merozoite surface protein, and this protein is expressed at the late schizont stage, but no study of Pv92, the orthologue of Pf92 in P. vivax, has been reported. Thus, the protein structure of Pv92 was analyzed, and the gene sequence was aligned with that of other Plasmodium spp. using bioinformatics tools. The recombinant Pv92 protein was expressed and purified using bacterial expression system and used for immunization of mice to gain the polyclonal antibody and for evaluation of antigenicity by protein array. Also, the antibody against Pv92 was used for subcellular analysis by immunofluorescence assay. The Pv92 protein has a signal peptide and a sexual stage s48/45 domain, and the cysteine residues at the N-terminal of Pv92 were completely conserved. The N-terminal of Pv92 was successfully expressed as soluble form using a bacterial expression system. The antibody raised against Pv92 recognized the parasites and completely merged with PvMSP1-19, indicating that Pv92 was localized on the merozoite surface. Evaluation of the human humoral immune response to Pv92 indicated moderate antigenicity, with 65% sensitivity and 95% specificity by protein array. Taken together, the merozoite surface localization and antigenicity of Pv92 implicate that it might be involved in attachment and invasion of a merozoite to a new host cell or immune evasion during invasion process.
Animals ; Computational Biology ; Cysteine ; Fluorescent Antibody Technique ; Humans ; Immune Evasion ; Immunity, Humoral ; Immunization ; Malaria ; Merozoites* ; Mice ; Parasites ; Plasmodium falciparum ; Plasmodium vivax* ; Plasmodium* ; Protein Array Analysis ; Protein Sorting Signals ; Schizonts ; Sensitivity and Specificity

Plasmodium vivax produces numerous caveola-vesicle complex (CVC) structures beneath the membrane of infected erythrocytes. Recently, a member helical interspersed subtelomeric (PHIST) superfamily protein, PcyPHIST/CVC-81₉₅, was identified as CVCs-associated protein in Plasmodium cynomolgi and essential for survival of this parasite. Very little information has been documented to date about PHIST/CVC-81₉₅ protein in P. vivax. In this study, the recombinant PvPHIST/CVC-81₉₅ N and C termini were expressed, and immunoreactivity was assessed using confirmed vivax malaria patients sera by protein microarray. The subcellular localization of PvPHIST/CVC-81₉₅ N and C termini in blood stage parasites was also determined. The antigenicity of recombinant PvPHIST/CVC-81₉₅ N and C terminal proteins were analyzed by using serum samples from the Republic of Korea. The results showed that immunoreactivities to these proteins had 61% and 43% sensitivity and 96.9% and 93.8% specificity, respectively. The N terminal of PvPHIST/CVC-81₉₅ which contains transmembrane domain and export motif (PEXEL; RxLxE/Q/D) produced CVCs location throughout the erythrocytic-stage parasites. However, no fluorescence was detected with antibodies against C terminal fragment of PvPHIST/CVC-81₉₅. These results suggest that the PvPHIST/CVC-81₉₅ is localized on the CVCs and may be immunogenic in natural infection of P. vivax.
Antibodies ; Erythrocytes ; Fluorescence ; Humans ; Malaria, Vivax ; Membranes ; Parasites ; Plasmodium cynomolgi ; Plasmodium vivax* ; Plasmodium* ; Protein Array Analysis ; Republic of Korea ; Sensitivity and Specificity