This study was performed to investigate the biochemical properties of Acanthamoeba proteinase, its role in the pathogenesis of Acanthamoeba keratitis and the therapeutic effect of the homogenate of amniotic membrane as a proteinase inhibitors. Acanthamoeba castellanii isolated from the keratitis patient was cultured in PYG medium, in which the excretory and secretory products were analysed. The secretory proteinases of A. castellanii wre identified using in vitro azocasein assay, activity-PAGE, and various protein substrate degradation assays, and one of them was purified and characterized. The pruified secretory proteinase was a kind of serine proteinase. Its molecular weight was 105 kDa and optimal pH was 8.5. It was able to degrade the various protein substrates such as fibronectin, IgA, IgG, fibrinogen. The various proteinase ingibitors and the amniotic membrane homogenates were tested in vitro against the purified seirne proteinase. The amniotic membrane homegenates markedly showed the inhibitory effect against the enzyme activity and this inhibitory effect was also revealed in animal study. In vivo study, this purified proteinase was infected into 14 pigmented rabbit corneas, pretreated with steroids. The corneal lesions induced by both of the purified proteinase and A. castellanii, showed similar clinical findings each other, in which the stromal infiltration and opacity with epithelial defect was revealed. These corneal lesions were significantly inhibited without any side effects of the amniotic membrane homogenates. Conclusively, Acanthamoeba proteinase was closely associated with the pathogenesis of Acanthamoeba keratitis. This study provides a successful animal model of Acanthamoeba keratitis using pigmented rabbit. And the fact that Acanthamoeba-induced corneal lesions were inhibited by the amniotic membrane homogenate, suggested that the amniotic membrane homogenate have the ability of the serine protinase inhibition further investigative studies are also necessary.
Acanthamoeba castellanii ; Acanthamoeba Keratitis* ; Acanthamoeba* ; Amnion* ; Animals ; Cornea ; Fibrinogen ; Fibronectins ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin A ; Immunoglobulin G ; Keratitis ; Models, Animal ; Molecular Weight ; Peptide Hydrolases ; Serine ; Serine Proteases ; Steroids

No abstract available.
Chorionic Gonadotropin* ; Gonadotropin-Releasing Hormone* ; Gonadotropins* ; Humans* ; Progesterone* ; Superovulation*

Though basal cell carcinoma is the most frequent and increasing malignant tumor of the skin in Korea, its pathological analysis has been done only on the small numbers. So, we did a comprehensive pathologic study on the 283 patients with basal cell carcinoma diagnosed in the Department of Pathology, Seoul National(233cases) and Chung-Ang(50cases) University Hospital during 1975-1992. The age distribution was ranged from 15 to 84 years with highest incidence rate in the age group of 5th-8th decades and 83.7% of all patients were over 40 years of age. Sex difference was not noted. The most common site was face occuring in 235 out of 283cases(83.0%) especially in the eyelid(25.5%), nose(17.9%) and cheek(16.6%). The most frequent histopathologic type was solid type(54.0%) followed by mixed(23.9%), adenoid(7.5%), and metatypical(4.7%). Among 51 mixed type, all showed solid components with adenoid(51.0%) followed by morphea(25.5%) and metatypical type(13.7%). And among 14 recurrent cases, solid type is found in 50% of cases. The characteristic clinicopathological findings are solid arrangement of tumor cells with various histological pattern and predominant occurence on the face.
Incidence

BACKGROUND: This study was performed to evaluate our experience on laparoscopic appendectomy. METHODS: Retrospective analysis was performed on 2,856 patients who had been operated by laparoscopic appendectomy under diagnosis of acute appendicitis at the Sung-Ae Hospital and Kwang-Myoung Sung-Ae Hospital from October 1991 to July 1998. RESULTS: Among 2,856 patients who had undergone laparoscopic appendectomy,2,379 patients (83.3%) were operated due to simple acute appendicitis, 275 patients (9.6%) due to perforated appendicitis. Operation time was 44.6 minutes for simple acute appendicitis and 60.3 minutes for perforated appendicitis. In perforated appendicitis, intra-peritoneal irrigation and drain insertion was performed. The length of hospital stay in patient with simple acute appendicitis was 3.7 days (5.82 days in conventional appendectomy) and patients with perfotrated appendicitis was 6.1 days (9.91 days in conventional appen-dectomy). Complications such as wound infection, intra-abdomen abscess, trocar site bleeding, subcutaneous emphysema developed in 43 (1.5%) patients (79/1,947, 4.5% in conventional appendectomy). In 202 (7.1%) patients, appendix was normal, but another diseases were detected, including acute pelvic inflammation, ovarian cyst, mesenteric lymphadenitis, enteritis, diverticulitis in order. CONCLUSION: Overall complication rate was lower in laparoscopic appendectomy compared with conventional appendectomy and the length of hospitalization of laparoscopic appendectomy was shorter. When the acute appendicitis is suspected, especially in the reproductive women, the laparoscopic approach would be better diagnostic and therapeutic value than conventional method. Therefore laparoscopic appendectomy would be replaced with conventional appendectomy.
Abscess ; Appendectomy* ; Appendicitis ; Appendix ; Diagnosis ; Diverticulitis ; Enteritis ; Female ; Hemorrhage ; Hospitalization ; Humans ; Inflammation ; Length of Stay ; Mesenteric Lymphadenitis ; Ovarian Cysts ; Retrospective Studies ; Subcutaneous Emphysema ; Surgical Instruments ; Wound Infection

The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on hosts defense-oriented or regulatory proteins such as immunoglobulins, interleukin-1, and protease inhibitors was investigated. The enzyme was found to degrade secretory immunoglobulin A (sIgA), IgG, and IgM. It also degraded interleukin-1alpha (IL-1alpha) and IL-1beta. Its activity was not inhibited by endogenous protease inhibitors, such as alpha2-macroglobulin, alpha1-trypsin inhibitor, and alpha2-antiplasmin. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of hosts defense-oriented or regulatory proteins by the Acanthamoeba proteinase suggested that the enzyme might be an important virulence factor in the pathogenesis of Acanthamoeba infection.
Acanthamoeba/*enzymology/pathogenicity ; Animals ; Endopeptidases/*physiology ; Immunoglobulins/*metabolism ; Interleukin-1/*metabolism ; Protease Inhibitors/*metabolism ; Support, Non-U.S. Gov't ; Virulence

No abstract available.
Shoulder Fractures*

No abstract available.
Humans ; von Willebrand Diseases*

No abstract available.
Humans ; von Willebrand Diseases*

No abstract available.
Acute Kidney Injury* ; Fever* ; Nephritis, Interstitial*

Translocation of azurophil granules is pivotal for bactericidal activity of neutrophils, the first-line defense cells against pathogens. Previously, we reported that lysophosphatidylcholine (LPC), an endogenous lipid, enhances bactericidal activity of human neutrophils via increasing translocation of azurophil granules. However, the precise mechanism of LPC-induced azurophil granule translocation was not fully understood. Treatment of neutrophil with LPC significantly increased CD63 (an azurophil granule marker) surface expression. Interestingly, cytochalasin B, an inhibitor of action polymerization, blocked LPC-induced CD63 surface expression. LPC increased F-actin polymerization. LPC-induced CD63 surface expression was inhibited by both a Rho specific inhibitor, Tat-C3 exoenzyme, and a Rho kinase (ROCK) inhibitor, Y27632 which also inhibited LPC-induced F-actin polymerization. LPC induced Rho-GTP activation. NSC23766, a Rac inhibitor, however, did not affect LPC-induced CD63 surface expression. Theses results suggest a novel regulatory mechanism for azurophil granule translocation where LPC induces translocation of azurophil granules via Rho/ROCK/F-actin polymerization pathway.