Chang Sub Uhm

Proteomic analysis in lung tissue of smokers and COPD patients.

RATIONALE Although cigarette smoking is the most important risk factor for COPD, COPD develops in only a minority of smokers, suggesting a significant genetic role. To solve the underlying pathophysiologic mechanism, it is critical to understand genes and their final product, ie, proteins. We investigated the exclusive proteins from the lung tissues obtained from COPD patients using proteomics. METHODS Nontumorous lung tissue specimens were obtained from patients who underwent surgery for lung cancer. We included 22 subjects: nonsmokers (n = 8), smokers without COPD (healthy smokers, n = 7), and smokers with COPD (n = 7). Proteins were separated from their spots with two-dimensional polyacrylamide gel electrophoresis and examined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). To validate the proteins from the above procedures, Western blotting and immunohistochemistry were conducted. RESULTS Twelve protein spots from COPD group significantly increased or decreased compared with the other two groups were chosen for MALDI-TOF-MS analysis. Eight proteins were up-regulated in the COPD group as compared with the nonsmokers. Meanwhile, five proteins from the COPD group were up-regulated and five were down-regulated when compared with healthy smokers. Of these, matrix metalloproteinase (MMP)-13 and thioredoxin-like 2 were significantly increased in the COPD patients by Western blot and immunohistochemistry. MMP-13 was mainly expressed in the alveolar macrophages and type II pneumocytes; however, thioredoxin-like 2 was primarily seen in the bronchial epithelium. CONCLUSIONS MMP-13 and thioredoxin-like 2 in lungs increased in patients with COPD. MMP-13 was mainly expressed in the alveolar macrophages and type II pneumocytes. In contrast, thioredoxin-like 2 was primarily seen in the bronchial epithelium.

An electron microscopic study--correlation of gastroesophageal reflux disease and laryngopharyngeal reflux.

Laryngopharyngeal reflux (LPR) originates from regurgitation of gastric contents, a mechanism seemingly identical to gastroesophageal reflux disease (GERD). Some researchers postulate a connection between LPR and GERD, whereas some assert LPR is a disease apart from GERD. We examined symptoms of GERD from LPR patients, and performed gastrointestinal endoscopy and transmission electron microscopy (TEM) to evaluate GERD findings from these patients.

Electron microscopic study of intercellular space: Correlation analysis of bronchial asthma and gastroesophageal reflux disease

Background and Aims:  Bronchial asthma (BA) is considered an extra‐esophageal syndrome of gastroesophageal reflux disease (GERD) with poor pathophysiological background. We analyzed the correlation between GERD and BA, examining esophageal epithelium with transmission electron microscopy (TEM), along with clinical findings.

Myoblast Transfer Therapy on mdx Mouse

Purpose : To observe dystrophin formation and histological improvement in dystrophic muscle of mdx mouse after normal myoblast injection. Materials and Methods : Cultured myoblasts from genetically normal rats were injected into the right quadriceps femoris of a 6-week-old mdx mouse (n=9). dPBS was injected into the left quadriceps femoris as a control. One, 2, and 3 months after injection, The control and experimental group were compared histologically and by dystrophin immunostaining. Results : When compared with controls 3 months postoperatively, quadriceps femoris in the experimental group exhibited greater cross-sectional area and total fiber number, and the experimental animals contained more normal-appearing and less abnormalappearing fibers than the control group. Most of the fibers in the experimental group showed positive results in dystrophin immunostaining, whereas immunostaining of mdx muscle fibers in the control group was completely negative. Conclusion : This study shows that normal myoblast injection improved the muscle architecture histologically and produced dystrophin protein in dystrophic muscle.