BackgroundEndoscopic submucosal dissection (ESD) has been widely accepted for treating superficial esophageal squamous cell carcinoma (SESCC). The aim of this study was to evaluate the efficacy and safety of ESD for SESCC and the effect of different sedation methods on their clinical outcomes.MethodsWe retrospectively analyzed a total of 169 patients (175 lesions) who underwent ESD for SESCC at Samsung Medical Center, Seoul, South Korea. Short-term and long-term clinical outcomes were evaluated and compared according to the sedation method (conscious sedation [CS] vs general anesthesia [GA]).ResultsEn bloc resection, complete resection, and curative resection (CuR) were achieved in 93.7, 74.9, and 58.9% of cancers, respectively. Perforation and stricture occurred in 8.0 and 12.0% of lesions, respectively. During a mean follow-up period of 33.7 months for survival, 3 (3.0%) patients died without evidence of recurrence after achieving CuR. During a mean follow-up period of 32.5 months for recurrence, 1 (1.0%) patient experienced lymph node metastasis. Synchronous and metachronous cancer were found in 1.0% and in 3.0% of patients, respectively. Multivariate analysis revealed that GA was associated with a higher complete resection rate and a lower perforation rate as compared to CS (odds ratio 3.401, 95% confidence interval 1.317–8.785, P = 0.011 and odds ratio 0.067, 95% confidence interval 0.006–0.775, P = 0.030, respectively).ConclusionsESD is an oncologically effective treatment modality for SESCC, particularly when CuR is achieved. Applying GA for esophageal ESD could improve the clinical outcomes of ESD in patients with SESCC.

BackgroundAbdominal tuberculosis (TB) is an uncommon form of infection with Mycobacterium tuberculosis in Korea. In this study, we aimed to highlight the clinical features, diagnostic methods, and outcomes of abdominal TB over 12 years in Southeastern Korea.MethodsA total of 139 patients diagnosed as having abdominal TB who received anti-TB medication from January 2005 to June 2016 were reviewed. Among them, 69 patients (49.6%) had luminal TB, 28 (20.1%) had peritoneal TB, 7 (5.0%) had nodal TB, 23 (16.5%) had visceral TB, and 12 (8.6%) had mixed TB.ResultsThe most frequent symptoms were abdominal pain (34.5%) and abdominal distension (21.0%). Diagnosis of abdominal TB was confirmed using microbiologic and/or histologic methods in 76 patients (confirmed diagnosis), while the remaining 63 patients were diagnosed based on clinical presentation and radiologic imaging (clinical diagnosis). According to diagnostic method, frequency of clinical diagnosis was highest in patients with luminal (50.7%) or peritoneal (64.3%) TB, while frequency of microscopic diagnosis was highest in patients with visceral TB (68.2%), and frequency of histologic diagnosis was highest in patients with nodal TB (85.2%). Interestingly, most patients, except those with nodal TB, showed a good response to anti-TB agents, with 84.2% showing a complete response. The mortality rate was only 1.4% in the present study.ConclusionsMost patients responded very well to anti-TB therapy, and surgery was required in only a minority of cases of suspected abdominal TB.

DBH is a copper-containing oxygenase that catalyzes the hydroxylation of the beta carbon of a wide variety of phenylethylamine derivatives using molecular oxygen ascorbate as cofactors. It is a glycoprotein with a molecular weight of 290,000 and consists of four identical subunits, each with a single copper atom and 5% carbohydrate by weight. The enzyme is a constituent of catecholamine storage vesicles in chromaffin cell and adrenergic neurons in the peripheral and central nervous system where it functions to synthesize noradrenaline from dopamine. Although endogenous inhibitors have been isolated, they have not been demonstrated to have a physiological function, and the kinetics of the enzyme in vitro and in vivo suggest that the enzyme is not a rate limiting step in catecholamine synthesis under normal conditions. DBH exists in both a soluble form within vesicles and as a constituent of their membranes with its active site directed inward. The significance of the partition of the enzyme into soluble and membrane forms is not understood, although the soluble form has a fivefold greater homospecific activity. DBH has been one of the most intensively investigated enzymes in neurochemistry for several reasons. It is a readily assayable constitutent of catecholamine storage vesicles and, as such, provides a convenient biochemical marker for subcellular fractionation work and studies of the cellular regulation of catecholamine synthesis, storage, and release. The adrenal medulla is a rich source of the enzyme for purification, and the purified enzyme is highly antigenic, thereby enabling the use of several immunological techniques to study the cellular dynamics of the enzyme and the organelles in which it is located. These include radioimmunoassay, immunohistochemistry, and cytochemistry. This review firstly summarizes the present state of knowledge concerning the molecular properties of DBH. It then describes the tissue, cellular, and subcellular localization of the enzyme and its physiological regulation. The remainder of the review concentrates on those aspects of research on DBH in which the authors have participated that have led to general advances such as the development of the concept of homospecific activity, the introduction of immunohistochemistry for the localization of enzymes involved in transmitter metabolism, the release of macromolecules from synaptic vesicles during the process of exocytosis, the use of antibodies to DBH administered in vivo to study the fate of synaptic vesicle membranes and to produce specific immunological lesions of noradrenergic nerves in the peripheral and central nervous system, the genetic, environmental, and physiological determinants of serum DBH activity as an index of sympathetic function in animals and man, and the question of its diagnostic value in disease.

ABSTRACr Lung innervation has been studied in the past by methylene blue staining and silver impregnation and more recently by histochemical methods. These techniques give only a partial picture of the total innervation. We have delineated the innervation of the lung in man and three other mammalian species by immunostaining with antibodies to two new markers of nervous tissue. These markers are neurone-specific enolase (NSE), an enzyme present in nerve cells in both the central and the peripheral nervous systems, and S-100, a protein found in glial cells. Throughout the respiratory tract NSE was localised in ganglion cells and nerve fibres in all species examined, while S-100 was found in the supporting glial cells of ganglia and in the Schwann cells of peripheral nerves. The distribution of NSE immunoreactivity in serial sections was compared with that of acetylcholinesterase-containing, noradrenergic, and peptide-containing nerves. In all areas NSE was found to be a specific marker for all three types of nerves. Thus these two antibodies provide an effective histological means of examining both the neuronal and the nonneuronal components of the lung innervation and should be of value in investigating this system in lung disease.The lung has a rich nerve supply, consisting of both sensory and motor divisions. The methods used to demonstrate this innervation by light microscopy in earlier studies included methylene blue and silver staining."3 More recently, histochemical techniques have been applied, for example, to localise acetylcholinesterase, which is thought to be a marker for cholinergic nerves,46 and to demonstrate formaldehyde-induced fluorescence in aminergic nerves.78 All these methods have their limitations and give only a partial view of the total innervation.Recently two highly acidic soluble proteins have been isolated from brain extracts and characterised.9The first, neurone-specific enolase (NSE), is an isoenzyme of the glycolytic enzyme enolase.'0 Antibodies raised against this enzyme and used as immunochemical reagents show that it is specifically localised in neurones" in both the central and the Address for reprint requests: