There was no difference of the 30-day mortality and intubation rate between HFNC and NIV groups.

Our findings suggest a brief intervention for rehabilitation nursing with more retainable, feasible, and cost-effective strategies to enhance self-management among the elderly patients with COPD.

BackgroundThe prevalence rate of pulmonary tuberculosis (PTB) is steadily decreasing in South Korea. However, PTB is a disease with relatively high mortality and morbidity rates throughout Korea. Although there are many studies and statistics about the risk factors of PTB mortality in many countries, there are only a limited number of domestic papers on this topic. The aim of this study is to determine predictive factors for mortality among in-hospital patients associated with PTB.MethodsFrom December 2006 to January 2011, we reviewed medical records of 2,122 adult patients diagnosed with tuberculosis at a single tertiary hospital in a suburban area. In this study period, 960 patients were diagnosed with PTB by positive Acid fast bacilli smear and/or mycobacterial culture of the respiratory specimen. We compared the groups of patients deceased and patients discharged alive with PTB. The number of dead patients was 82 (47 males, 35 females).ResultsMortality was significantly associated with increased values of white blood cells (WBC), blood urine nitrogen (BUN), creatinine, C-reactive protein (CRP), numbers of involved lung field, and length of hospitalization. Also, it was associated with the decreased values of hemoglobin, lymphocyte, sodium, albumin, and cholesterol. Furthermore, admission through the emergency department, initial intensive care unit admission, and drug resistant PTB affected mortality in PTB patients. Independent predictors associated with PTB mortality are BUN, initial intensive care unit care, and admission during treatment of tuberculosis.ConclusionIn our study, mortality of pulmonary tuberculosis was related with parameters associated with nutritional status, disease severity at the time of admission, and drug resistance.

Pneumocystis carinii pneumonia remains an important, lifethreatening opportunistic infection in immunocompromised patients. It is particularly prevalent among those with AIDS, hematologic or solid malignancies, or transplanted organs and among patients receiving chronic immunosuppressive therapies, particularly corticosteroids (23,25,35,39,59). Histologically, P. carinii pneumonia is characterized by filling of the alveolar space with distinctive protein-rich frothy exudates containing prominent aggregates of organisms (32). The exact chemical nature of the proteinaceous alveolar exudates is not known, but prior studies have shown that these exudates are particularly rich in surfactant proteins A and D (SP-A and SP-D), fibronectin, and vitronectin (54). Interactions of these host components, particularly the surfactant-associated proteins, with P. carinii has been an area of intensive investigation (37,47,53,58,60).Pulmonary surfactant is a complex mixture of lipids and proteins synthesized by alveolar type II cells and secreted into the alveolar spaces. This surfactant exerts multiple functions including reduction of alveolar surface tension and modulation of host defense and inflammatory responses (20,29). It contains at least four associated proteins, of which two, SP-B and SP-C, are hydrophobic and two, SP-A and SP-D, are hydrophilic. SP-A and SP-D have been demonstrated to accumulate during P. carinii pneumonia, while SP-B and SP-C are suppressed during this infection (3,42,44). These surfactantassociated proteins have further been shown to modulate the interaction of P. carinii with host cells and to regulate host inflammatory responses to the organism (26,30,42,57).SP-D is a soluble, collagenous protein synthesized and secreted by type II pneumocytes and nonciliated bronchiolar cells (43). Structurally, it belongs to the group III, mammalian C-type lectin family that includes SP-A, mannose binding protein, and bovine conglutinin (21). SP-D is composed of 43-kDa monomers, each consisting of four major domains: a short cysteine-containing amino-terminal region, a triple helical collagenous domain, a trimeric coiled neck region, and a globular carboxy-terminal carbohydrate recognition domain (CRD) (11). These monomers are assembled into triple helical trimers, which form a single collagenous "arm" displaying the CRDs on the end. Four trimeric subunits undergo disulfide cross-linking within their amino-terminal domains to form a cruciform dodecameric structure (10). Although rat SP-D is assembled as dodecamers, human SP-D appears to consist of a complex of dodecamers and variable proportions of higherorder multimers and trimers (11). In addition, the extent of SP-D binding to P. carinii ligands appears to correlate with the number of CRDs in higher-order multimers of the molecule (55).Recent