The Role of Endobronchial Ultrasound in Early-Stage Non-Small Cell Lung Cancer.

Aim The aim of this study is to assess the impact of EBUS on the concordance of clinical and pathological NSCLC staging in our center. Methods Data was collected retrospectively from the hospital database regarding patients who underwent surgical resection for early stage NSCLC between 2012 and 2017. Results A total of 251 patients were included. The mean age was 67 (±9), 55% (n=137) were male and 83% (n=209) were current/former smokers. In group A (n=154, 61%) clinical nodal stage (cN) was established from a combination of CT, PET CT and mediastinoscopy. Group B underwent additional EBUS (n=97, 39%). cN and pathological nodal staging (pN) were concordant in 78% (n=120) in group A versus 62% (n=60) in group B (p=0.009). Conclusion This study demonstrated higher rates of nodal discordance in patients who underwent EBUS which contrasts existing data that demonstrates improved concordance with EBUS. We describe these findings and potential explanations further in this study.

Monoclonal antibodies directed against extracellular matrix proteins reduce the adherence of Candida albicans to HEp-2 cells.

The presence of the extracellular matrix (ECM) proteins collagen types I and IV, laminin and fibronectin on the surface of HEp-2 cells was confirmed by flow cytometry using monoclonal antibodies. Monoclonal antibodies directed against these ECM proteins reduced the adherence of C. albicans ATCC 44990 to HEp-2 cells, the greatest reductions being evident in assays which incorporated anti-collagen type IV monoclonal antibody. The ability of sugaramines to inhibit the adherence of C. albicans to a variety of cell types has been demonstrated previously and the most significant reduction in C. albicans-HEp-2 adherence was in assays which incorporated 0.2M galactosamine. The combination of anti-collagen IV monoclonal antibody and galactosamine reduced the adherence of C. albicans to HEp-2 cells by approximately 70% (p < 0.05).

Production of autostimulatory growth factors by the human carcinoma line, RPMI 2650.

The human carcinoma line RPMI 2650 produces autocrine factors; they are detected by the ability of RPMI 2650 conditioned medium (CM) to stimulate growth in soft agar of RPMI 2650 cells plated at low density. The autocrine activity in crude CM can be fractionated by ultrafiltration into a lower molecular weight (MW) fraction (R1-30), which concentrates molecules in the 1000-30,000 Da range; and a higher MW fraction (R30) with molecules greater than 30,000 Da in a more concentrated form. R1-30 is labile to acid, base, and heat treatment, whereas R30 is stable to (and sometimes activated by) these treatments. Boiling of R30, however, renders it labile to acid, base, and trypsin treatments. CM can be separated into a weakly heparin-binding fraction (with stability properties similar, but not identical, to R1-30), and a non-heparin binding fraction (with stability properties similar to R30). RPMI 2650 cells secrete transforming growth factor (TGF)alpha- and TGF beta-like molecules, but the R1-30 fraction can be distinguished from these TGFs, and from most other known growth factors, by its unusual combination of acid lability and weak affinity for heparin. Since the R30/non-heparin binding fraction is rendered labile by boiling or acid treatment, it may represent a bound or conformationally stable form of a growth factor.

Biochemical characterisation studies on a leukocyte alloantigen expressed with high frequency in leukaemia patients.

In this report we describe, using a previously characterised monoclonal antibody (NC-2), the biochemical characteristics of a human leukaemia-associated alloantigen. Two proteins with molecular weights of 50 kDa and 15 kDa were immunoprecipitated from 125I surface labelled HL-60 cells. Both proteins appeared to be sensitive to digestion with trypsin, the 50 kDa protein in particular. Treatment with glycopeptidase F indicated the presence of N-linked oligosaccharides, whereas treatment with neuraminidase had no effect on the mobility of the antigens in SDS-PAGE indicating the absence of detectable sialic acid residues. Sensitivity to glycopeptidase F indicates that the reacting antigens are glycoproteins in nature. The antibody reacts with a range of normal tissues and appears to be associated with cytoplasmic granules in HL-60 cells.