Single-incision versus multiport video-assisted thoracoscopic surgery in the treatment of lung cancer: a systematic review and meta-analysis

<p><b>Objectives:</b> Recent studies compared single-incision thoracoscopic surgery (SITS) with more widely used conventional multiport video-assisted thoracoscopic surgery in the treatment of lung cancer. To establish the safety and feasible of SITS in the treatment of lung cancer, we conducted this systematic review and meta-analysis.</p> <p><b>Methods:</b> Eleven studies were identified from the databases of PubMed, Cochrane Library, SpringerLink, and ScienceDirect. The randomized controlled trials (RCTs) and non-randomized studies evaluated the outcomes of SITS compared with multiport video-assisted thoracoscopic surgery in the treatment of lung cancer were included for analysis. Odds ratio (OR, used to compare dichotomous variables) and weight mean difference (WMD, used to compare continuous variables) were calculated with 95% confidence intervals (CIs) based on intention-to-treat analysis.</p> <p><b>Results:</b> Eleven studies including 1314 patients were included for analysis. Our analysis showed that the operative time, blood loss amount, mean duration of chest tube, lymph nodes retrieved were similar between two approaches, the SITS pulmonary resection might be associated with shorter hospital stay (<i>p</i> = .008) and lower complication rate (<i>p</i> = .009) when compared with conventional multiport video-assisted thoracoscopic surgery approaches.</p> <p><b>Conclusions:</b> In selected patients SITS is safe, feasible and may be considered an alternative to multiport VATS.</p

Correlation between dimensions of the femoral neck and the acetabulum.

<p>AAVA: acetabular anteversion angle, AABA: acetabular abduction angle, ASD: acetabular suprainferior diameter.</p><p>FAVA: femoral anteversion angle, NSA: neck-shaft angle, FHD: diameter of the femoral head.</p><p>*<i>P</i><0.05.</p

Correlation between dimensions of the femoral neck and femoral sizes.

<p>FAVA: femoral anteversion angle, NSA: neck-shaft angle, FHD: diameter of the femoral head, MLD+20 and APD+20: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at a plane of 20 mm above the lesser trochanter, MLD and APD: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at the midpoint of the lesser trochanter, MLD−20 and APD−20: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at a plane of 20 mm below the lesser trochanter, IID: internal diameter of the isthmus, IED: external diameter of the isthmus, IP: distance from the midpoint of the lesser trochanter to the isthmus.</p><p>*<i>P</i><0.05.</p

Results of measurement of dimensions at different levels of the proximal femur and femoral indices.

<p>FAVA: femoral anteversion angle, NSA: neck-shaft angle, FHD: diameter of the femoral head, Offset: femoral offset, MLD+20 and APD+20: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at a plane of 20 mm above the lesser trochanter, MLD and APD: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at the midpoint of the lesser trochanter, MLD−20 and APD−20: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at a plane of 20 mm below the lesser trochanter, IID: internal diameter of the isthmus, IED: external diameter of the isthmus, IP: distance from the midpoint of the lesser trochanter to the isthmus. CFI: Canal flare index. MCFI: Metaphyseal canal flare index. DCFI: Distal canal flare index.</p><p>*There was significant difference between the male and the female (P<0.05).</p

Correlation between diameters at different levels of the proximal femur with age and height.

<p>MLD+20 and APD+20: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at a plane of 20 mm above the lesser trochanter, MLD and APD: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at the midpoint of the lesser trochanter, MLD−20 and APD−20: medial-lateral diameter and antero-posterior diameter of bone medullary cavity at a plane of 20 mm below the lesser trochanter, IID: internal diameter of the isthmus, IED: external diameter of the isthmus, IP: distance from the midpoint of the lesser trochanter to the isthmus. CFI: Canal flare index. MCFI: Metaphyseal canal flare index.</p><p>*<i>P</i><0.05.</p

Distribution of the CFI of the proximal femur.

<p>Distribution of the CFI of the proximal femur.</p

Results of measurement of the acetabula of healthy adults in South China.

<p>AAVA: acetabular anteversion angle, AABA: acetabular abduction angle, ASD: acetabular suprainferior diameter.</p><p>*There was significant difference between the male and the female (P<0.05).</p

Table_1_Role of N-Glycosylation in FcγRIIIa interaction with IgG.xlsx

Immunoglobulins G (IgG) and their Fc gamma receptors (FcγRs) play important roles in our immune system. The conserved N-glycan in the Fc region of IgG1 impacts interaction of IgG with FcγRs and the resulting effector functions, which has led to the design of antibody therapeutics with greatly improved antibody-dependent cell cytotoxicity (ADCC) activities. Studies have suggested that also N-glycosylation of the FcγRIII affects receptor interactions with IgG, but detailed studies of the interaction of IgG1 and FcγRIIIa with distinct N-glycans have been hindered by the natural heterogeneity in N-glycosylation. In this study, we employed comprehensive genetic engineering of the N-glycosylation capacities in mammalian cell lines to express IgG1 and FcγRIIIa with different N-glycan structures to more generally explore the role of N-glycosylation in IgG1:FcγRIIIa binding interactions. We included FcγRIIIa variants of both the 158F and 158V allotypes and investigated the key N-glycan features that affected binding affinity. Our study confirms that afucosylated IgG1 has the highest binding affinity to oligomannose FcγRIIIa, a glycan structure commonly found on Asn162 on FcγRIIIa expressed by NK cells but not monocytes or recombinantly expressed FcγRIIIa.</p

Characterization of Binding Epitopes of CA125 Monoclonal Antibodies

The most used cancer serum biomarker is the CA125 immunoassay for ovarian cancer that detects the mucin glycoprotein MUC16. Several monoclonal antibodies (mAbs) including OC125 and M11 are used in CA125 assays. However, despite considerable efforts, our knowledge of the molecular characteristics of the recognized epitopes and the role played by glycosylation has remained elusive. Here a comprehensive set of recombinant MUC16 tandem repeats (TRs) expressed in glycoengineered mammalian cells and <i>E. coli</i>, together with overlapping peptides, was used to probe antigen-binding epitopes. We present a complete analysis of N- and O-glycosylation sites of a MUC16 TR expressed in CHO cells and demonstrate that neither N- nor O-glycosylation appear to substantially influence binding of OC125 and M11 mAbs. A series of successive N- and C-terminal truncations of a MUC16 TR construct expressed in <i>E. coli</i> narrowed down the epitopes for OC125 and M11 to a segment containing parts of two consecutive SEA domains with a linker. Thus, a complete SEA domain is not required. These findings suggest that binding epitopes of mAbs OC125 and M11 are dependent on conformation but not on glycosylation. The availability of recombinant TR constructs with and without aberrant glycosylation now opens the way for vaccine studies

DataSheet_1_Role of N-Glycosylation in FcγRIIIa interaction with IgG.pdf

Immunoglobulins G (IgG) and their Fc gamma receptors (FcγRs) play important roles in our immune system. The conserved N-glycan in the Fc region of IgG1 impacts interaction of IgG with FcγRs and the resulting effector functions, which has led to the design of antibody therapeutics with greatly improved antibody-dependent cell cytotoxicity (ADCC) activities. Studies have suggested that also N-glycosylation of the FcγRIII affects receptor interactions with IgG, but detailed studies of the interaction of IgG1 and FcγRIIIa with distinct N-glycans have been hindered by the natural heterogeneity in N-glycosylation. In this study, we employed comprehensive genetic engineering of the N-glycosylation capacities in mammalian cell lines to express IgG1 and FcγRIIIa with different N-glycan structures to more generally explore the role of N-glycosylation in IgG1:FcγRIIIa binding interactions. We included FcγRIIIa variants of both the 158F and 158V allotypes and investigated the key N-glycan features that affected binding affinity. Our study confirms that afucosylated IgG1 has the highest binding affinity to oligomannose FcγRIIIa, a glycan structure commonly found on Asn162 on FcγRIIIa expressed by NK cells but not monocytes or recombinantly expressed FcγRIIIa.</p