Complement component analysis in angiodema. Diagnostic value

1975 ◽  
Vol 111 (9) ◽  
pp. 1140-1142 ◽  
Author(s):  
G. W. Brasher
2017 ◽  
Vol 35 (4_suppl) ◽  
pp. 19-19 ◽  
Author(s):  
Virendra Joshi ◽  
Alok Shah ◽  
Ian Brown ◽  
Clay Winterford ◽  
Michelle Hill

19 Background: Esophageal adenocarcinoma (EAC) continues an upward trend. Mortality rate and treatment costs for EAC are very high overall and significantly increase with disease stage. Diagnosis at early stage (T1) compared to advanced stage (T3) improves 5 year survival from 20% to 80-90%. Endoscopic surveillance has been ineffective in reducing EAC. Therefore the need for better diagnostic tools for early detection.Previously we reported validation of a list of serum glycoprotein biomarker candidates for EAC in an Australian cohort (Shah et al. 2015 Mol Cell Proteomics. 14:3023-39.). Here we further evaluate the serum and tissue expression of top candidate C9 in an independent cohort from the USA. Methods: Serum samples (n=38) and FFPE tissue sections (n=34) were collected from participants with IRB approved protocol, from the Ochsner Clinic undergoing endoscopic surveillance for Barrett’s and esophageal cancer. Serum glycoprotein candidates were measured using lectin magnetic bead array-coupled multiple reaction monitoring assay (Shah et al. 2015 Mol Cell Proteomics. 14:3023-39.). Immunohistochemistry was optimised for complement component C9 antibody. Initial evaluation of 2 different antibodies gave similar results, thereafter, a polyclonal antibody from Sigma Aldrich was used. Staining was assessed by a gastrointestinal pathologist. Results: Specific glycosylated forms of 3 candidate serum biomarkers were confirmed to be significantly different between EAC and benign groups (p<0.05, Kruskal-Wallis). The diagnostic value for the 3 individual markers, complement component C9, gelsolin and alpha-1-antichymotrypsin (Serpin A3) was 0.71 to 0.82 area under the receiver operating curve (AUROC). A multivariate panel consisting of 8 glycoprotein biomarkers achieved AUROC of 0.96, indicative of high diagnostic value. Immunohistochemistry of tissues detected high levels of C9 in BE and EAC compared to normal squamous epithelium. Infiltrated lymphocytes showed variable staining. Conclusions: We propose a novel candidate biomarker complement component C9 which could add to current endoscopic surveillance strategy for early detection of adenocarcinoma.


1970 ◽  
Vol 131 (4) ◽  
pp. 629-641 ◽  
Author(s):  
R. A. Thompson ◽  
P. J. Lachmann

This paper describes the characteristics of the indicator factor (I) which takes part in reactive hemolysis and its identification as the seventh component of complement. I was shown to be a beta globulin with a sediment coefficient of 5.7S and a molecular weight of about 140,000. Experiments on the depletion of I activity with anti-I antiserum or with activated R euglobulin showed that I was a late acting complement component necessary for the lysis of cells after the EAC142 stage. Complement component analysis of purified I fractions excluded all known components except C7. The physicochemical characteristics of I are compatible with published data on C7. The method of quantitation described represents a convenient method of testing for C7.


Author(s):  
Gerald Fine ◽  
Azorides R. Morales

For years the separation of carcinoma and sarcoma and the subclassification of sarcomas has been based on the appearance of the tumor cells and their microscopic growth pattern and information derived from certain histochemical and special stains. Although this method of study has produced good agreement among pathologists in the separation of carcinoma from sarcoma, it has given less uniform results in the subclassification of sarcomas. There remain examples of neoplasms of different histogenesis, the classification of which is questionable because of similar cytologic and growth patterns at the light microscopic level; i.e. amelanotic melanoma versus carcinoma and occasionally sarcoma, sarcomas with an epithelial pattern of growth simulating carcinoma, histologically similar mesenchymal tumors of different histogenesis (histiocytoma versus rhabdomyosarcoma, lytic osteogenic sarcoma versus rhabdomyosarcoma), and myxomatous mesenchymal tumors of diverse histogenesis (myxoid rhabdo and liposarcomas, cardiac myxoma, myxoid neurofibroma, etc.)


1957 ◽  
Vol 33 (2) ◽  
pp. 163-171 ◽  
Author(s):  
Perry J. Culver ◽  
William V. McDermott ◽  
Chester M. Jones

1965 ◽  
Vol 48 (1) ◽  
pp. 12-17 ◽  
Author(s):  
Howard E. Ticktin ◽  
Nelson P. Trujillo ◽  
Phyllis F. Evans ◽  
Joseph H. Roe

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