The measurement of circulating prealbumin has been shown to be clinically useful in the assessment of nutritional status, both as an initial screen and in the monitoring of nutritional recovery. We describe a fully automated, noncompetitive, homogenous, light-scattering immunoassay that has been developed for this analyte on a Dimension® (Dade) analyzer. A sheep anti-prealbumin IgG fraction was covalently coupled to 40-nm chloromethyl styrene particles and, after the addition of sample, polyethylene glycol-assisted immunoagglutination was monitored by turbidimetry. The prealbumin working assay range was 8–550 mg/L at a sample volume of 2 μL and a reaction time of 6.5 min. When data were analyzed using ANOVA, total and within-run assay imprecision values (CVs) were 1–5%, and calibration and reagent stabilities were in excess of 40 days. Mean analytical recoveries were 102% ± 4% (SD), and there was no lack of parallelism. Hemolysis, lipemia, and bilirubin did not interfere. Both plasma anticoagulated with heparin or EDTA and serum from plain or serum-separation tubes were acceptable as sample matrices. Comparison with the Beckman Array® method gave a Passing and Bablok regression of: Dimension analyzer = 1.01Beckman + 7.1 (n = 103), using a common calibrator. We conclude that the prealbumin method is appropriate for clinical use according to the analytical criteria used in this study.

The neural cell adhesion molecule (NCAM) is a tumourrelated antigen found on the surface of small-cell lung cancer (SCLC). NCAM exists in several molecular forms, including a soluble isoform. We have measured serum levels of NCAM using an enzyme immunoassay with 2 anltibodies, NCC-LU-246 and NCC-LU-243, that react with different epitopes on the NCAM molecule. NCAM activity from 83 patients with active SCLC, either pre-treatment, progressing oir in relapse was significantly higher than in 70 patients on follow-up. Overall, 40% of patients with active SCLC and 7% patients on follow-up had serum levels of NCAM > 2SD above controls; 61% of patients with relapsed SCLC had elevated levels of NCAM. Isre-treatment NCAM levels were significantly higher in 35 patients with "extensive" disease than in I9 patients with "limited" disease. Serum NCAM activity was also significantly higher in patients with tumour infiltration of the bone marrow. This difference could not be explained solely by the presence of "extensive" disease. Serum NSE levels in these patients were correlated with NCAM activity. The presence of raised serum NCAM in active disease and in patients in relapse suggests that this antigen could be used as a target for antibody-directed therapy of micrometastases.o 1994 Wiley-Liss, Inc.

Summary Spheroids of a small-cell lung cancer (SCLC) cell line POC were used to evaluate the uptake and penetration of two antibodies recognising different SCLC antigens. Spheroids approximately 300-400 gm in diameter were incubated with 1 jig ml-"25I-labelled NY.3DI 1, an antibody which reacts with the cluster I group antigen (neural cell adhesion molecule; NCAM) and ['25I]SWAI 1, which binds to the cluster w4 antigen. The rate of uptake of both antibodies was similar; an initially rapid phase was seen during the first 8 h and maximum uptake occurred by 24 h. This increased to about 100 txm after 4 h incubation with I or 100 fig ml-' SWAI 1. The results with I lg mlh' NY.3D1 were similar, but in the presence of 100 jg ml-' NY.3DI I penetration into the spheroid was deep and diffuse. These results demonstrate a major concentration-dependent difference in the uptake and penetration of cluster I and cluster w4 antibodies in this spheroid model and they have implications for the selection of antibodies for targeted therapy of SCLC.

SUMMARY. Neural cell adhesion molecules (NCAMs) are found predominantly in neural, muscle and endocrine cells. Recent interest has focused on their potential role in tumorigenesis. We have analysed the expression and secretion of NCAM in a series of 48 human pituitary adenomas. Immunocytochemical analysis of 19 adenomas demonstrated NCAM expression in all tumours with, in each case, diffuse cytoplasmic staining being found with variable membrane accentuation. There were no apparent differences in the expression of immunoreactivity seen on sections between individual tumours. Cell culture media from 43 dispersed human pituitary tumours were analysed by immunoassay for the secretion of soluble NCAM and all the pituitary hormones. In contrast to the immunocytochemical studies, soluble NCAM was released from only 27% of human pituitary tumours, but this was not related to tumour type nor was the amount of soluble NCAM released correlated with the amount of pituitary hormone secreted by each adenoma. NCAM expression is common to all human pituitary adenoma types and the observed differences in release of soluble NCAM between individual tumours may reflect different molecular mechanisms, altering adhesive interactions between normal and adenomatous tissue.

Background: Available assays for cardiac troponin I (cTnI) yield numerically different results. The aim of this study was to compare patient values obtained from four cTnI immunoassays. Methods: We studied the Stratus® II assay, the Opus® II assay, the Access® assay, and a research-only cTnI heterogeneous immunoassay that uses the Dade Behring aca® plus immunoassay system equipped with two new noncommercial monoclonal antibodies. Because the aca plus cTnI assay is for research only, we first evaluated and analytically validated it for serum and citrated plasma. Initially, each method was calibrated using the method-specific calibrator supplied by each manufacturer; however, the aca plus cTnI assay was calibrated using patient serum pools containing cTnI and selected on the basis of increased creatine kinase MB isoenzyme and with values assigned by use of the Stratus cTnI assay. For method comparisons, individual patient sample cTnI values were determined and compared with the Stratus II assay. Results: Passing and Bablock regression analysis yielded slopes of 1.44 (r = 0.96; n = 72) for the Opus II vs Stratus II assays; 0.07 (r = 0.91; n = 72) for the Access vs Stratus II assays; and 0.90 (r = 0.91, n = 72) for the aca plus vs Stratus II assays. The recalibration of each method with a Stratus II-assigned serum pool improved, but did not entirely eliminate, the slope differences between the different assays (range, 1.00–1.16). The observed scatter in the correlation curves remained. Conclusion: There is a need to further explore the specificities of these assays with respect to the different circulating forms of cTnI.