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Department of Clinical Chemistry and Central Laboratory, Philipps University, Marburg, Germany.
a Address for correspondence. Abteilung für Klinische Chemie und Zentrallaboratorium, Klinikum der Philipps-Universität, Baldingerstraße, 35033 Marburg, Germany. Fax (+49) 6421 28 5594; e-mail kropf{at}mailer.uni-marburg.de and www.med.uni-marburg.de/labmed.
Development of a new, sensitive immunoassay for measuring transforming
growth factor beta 1 (TGF-ß1) is described and compared with four
commercially available TGF-ß1 immunoassays. Preanalytical conditions
were evaluated. The nonlinearity found in serum or plasma is due to
masking of TGF-ß1 by binding proteins in blood. Mixing TGF-ß1 with
latency-associated peptide or
2-macroglobulin at
physiological concentrations suppressed most of the TGF-ß1 signal.
Plasma fibronectin showed no effect, even at concentrations exceeding
its physiological range. Equilibrium concentrations computed from a
model system confirmed the experimental results. Dilutional
nonlinearity could be markedly reduced by an appropriately designed
activation procedure that minimized the effects of reassociation
between TGF-ß1 and its binding partners during restoration of a
neutral pH. Plasma should be used for measuring TGF-ß1 in blood.
Because serum TGF-ß1 is highly significantly correlated with the
platelet count, probably most of the TGF-ß1 is released by platelet
degranulation.
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