Synthesis of Immunoglobulins and 15 Other Proteins by Diseased Human Kidneys

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Abstract
In an effort to determine the synthetic capacity of human kidneys for serum proteins, pieces of both kidneys removed at operation prior to transplantation were placed in organ culture. Incubation with 14C labeled amino acids and subsequent radioimmunoelectrophoresis [RI] with antisera to all 5 classes of immunoglobulins [Ig] showed synthesis of IgG by all 5 pairs of kidneys of IgA and IgE by 4 and of IgM by 2. None synthesized IgD. RI with specific antisera to 15 non-Ig proteins revealed synthesis of lactoferrin and uromucoid. Several other serum proteins, such as .alpha.1 and antitrypsin and .alpha.2 macroglobulin, known for their binding properties, showed apparent synthesis. No evidence for secretory component synthesis was seen despite positive immunofluorescent localization in the tubular cells. Zn .alpha.2 and .beta.2GP I [.beta.2 glycoprotein I] showed positive immunofluorescence but negative synthesis. These latter proteins may not be synthesized by the tubular cells, but may be actively excreted or reabsorbed by them.

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