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- W2033586918 abstract "The rate of synthesis of α1-antitrypsin has been studied in organ cultures of fetal human liver. By de novo synthesis, α1-antitrypsin of the same electrophoretic mobility and molecular size as plasma α1-antitrypsin was produced. Synthetic rate was comparable to in vivo conditions and was suppressed by cycloheximide, colchicine and neuraminidase. By increasing α1-antitypsin levels in culture medium, suppression of α1-antitrypsin release from the intra-to the extracellular site was achieved, i.e., synthesis does not proceed autonomously. This suppression was preceded by a temporary enhancement of synthesis. Both effects were found to be independent of degree of sialylation of added α1-antitrypsin. In contrast to α1-antitrypsinreleased in tissue culture, the intracellular protein, as analyzed by crossed immunoelectrophoresis of Triton X-100 extracts from fetal liver, was found to occur partly as slowly moving peaks. Whether these peaks represent proforms or incompletely glycosylated precursors of export α1-antitrypsin or complexes with proteases remains unsettled. A variety of other plasma proteins are released in organ cultures making the system suitable for study of factors regulating plasma protein synthesis." @default.
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- W2033586918 date "1978-09-01" @default.
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- W2033586918 title "Organ cultures of human fetal hepatocytes in the study of extra- and intracellular α1-antitrypsin" @default.
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- W2033586918 doi "https://doi.org/10.1016/0304-4165(78)90379-3" @default.
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