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Xenopus oocytes can synthesise but do not secrete the Z variant of human α 1 ‐antitrypsin
Author(s) -
Foreman R.C.,
Judah J.D.,
Colman A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80211-2
Subject(s) - xenopus , tunicamycin , immunoprecipitation , secretion , biology , glycoprotein , secretory protein , messenger rna , microbiology and biotechnology , intracellular , gene , biochemistry , unfolded protein response
Human liver mRNA was prepared from a patient homozygous for α 1 ‐antitrypsin deficiency (PiZZ) and from a normal subject (PiMM). Both liver RNAs were microinjected into Xenopus oocytes and α 1 ‐antitrypsin identified by immunoprecipitation. The normal M variant of α 1 ‐antitrypsin is synthesised and secreted by Xenopus oocytes, the abnormal Z protein is not secreted and an intracellular form accumulates in the oocytes. In the presence of tunicamycin an unglycosylated form of M α 1 ‐antitrypsin appears in the incubation medium but no corresponding unglycosylated version of the Z protein is secreted.