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Processing and secretion of rat α 1 ‐microglobulin‐bikunin expressed in eukaryotic cell lines
Author(s) -
Bratt Tomas,
Cedervall Tommy,
Åkerström Bo
Publication year - 1994
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(94)01087-0
Subject(s) - secretion , microbiology and biotechnology , beta 2 microglobulin , cell , cell culture , chemistry , biology , biochemistry , genetics , immunology
The precursor protein α 1 ‐microglobulin‐bikunin was cleaved to the same degree whether expressed in CHO cells or in mutated CHO cells, RPE.40 cells, suggested to lack a functional form of the intracellular protease furin. Thus, α 1 ‐microglobulin‐bikunin probably is not cleaved in vivo by furin. However, simultaneous overexpression of the precursor and furin in COS, CHO and RPE.40 cells increased the cleavage, suggesting that compartmentalisation and concentrations of protease and precursor are important for the cleavage, besides the in vitro specificity. Expression of α 1 ‐microglobulin and bikunin alone gave different protein patterns on SDS‐PAGE as compared to expression of the precursor and subsequent cleavage, suggesting that the precursor protein is important for the post‐translational handling of α 1 ‐microglobulin and bikunin.