Processing and secretion of rat alpha 1-microglobulin-bikunin expressed in eukaryotic cell lines

Research output: Contribution to journalArticle


The precursor protein alpha 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, alpha 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 alpha 1-microglobulin and bikunin alone gave different protein patterns of 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 alpha 1-microglobulin and bikunin.


External organisations
  • Lund University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Immunology in the medical area


  • Alpha-Globulins/chemistry, Animals, Base Sequence, CHO Cells, Cricetinae, Furin, Gene Expression, Glycoproteins/chemistry, Membrane Glycoproteins, Molecular Sequence Data, Molecular Weight, Protease Inhibitors/metabolism, Protein Precursors/genetics, Protein Processing, Post-Translational/physiology, Rats, Subtilisins/genetics, Transfection, Trypsin Inhibitor, Kunitz Soybean
Original languageEnglish
Pages (from-to)57-61
JournalFEBS Letters
Issue number1
Publication statusPublished - 1994 Oct 31
Publication categoryResearch