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

FEBS Letters
T BrattB Akerström

Abstract

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.

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Citations

May 23, 2001·Archives of Biochemistry and Biophysics·C FalkenbergB Akerström
Nov 4, 2000·Biochimica Et Biophysica Acta·B AkerströmA Lindqvist
Jan 23, 1999·European Journal of Biochemistry·N Martin-VandeletM Diarra-Mehrpour
Jul 23, 1996·Proceedings of the National Academy of Sciences of the United States of America·M W Nachtigal, H A Ingraham
Jul 22, 1998·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·T BerggårdJ J Enghild
May 21, 2004·The Journal of Biological Chemistry·Lisheng ZhuoKoji Kimata
May 16, 2006·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Sarah L Griffiths, David J Grainger
Jul 9, 2020·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·Megan S LordJohn M Whitelock
Oct 9, 2004·The Journal of Biological Chemistry·Anton J M RoebroekJohn W M Creemers

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