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Processing of mutated proinsulin with tetrabasic cleavage sites to bioactive insulin in the non‐endocrine cell line, COS‐7

Processing of mutated proinsulin with tetrabasic cleavage sites to bioactive insulin in the... The amino acid sequence, Arg−4‐X−3‐Lys/Arg−2‐Arg−1 ↓ X+1, is thought to be a consensus processing site for a constitutive secretory pathway in non‐endocrine cells. We created a mutant proinsulin DNA with a peptide structure of B chain‐Arg‐Arg‐Lys‐Arg‐C peptide‐Arg‐Arg‐Lys‐Arg‐A chain, which compares to the native proinsulin structure of B chain‐Arg‐Arg‐C peptide‐Lys‐Arg‐A chain. When the mutant insulin was expressed in a monkey kidney‐derived cell line, COS‐7, approximately 60% of the total immunoreactive insulin appeared as mature insulin in the culture medium. This conversion to the mature form was strikingly facilitated by co‐expressing the mutant proinsulin with furin, a homologue of the yeast endoprotease, Kex2. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Febs Letters Wiley

Processing of mutated proinsulin with tetrabasic cleavage sites to bioactive insulin in the non‐endocrine cell line, COS‐7

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References (28)

Publisher
Wiley
Copyright
© 2015 Federation of European Biochemical Societies
eISSN
1873-3468
DOI
10.1016/0014-5793(92)81366-T
Publisher site
See Article on Publisher Site

Abstract

The amino acid sequence, Arg−4‐X−3‐Lys/Arg−2‐Arg−1 ↓ X+1, is thought to be a consensus processing site for a constitutive secretory pathway in non‐endocrine cells. We created a mutant proinsulin DNA with a peptide structure of B chain‐Arg‐Arg‐Lys‐Arg‐C peptide‐Arg‐Arg‐Lys‐Arg‐A chain, which compares to the native proinsulin structure of B chain‐Arg‐Arg‐C peptide‐Lys‐Arg‐A chain. When the mutant insulin was expressed in a monkey kidney‐derived cell line, COS‐7, approximately 60% of the total immunoreactive insulin appeared as mature insulin in the culture medium. This conversion to the mature form was strikingly facilitated by co‐expressing the mutant proinsulin with furin, a homologue of the yeast endoprotease, Kex2.

Journal

Febs LettersWiley

Published: Oct 12, 1992

Keywords: ; ; ; ; ;

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