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Scientific article
English

Slow cleavage at the proinsulin B-chain/connecting peptide junction associated with low levels of endoprotease PC1/3 in transformed beta cells

Published inThe Journal of biological chemistry, vol. 268, no. 22, p. 16098-16100
Publication date1993
Abstract

Conversion of rat proinsulins I and II was slower in transformed INS cells than in primary (islet) beta cells, with accumulation of des-64,65 but no detectable des-31,32-split proinsulin, indicating slow cleavage at the B-chain/connecting peptide (C-peptide) junction. Western blot analysis showed lower levels of the endoprotease PC1/3 in INS cells than in beta cells, as well as a 4-fold reduction in the ratio of PC1/3 to PC2, thus supporting the hypothesis that PC1/3 is the endoprotease responsible for cleavage at the B-chain/C-peptide junction.

Keywords
  • Animals
  • Aspartic Acid Endopeptidases/ metabolism
  • C-Peptide/genetics/ metabolism
  • Cell Line
  • Islets of Langerhans/cytology/metabolism
  • Kinetics
  • Male
  • Proprotein Convertases
  • Rats
  • Rats, Sprague-Dawley
Citation (ISO format)
NEERMAN ARBEZ, Marguerite, SIZONENKO, S. V., HALBAN, Philippe A. Slow cleavage at the proinsulin B-chain/connecting peptide junction associated with low levels of endoprotease PC1/3 in transformed beta cells. In: The Journal of biological chemistry, 1993, vol. 268, n° 22, p. 16098–16100.
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Identifiers
ISSN of the journal0021-9258
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