Glycosylation influences intracellular transit time and secretion rate of human prorenin in transfected cells.


Journal Article

The mouse pituitary tumour (AtT-20) cell transfected with the human renin gene has been shown to be a useful model system to study human renin biosynthesis. To investigate the influence of glycosylation on secretion of human renin from these cells, we performed pulse labelling experiments on transfected cells in the presence or absence of tunicamycin, a potent inhibitor of n-linked glycosylation. Intracellular and secreted renins were characterized by immunoprecipitation, sodium dodecyl sulphate (SDS) gel electrophoresis and fluorography. Our data showed that blockade of n-linked glycosylation reduced the intracellular transit time and increased the rate of prorenin secretion from transfected cells. We conclude that the carbohydrate moiety influences the kinetics of human renin secretion. This result provides one possible explanation for the observation that the secretion of glycosylated human renin is considerably slower than that of the unglycosylated mouse renin-2.

Full Text

Duke Authors

Cited Authors

  • Paul, M; Nakamura, N; Pratt, RE; Dzau, VJ

Published Date

  • December 1988

Published In

Volume / Issue

  • 6 / 4

Start / End Page

  • S487 - S489

PubMed ID

  • 3071590

Pubmed Central ID

  • 3071590

International Standard Serial Number (ISSN)

  • 0952-1178

Digital Object Identifier (DOI)

  • 10.1097/00004872-198812040-00154


  • eng

Conference Location

  • England