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Cell-free synthesis and co-translational processing of the human asialoglycoprotein receptor.

Authors
  • Breitfeld, P P
  • Schwartz, A L
Type
Published Article
Journal
European journal of biochemistry / FEBS
Publication Date
Jul 15, 1985
Volume
150
Issue
2
Pages
409–414
Identifiers
PMID: 4018091
Source
Medline
License
Unknown

Abstract

The human asialoglycoprotein receptor is a 46-kDa membrane glycoprotein. It is initially synthesized as a 40-kDa precursor species possessing two N-linked high-mannose oligosaccharides which is subsequently converted to the 46-kDa mature product upon modification of its oligosaccharides of the complex form [Schwartz, A. L. & Rup, D. (1983) J. Biol. Chem. 258, 11 249-11 255]. To investigate further the biosynthesis of the human asialoglycoprotein receptor, we have utilized a cell-free wheat germ translation system supplemented with dog pancreatic microsomal membranes and programmed with HepG2 and human liver RNA. The primary translation product of the human receptor is a single 34-kDa species and this species is expressed throughout human fetal and adult development. The primary translation product possesses no cleavable signal peptide and is cotranslationally glycosylated to form the 40-kDa precursor species. In addition, the human asialoglycoprotein receptor is co-translationally inserted into microsomal membranes such that a 4-kDa cytoplasmic tail is susceptible to trypsin digestion.

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