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PMID: 293711 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Processing in vitro of placental peptide hormones by smooth microsomes.

Bielinska M, Rogers G, Rucinsky T, Boime I

Abstract

Rough and smooth microsomes were prepared from ascites tumor cells, rat liver, and bovine adrenal cortex. Proteolytic removal of the signal peptide in pre-placental lactogen and asparagine-linked glycosylation of the alpha subunit of chorionic gonadotropin by these fractions were examined in mRNA-dependent lysates from ascites cells. Both processing steps were performed by smooth microsomes, which was unexpected because it has been presumed that only rough microsomes contain components for ribosomal binding. Thus smooth microsomes are apparently capable of interacting with polysomes bearing secretory nascent chains, and cleavage and asparagine-linked glycosylation activities are present in both rough and smooth endoplasmic reticulum.

MeSH Terms
Adrenal Cortex/ultrastructure Animals Ascites/pathology Cattle Chorionic Gonadotropin/metabolism Glycoproteins/metabolism Hexosyltransferases/metabolism Membrane Proteins/metabolism Microsomes/metabolism Microsomes, Liver/metabolism Molecular Weight Neoplasms, Experimental/ultrastructure Placental Lactogen/metabolism Protein Precursors/metabolism Rats
Chemicals
Chorionic Gonadotropin Glycoproteins Membrane Proteins Protein Precursors Placental Lactogen Hexosyltransferases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bielinska M
Rogers G
Rucinsky T
Boime I
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21 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1979-12-00
Pages
6152-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC411821
Subset
IM
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