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PMID: 2891353 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Glycolipid anchors are attached to Thy-1 glycoprotein rapidly after translation.

The Biochemical journal ·Vol. 246 ·No. 3 ·1987-09-15 ·Pages 605-10

Conzelmann A, Spiazzi A, Bron C

Abstract

The attachment of glycolipid anchors to the Thy-1 glycoprotein during biosynthesis was followed by the change of detergent-binding properties of biosynthetically labelled Thy-1 precursors upon phospholipase C treatment in the murine thymoma lines BW5147 and S1A. In S1A, 80% of the Thy-1 molecules were phospholipase-C-sensitive after a 2 min pulse with [35S]methionine, indicating that these molecules were already anchored via a glycolipid tail. In BW5147, 47% of the Thy-1 molecules had phospholipase-C-sensitive anchors attached after a 1.5 min labelling and, with longer pulses, this percentage rose to 76%. Tunicamycin did not block the addition of glycolipid anchors, and glycolipid attachment also occurred at 21 degrees C. The findings suggest that the attachment of glycolipid anchors occurs in the rough endoplasmic reticulum.

MeSH Terms
Antigens, Surface/analysis Cell Line Chemical Precipitation Electrophoresis, Polyacrylamide Gel Glycolipids/pharmacokinetics Protein Biosynthesis Thy-1 Antigens Tunicamycin/pharmacology Type C Phospholipases
Chemicals
Antigens, Surface Glycolipids Thy-1 Antigens Tunicamycin Type C Phospholipases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Conzelmann A
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
Spiazzi A
Bron C
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2460605
Published
1987-09-15
Pages
605-10
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1148323
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2460605 PMC Full Text View journal details
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