Loading…

A Single Mutation Affects Both N-Acetylglucosaminyltransferase and Glucuronosyltransferase Activities in a Chinese Hamster Ovary Cell Mutant Defective in Heparan Sulfate Biosynthesis

Mutants of Chinese hamster ovary cells have been found that no longer produce heparan sulfate. Characterization of one of the mutants, pgsD-677, showed that it lacks both N-acetylglucosaminyl- and glucuronosyltransferase, enzymes required for the polymerization of heparan sulfate chains. pgsD-677 al...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1992-03, Vol.89 (6), p.2267-2271
Main Authors: Lidholt, Kerstin, Weinke, Julie L., Kiser, Cheryl S., Lugemwa, Fulgentius N., Bame, Karen J., Cheifetz, Sela, Massague, Joan, Lindahl, Ulf, Esko, Jeffrey D.
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mutants of Chinese hamster ovary cells have been found that no longer produce heparan sulfate. Characterization of one of the mutants, pgsD-677, showed that it lacks both N-acetylglucosaminyl- and glucuronosyltransferase, enzymes required for the polymerization of heparan sulfate chains. pgsD-677 also accumulates 3- to 4-fold more chondroitin sulfate than the wild type. Cell hybrids derived from pgsD-677 and wild type regained both transferase activities and the capacity to synthesize heparan sulfate. Two segregants from one of the hybrids reexpressed the dual enzyme deficiency, the lack of heparan sulfate synthesis, and the enhanced accumulation of chondroitin sulfate, suggesting that all of the traits were genetically linked. These findings indicate that the pgsD locus may represent a gene involved in the coordinate control of glycosaminoglycan formation.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.89.6.2267