A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis Journal Article

   

Authors:	Lidholt, K.; Weinke, J. L.; Kiser, C. S.; Lugemwa, F. N.; Bame, K. J.; Cheifetz, S.; Massagué, J.; Lindahl, U.; Esko, J. D.
Article Title:	A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis
Abstract:	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. (.
Keywords:	gene mutation; mutation; nonhuman; animal cell; phenotype; animal; chromatography, high pressure liquid; glucuronosyltransferase; autoradiography; heparan sulfate; heparitin sulfate; cell fusion; enzyme deficiency; cho cell; cho cells; cricetinae; cricetulus griseus; genetic regulation; proteoglycans; chondroitin sulfate; sulfates; glycosaminoglycan; glycosyltransferases; priority journal; article; glycosaminoglycans; sulfur radioisotopes; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; n acetylglucosaminyltransferase; hamsters; glucosyltransferases; proteoglycan synthesis; replica plating
Journal Title:	Proceedings of the National Academy of Sciences of the United States of America
Volume:	89
Issue:	6
ISSN:	0027-8424
Publisher:	National Academy of Sciences
Date Published:	1992-03-15
Start Page:	2267
End Page:	2271
Language:	English
DOI:	10.1073/pnas.89.6.2267
PUBMED:	1532254
PROVIDER:	scopus
PMCID:	PMC48638
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026577602&doi=10.1073%2fpnas.89.6.2267&partnerID=40&md5=6e11ed10e78b23a601b6cceffcda6528
Notes:	Source: Scopus

https://synapse.mskcc.org/synapse/works/has_related_data_chk/150002