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DNA-mediated transformation of N-acetylglucosaminyltransferase I activity into an enzyme deficient cell line.

Abstract：

:N-acetylglucosaminyltransferase I (GlcNAc-TI) catalyzes the first reaction in the conversion of ASN-linked cell surface oligosaccharides from a mannose-terminating structure to more complex carbohydrate structures. The mutant Chinese hamster ovary (CHO) cell line, Lec1, is deficient in this enzyme and, therefore, shows increased sensitivity to the lectin, Concanavalin A, which binds to the mannose-terminating oligosaccharides that accumulate on Lec1 cell surface glycoproteins. Spontaneous revertants of the Lec1 phenotype have never been observed. We report here the isolation of stable revertants of Lec1 cells to the parental CHO cell lectin-resistance phenotype after DNA-mediated transformation with human DNA. Both primary and secondary transformants express varying levels of GlcNAc-TI enzyme activity which was stable even when the cells were cultured in nonselective conditions. Human alu repeat DNA sequences are present in the primary transformants, but these sequences could not be detected in the secondary transformants.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ripka J,Pierce M,Fregien N

doi

10.1016/0006-291x(89)90029-6

subject

Has Abstract

pub_date

1989-03-15 00:00:00

pages

554-60

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)90029-6

journal_volume

159

pub_type

杂志文章

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