Functional integrins from normal and glycosylation-deficient baby hamster kidney cells. Terminal processing of asparagine-linked oligosaccharides is not correlated with fibronectin-binding activity.

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Article

Functional integrins from normal and glycosylation-deficient baby hamster kidney cells. Terminal processing of asparagine-linked oligosaccharides is not correlated with fibronectin-binding activity.

The Journal of biological chemistry - 25 Dec 1992

Koyama T, Hughes R C

Abstract excerpt

We have examined the properties of the alpha 5 beta 1 integrin of baby hamster kidney (BHK) cells, a ricin-resistant variant Ric14 lacking N-acetylglucosaminyl transferase I, and hence unable to complete assembly of hybrid- or complex-type N-glycans, and BHK cells treated with 1-deoxymannojirimycin (dMM), an inhibitor of Golgi mannosidases involved in the initial processing of N-glycan precursors. Comparable...

Topics

1-Deoxynojirimycin
Animals
Asparagine
Cell Line
Chromatography, Affinity
Cricetinae
Fibronectins
Genetic Variation
Glycosylation
Humans
Integrins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Iodine Radioisotopes

Kidney

Macromolecular Substances

Mannosidases

N-Acetylglucosaminyltransferases

Oligosaccharides

Protein Processing, Post-Translational

Source

Open in PubMed

Identifiers

PMID: 1464606

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1464606-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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