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Cited by 270

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin.

Open access
Sato, S, Hughes, R.C.·1992·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)50525-7
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Abstract

The carbohydrate binding specificity of Mr = 30,000 lectin (CBP30) from baby hamster kidney (BHK) cells has been studied by inhibition of binding of the radiolabeled lectin to asialofetuin-Sepharose using model oligosaccharides and glycopeptides. CBP30 binds type I or II Gal beta(1----3(4))GlcNAc chains but not Gal(beta 1----3)GalNAc. The inhibitory potency of straight chain polylactosamine structures or complex-type branched glycans is increased in proportion to the number of Gal(beta 1----3(4)) units present. Fucosylation or sialylation of terminal galactose residues or further substitution by (alpha 1----3)-linked galactose or N-acetylgalactosamine does not affect binding whereas substitution of the penultimate N-acetylglucosamine residue drastically reduces binding. Thus, blood group A, H type I or H type II structures, shows high affinity whereas Lex, Lea, and Leb structures bind poorly. CBP30 binds to murine Engelbreth-Holm-Swarm (EHS) tumor laminin and human amniotic fluid fibronectin but not human plasma fibronectin. Binding involves polylactosamine glycans as well as tri- and tetraantennary complex-type glycans present in EHS laminin and amniotic fluid fibronectin but absent in plasma fibronectin. Proteolytic fragments of EHS laminin (E1X/Nd, P1, E8, and E3) bind CBP30, but only fragment E8 supports attachment and spreading of BHK cells. BHK cell adhesion to EHS laminin or fragment E8 was not disturbed by CBP30-specific antibodies, but at relatively high concentrations (45 micrograms/ml) CBP30 inhibited spreading and partially attachment of cells on laminin.

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Metadata

Authors
Sato, S., & Hughes, R. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-04
Volume
267
Issue
10
Pages
6983-6990
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)50525-7
OpenAlex
W1520800891
Cited by
270
References
32
FWCI
3.94
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin. https://app.cochat.ai/papers/10.1016/s0021-9258(19)50525-7
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Sato, S., & Hughes, R. C. (1992). Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)50525-7

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.