Neoglycoenzymes: A versatile tool for lectin detection in solid-phase assays and glycohistochemistry

Gabius, Sigrun; Hellmann, Klaus P.; Hellmann, Thea; Brinck, Ulrich; Gabius, H.‐J.

doi:10.1016/0003-2697(89)90621-0

Cited by 52 publications

(13 citation statements)

References 27 publications

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“…The use of neoglycoenzymes (see below) in similar applications can increase the detection sensitivity even further. Changes occurring during malignancy have been probed and documented by such methods (Gabius et al, 1989).…”

Section: Cytochemical Markersmentioning

confidence: 99%

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Neoglycoconjugates

Lee¹,

Lee²

1996

Glycosciences

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Section: Cytochemical Markersmentioning

confidence: 99%

“…A immobilized on plastic microtiter plates. Lactose-modified pgalactosidase was effective in histochemical detection of galactoside-specific lectins (Gabius et al, 1989).…”

Section: Neoglycoenzymesmentioning

confidence: 99%

Neoglycoconjugates

Lee¹,

Lee²

1996

Glycosciences

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“…Sulfated polysaccharides were biotinylated after mild cyanogen bromide treatment and aminoalkylation, as described [9,15]. Glycosylation of fi-galactosidase from E.coli (Boehringer, Mannheim, FRG), to obtain a panel of neoglycoenzymes, was performed under activity-preserving conditions by carbodiimide-mediated coupling of p-aminophenyl glycosides with a sugar incorporation of 25 _+ 5 moieties per enzyme subunit, as described recently [16].…”

Section: Initiation and Maintenance Of Culturesmentioning

confidence: 99%

Sugar receptors of the stromal cell layer in human long-term bone marrow cultures: Their presence, modulatory responses to changes in the microenvironment and potential role in cellular adhesion

Gabius

1990

Blut

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Intimate cellular contacts and coordinated supply of regulatory factors are required to maintain the still inexplicable dynamic equilibrium of hemopoiesis. To infer the potential participation of protein-carbohydrate interaction in this complex process, human long-term bone marrow cultures were initiated from eleven donors, and the adherent cell layer was characterized enzyme- and immunohistochemically. Utilizing an array of carrier-immobilized carbohydrate ligands and sulfated polysaccharides as probes, specific binding of various constituents of the carbohydrate chains of cellular glycoconjugates to the stromal cells was unmistakably disclosed. Biochemical analysis, employing glycocytologically effective ligands in affinity chromatography, corroborated this result. The extent of binding was markedly lower in the two samples, derived from leukemia patients. Pronounced adaptive responses for this characteristic followed changes in the culture microenvironment that are known to influence qualitative and quantitative aspects of hemopoiesis in vitro, namely omission of hydrocortisone and horse serum or addition of cytokines. Similarly, such adaptive modulation occurred on the level of accessible cell surface receptors, monitored by neoglycoenzymes. These binding sites can be involved in mediation of cellular interactions, as revealed in a model system by the interference of N-acetyl-D-galactosamine in cell adhesion. Overall, the results support the idea that glycobiological recognition may contribute to the functional integrity of the stromal cell layer as well as provide the basis for further analysis.

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“…Biotinylated lectins bound to the copolymers and were detected by standard methods. In a reverse approach, ELISA plates were coated with native lectin followed by copolymer containing both the haptenic monosaccharide and biotin or a neoglycoenzyme, and finally the lectin detected and quantified by standard methods [Gabius et al, 1989;Tichá et al, 1991;Hatakeyama et al, 1992]. Coating the plates with a lipophilic neoglycoconjugate [Hesse and Rüdiger, 1997] or with carbohydrate-containing copolymers generated in situ in the wells of the plate [Suffel and Rüdiger, 1997] has also proved to be suitable for detecting and quantifying biotinylated lectins.…”

Section: Defining the Carbohydrate Specificitymentioning

confidence: 99%