Applications of Lectins and Neoglycoconjugates in Histology and Pathology

Danguy, André; Decaestecker, Christine; Genten, Franck; Salmon, Isabelle; Kiss, Róbert

doi:10.1159/000046459

Cited by 56 publications

(21 citation statements)

References 68 publications

(77 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lectins are carbohydrate-binding proteins found widely in plant and animal tissues [7,8,12,17]. Their specific carbohydrate-binding properties allow lectins to recognize particular glycoconjugates, suggesting that lectins participate in the regulation of physiological and pathological processes that involve binding of specific glycoconjugates [6,13,28].…”

Section: Discussionmentioning

confidence: 99%

Lectin binding patterns of alveolar epithelium and subepithelial seromucous glands of the bronchi in sepsis and controls – an approach to characterize the non-specific immunological response of the human lung to sepsis

2001

View full text Add to dashboard Cite

A delayed or deficient immunological protection as well as an overstimulation of the mucosal immune system may act as possible additional promoters of sepsis-induced lung injury in patients suffering from a severe septic condition. Lectin-binding patterns in pulmonary tissue samples obtained at autopsy from septic patients and control individuals were studied using 11 carbohydrate-specific lectins (Con A, UEA, GSA I, GSA II, MPA, PNA, Jac, WGA, MAA, LPA, and SNA). There were no differences in the secretory product of serous parts of bronchial glands detectable in the two study groups, whereas lectin binding patterns of alveolar epithelium and mucous parts of subepithelial seromucous glands were different in sepsis cases when compared to controls. Apart from differences in binding sites for alpha-mannose, N-acetyl-neuraminic acid and alpha-(2-6)-galactose (as detected by different expression for Con A, MAA and SNA) in the two study groups, the main finding was that no binding sites for alpha-N-acetyl-galactosamine (as investigated by MPA immunoreactivity) could be detected on alveolar epithelial cells and mucous parts of subepithelial seromucous glands in sepsis cases in contrast to the presence of such binding sites in the control cases. We hypothesize that the finding of an altered secretory product of alveolar epithelial cells and bronchial glands in sepsis may be a result of specific carbohydrate deprivation or consumption, respectively, possibly due to direct bacterial effects or pathogenetic events in response to bacterial toxins during the complex cascade of the host's systemic inflammatory response in sepsis. The altered type of mucus glycoprotein physiologically secreted by alveolar epithelium and mucous parts of subepithelial seromucous glands of the bronchi with subsequent loss of a considerable proportion of protection of the mucosal barrier in sepsis may play an important additional role in the development of sepsis-induced lung injury.

show abstract

Section: Discussionmentioning

confidence: 99%

Lectin binding patterns of alveolar epithelium and subepithelial seromucous glands of the bronchi in sepsis and controls – an approach to characterize the non-specific immunological response of the human lung to sepsis

2001

View full text Add to dashboard Cite

show abstract

“…For example, one defect in the mutant capsule may be a change in the composition of the extracellular matrix (ECM), as there is an ectopic reactivity of PNA and lectins adhere to sugar moieties of glycoproteins that are often expressed in the ECM (Faraggiana et al, 1982). Indeed, a change in lectin histochemistry is a valid criterion of disease in the study of pathology (Danguy et al, 1998;Silva et al, 1993).…”

Section: Loss Of Foxd1 Expression Results In Fused Kidneys Due To Capmentioning

confidence: 99%

Foxd1-dependent signals control cellularity in the renal capsule, a structure required for normal renal development

et al. 2005

View full text Add to dashboard Cite

Development of the metanephric kidney involves the establishment of discrete zones of induction and differentiation that are crucial to the future radial patterning of the organ. Genetic deletion of the forkhead transcription factor, Foxd1, results in striking renal abnormalities, including the loss of these discrete zones and pelvic fused kidneys. We have investigated the molecular and cellular basis of the kidney phenotypes displayed by Foxd1-null embryos and report here that they are likely to be caused by a failure in the correct formation of the renal capsule. Unlike the single layer of Foxd1-positive stroma that comprises the normal renal capsule, the mutant capsule contains heterogeneous layers of cells, including Bmp4-expressing cells, which induce ectopic phospho-Smad1 signaling in nephron progenitors. This missignaling disrupts their early patterning,which, in turn, causes mispatterning of the ureteric tree, while delaying and disorganizing nephrogenesis. In addition, the defects in capsule formation prevent the kidneys from detaching from the body wall, thus explaining their fusion and pelvic location. For the first time, functions have been ascribed to the renal capsule that include delineation of the organ and acting as a barrier to inappropriate exogenous signals, while providing a source of endogenous signals that are crucial to the establishment of the correct zones of induction and differentiation.

show abstract

“…As exemplarily documented in figure 28 for carbohydrate-reactive sites in the epineurium of a human accessory nerve [611,612], specific glycoligand-dependent binding can readily be assessed. Thus, the monitoring of accessible binding sites on cells and in tissues by glycohistochemistry [218,219,606,613,614] can guide further efforts to purify the observed activity. In histopathology, this class of markers leads to results equivalent to the application of antilectin antibodies [220,[615][616][617][618][619][620][621][622].…”

Section: Glycan Recognitionmentioning

confidence: 99%

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Reuter¹,

Gabius²

1999

Cellular and Molecular Life Sciences (CMLS)

214

141

View full text Add to dashboard Cite

Protein and lipid glycosylation is a ubiquitous phenomenon. The task of cataloguing the great structural variety of the glycan part has demanded considerable efforts over decades. This patient endeavor was imperative to discern the inherent rules of glycosylation which cannot affirm assumptions on a purely coincidental nature of this type of protein and lipid modification. These results together with theoretical considerations uncover a salient property of oligosaccharides. In comparison with amino acids and nucleotides, monosaccharides excel in their potential to serve as units of hardware for storing biological information. Thus, the view that glycan chains exclusively affect physiochemical properties of the conjugates is indubitably flawed. This original concept has been decisively jolted by the discovery of endogenous receptors (lectins) for distinct glycan epitopes which are as characteristic as a fingerprint or a signature for a certain protein (class) or cell type. Recent evidence documents that these binding proteins are even endowed with the capacity to select distinct low-energy conformers of the often rather flexible oligosaccharides, granting entry to a new level of regulation of ligand affinity by shifting conformer equilibria. The assessment of the details of this recognition by X-ray crystallography, nuclear magnetic resonance spectroscopy, microcalorimetry and custom-made derivatives is supposed to justify a guarded optimism in satisfying the need for innovative drug design in antiadhesion therapy, for example against viral or bacterial infections and unwanted inflammation. This review presents a survey of the structural aspects of glycosylation and of evidence to poignantly endorse the notion that carrier-attached glycan chains can partake in biological information transfer at the level of cell compartments, cells and organs.

show abstract

Applications of Lectins and Neoglycoconjugates in Histology and Pathology

Cited by 56 publications

References 68 publications

Lectin binding patterns of alveolar epithelium and subepithelial seromucous glands of the bronchi in sepsis and controls – an approach to characterize the non-specific immunological response of the human lung to sepsis

Lectin binding patterns of alveolar epithelium and subepithelial seromucous glands of the bronchi in sepsis and controls – an approach to characterize the non-specific immunological response of the human lung to sepsis

Foxd1-dependent signals control cellularity in the renal capsule, a structure required for normal renal development

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Contact Info

Product

Resources

About