The Involvement of the Oligosaccharide Chains of Glycoproteins in Gamete Interactions at Fertilization

Hirohashi, Noritaka; Lennarz, William J.; Ernst, Beat; Hart, Gerald W.; Sînaÿ, Pierre

doi:10.1002/9783527618255.ch93

Cited by 1 publication

(2 citation statements)

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“…Fluorescent labelling can be used as an alternative to this type of enzyme cytochemistry. By means of¯uorescence microscopy the speci®c binding of carbohydrates to spermatozoa has been detected (Sinowatz et al, 1988(Sinowatz et al, , 1989, thereby supporting the hypothesis that glycan recognition plays an important role in mammalian fertilization (Shalgi and Raz, 1997;Sinowatz et al, 1997Sinowatz et al, , 1998McLeskey et al, 1998;Dell et al, 1999;Takasaki et al, 1999;Wassarman, 1999;Hirohashi and Lennarz, 2000). This con®rms what Lillie had postulated in 1912, that a lock-and-key mechanism appeared to guide the sperm±egg interaction (Lillie, 1913).…”

Section: Reverse Lectin Cyto-and Histochemistrysupporting

confidence: 56%

“…Carbodiimide-mediated incorporation of p-aminophenyl glycosides was the basis for the establishment of a non-radioactive, rapid and sensitive assay, which has extended application beyond lectinology in other branches of receptor analysis (S. . By means of¯uorescence microscopy the speci®c binding of carbohydrates to spermatozoa has been detected (Sinowatz et al, 1988(Sinowatz et al, , 1989, thereby supporting the hypothesis that glycan recognition plays an important role in mammalian fertilization (Shalgi and Raz, 1997;Sinowatz et al, 1997Sinowatz et al, , 1998McLeskey et al, 1998;Dell et al, 1999;Takasaki et al, 1999;Wassarman, 1999;Hirohashi and Lennarz, 2000). These studies have also detected binding sites which mediate cell adhesion to a matrix presenting the appropriate carbohydrates (S. Wawotzny et al, 1995).…”

Section: Reverse Lectin Cyto-and Histochemistrymentioning

confidence: 75%

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Glycohistochemistry: The Why and How of Detection and Localization of Endogenous Lectins

Gabius¹

2001

Anat Histol Embryol

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The central dogma of molecular biology limits the downstream flow of genetic information to proteins. Progress from the last two decades of research on cellular glycoconjugates justifies adding the enzymatic production of glycan antennae with information-bearing determinants to this famous and basic pathway. An impressive variety of regulatory processes including cell growth and apoptosis, folding and routing of glycoproteins and cell adhesion/migration have been unravelled and found to be mediated or modulated by specific protein (lectin)-carbohydrate interactions. The conclusion has emerged that it would have meant missing manifold opportunities not to recruit the sugar code to cellular information transfer. Currently, the potential for medical applications in anti-adhesion therapy or drug targeting is one of the major driving forces fuelling progress in glycosciences. In histochemistry, this concept has prompted the introduction of carrier-immobilized carbohydrate ligands (neoglycoconjugates) to visualize the cells' capacity to be engaged in oligosaccharide recognition. After their isolation these tissue lectins will be tested for ligand analysis. Since fine specificities of different lectins can differ despite identical monosaccharide binding, the tissue lectins will eventually replace plant agglutinins to move from glycan profiling and localization to functional considerations. Namely, these two marker types, i.e. neoglycoconjugates and tissue lectins, track down accessible binding sites with relevance for involvement in interactions in situ. The documented interplay of synthetic organic chemistry and biochemistry with cyto- and histochemistry nourishes the optimism that the application of this set of innovative custom-prepared tools will provide important insights into the ways in which glycans can act as hardware in transmitting information during normal tissue development and pathological situations.

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