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Titolo:
Glycohistochemistry: The why and how of detection and localization of endogenous lectins
Autore:
Gabius, HJ;
Indirizzi:
Univ Munich, Tierarztliche Fak, Inst Physiol Chem, D-80539 Munich, GermanyUniv Munich Munich Germany D-80539 Physiol Chem, D-80539 Munich, Germany
Titolo Testata:
Anatomia, histologia, embryologia
fascicolo: 1, volume: 30, anno: 2001,
pagine: 3 - 31
SICI:
0340-2096(200102)30:1<3:GTWAHO>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-CARBOHYDRATE INTERACTIONS; CYSTEINE-RICH DOMAIN; HEPARIN-BINDING LECTIN; METHYL BETA-LACTOSIDE; ASPARAGINE-LINKED OLIGOSACCHARIDES; MANNOSE 6-PHOSPHATE RECEPTORS; BIOTINYLATED HYALURONIC-ACID; SQUAMOUS-CELL CARCINOMAS; BOVINE HEART GALECTIN-1; SPERM-EGG INTERACTION;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
440
Recensione:
Indirizzi per estratti:
Indirizzo: Gabius, HJ Univ Munich, Tierarztliche Fak, Inst Physiol Chem, Vet Str 13, D-80539 Munich, Germany Univ Munich Vet Str 13 Munich Germany D-80539 Munich, Germany
Citazione:
H.J. Gabius, "Glycohistochemistry: The why and how of detection and localization of endogenous lectins", ANAT HISTOL, 30(1), 2001, pp. 3-31

Abstract

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 emergedthat it would have meant missing manifold opportunities not to recruit thesugar 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 beengaged in oligosaccharide recognition. After their isolation these tissuelectins 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 18:53:38