From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins.
About 60 years ago, the efforts to identify blood group-specific haemagglutinins in plant extracts by broad-scale testing were beginning to make a large panel of these proteins available as laboratory tools. Their ability to ‘read’ cell surface signals like antibodies do was the reason for W. C. Boy...
| Publicado en: | Histochemistry & Cell Biology Vol. 149; no. 6; pp. 547 - 569 |
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| Autores principales: | , , , , |
| Formato: | Journal Article |
| Publicado: |
Springer Nature
Jun2018
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=130148057&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 130148057 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 09486143 NQI jtl: Histochemistry & Cell Biology issn: 09486143 maglogo: N pubinfo: dt: Jun2018 vid: 149 iid: 6 pid: 237 pub: Springer Nature place: New York, New York artinfo: ui: 130148057 10.1007/s00418-018-1676-7 130148057 ppf: 547 ppct: 22 formats: fmt: – @attributes: type: T – @attributes: type: P tig: atl: From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins. aug: au: Kaltner, Herbert García Caballero, Gabriel Ludwig, Anna-Kristin Manning, Joachim C. Gabius, Hans-Joachim affil: Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany sug: ab: About 60 years ago, the efforts to identify blood group-specific haemagglutinins in plant extracts by broad-scale testing were beginning to make a large panel of these proteins available as laboratory tools. Their ability to ‘read’ cell surface signals like antibodies do was the reason for W. C. Boyd to call them lectins, from Latin legere (to read). These proteins turned out to be as widely present in nature as glycans (polysaccharides or carbohydrate chains of cellular glycoconjugates) are. Since carbohydrates have the virtue to facilitate high-density coding in a minimum of space and lectins (initially mostly from plants called phytohaemagglutinins) turned out to be receptors for glycans, their pairing made many applications possible. Most prominently, these proteins were instrumental to map glycome complexity and sites of product generation during glycan assembly in the cell. The detection of mammalian (tissue) lectins and the emerging evidence for intimate molecular recognition between this class of receptors and their (glycoconjugate) counterreceptors substantiate that understanding the rules of the sugar code is presently a major challenge. pubtype: Academic Journal doctype: Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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