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Galectins: their network and roles in immunity/tumor growth control.

Authors
  • Kaltner, Herbert1
  • Toegel, Stefan2
  • Caballero, Gabriel García1
  • Manning, Joachim C1
  • Ledeen, Robert W3
  • Gabius, Hans-Joachim4
  • 1 Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539, Munich, Germany. , (Germany)
  • 2 Karl Chiari Lab for Orthopaedic Biology, Department of Orthopaedics, Medical University of Vienna, 1090, Vienna, Austria. , (Austria)
  • 3 Department of Pharmacology, Physiology and Neurosciences, Rutgers - The State University of New Jersey, New Jersey Medical School, Newark, NJ, 07103, USA. , (Jersey)
  • 4 Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539, Munich, Germany. [email protected] , (Germany)
Type
Published Article
Journal
Histochemistry and cell biology
Publication Date
Feb 01, 2017
Volume
147
Issue
2
Pages
239–256
Identifiers
DOI: 10.1007/s00418-016-1522-8
PMID: 28012132
Source
Medline
Keywords
License
Unknown

Abstract

One route of realizing the information of glycans involves endogenous receptors (lectins). Occurrence at branch ends renders galactosides particularly accessible. Thus, they are suited for such a recognition process. Fittingly, these epitopes serve as physiological ligands. The ga(lactoside-binding) lectins share the β-sandwich fold with a sequence signature around a central tryptophan residue besides this specificity. Three modes of presentation of the carbohydrate recognition domain are known for galectins, and genome monitoring from fungi to mammals discloses that galectins form a network. The extent of its complexity varies considerably between organisms, for chicken reaching seven proteins, more for mammals. The current status of network analysis reveals overlapping and distinct expression profiles. Matching intra- and extracellular galectin presence, they have a broad range of functions at each site depending on their specific counterreceptor(s), with the possibility even for functional antagonism between family members. Orchestration of expression of galectin, the cognate glycan, its scaffold (protein or sphingolipid) and spatial aspects of glycoconjugate presentation has been detected to lead to growth regulation of immune and tumor cells. To delineate the factors that underlie the specificity of a galectin for its counterreceptor(s) in the cellular context and the details of structure-activity relationships by comparatively analyzing natural and rationally engineered proteins is the main challenge for ongoing research.

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