Translating the 'Sugar Code' into Immune and Vascular Signaling Programs. Issue 4 (April 2017)
- Record Type:
- Journal Article
- Title:
- Translating the 'Sugar Code' into Immune and Vascular Signaling Programs. Issue 4 (April 2017)
- Main Title:
- Translating the 'Sugar Code' into Immune and Vascular Signaling Programs
- Authors:
- Cerliani, Juan P.
Blidner, Ada G.
Toscano, Marta A.
Croci, Diego O.
Rabinovich, Gabriel A. - Abstract:
- Abstract : The vast range and complexity of glycan structures and their dynamic variations in health and disease have presented formidable challenges toward understanding the biological significance of these molecules. Despite these limitations, compelling evidence highlights a major role for galectins, a family of soluble glycan-binding proteins, as endogenous decoders that translate glycan-containing information into a broad spectrum of cellular responses by modulating receptor clustering, reorganization, endocytosis, and signaling. Here, we underscore pioneer findings and recent advances in understanding the biology of galectin–glycan interactions in myeloid, lymphoid, and endothelial compartments, highlighting important pathways by which these multivalent complexes control immune and vascular programs. Implementation of novel glycoanalytical approaches, as well as the use of genetically engineered cell and organism models, have allowed glycans and galectins to be explored across a range of cellular processes. Trends: Galectins initiate, amplify, or attenuate immune and vascular signaling programs by reprogramming the function of glycosylated receptors in the absence or presence of their canonical ligands. Galectin–glycan interactions act by modulating clustering, reorganization, distancing, internalization, and signaling of relevant receptors in myeloid, lymphoid, and endothelial compartments. A dynamic glycosylation signature on target cells controls theAbstract : The vast range and complexity of glycan structures and their dynamic variations in health and disease have presented formidable challenges toward understanding the biological significance of these molecules. Despite these limitations, compelling evidence highlights a major role for galectins, a family of soluble glycan-binding proteins, as endogenous decoders that translate glycan-containing information into a broad spectrum of cellular responses by modulating receptor clustering, reorganization, endocytosis, and signaling. Here, we underscore pioneer findings and recent advances in understanding the biology of galectin–glycan interactions in myeloid, lymphoid, and endothelial compartments, highlighting important pathways by which these multivalent complexes control immune and vascular programs. Implementation of novel glycoanalytical approaches, as well as the use of genetically engineered cell and organism models, have allowed glycans and galectins to be explored across a range of cellular processes. Trends: Galectins initiate, amplify, or attenuate immune and vascular signaling programs by reprogramming the function of glycosylated receptors in the absence or presence of their canonical ligands. Galectin–glycan interactions act by modulating clustering, reorganization, distancing, internalization, and signaling of relevant receptors in myeloid, lymphoid, and endothelial compartments. A dynamic glycosylation signature on target cells controls the immunoregulatory and proangiogenic activities of galectins. Galectins have emerged as novel therapeutic targets in autoimmunity, inflammation, fibrosis, and cancer, and their expression may confer resistance to anticancer therapies. … (more)
- Is Part Of:
- Trends in biochemical sciences. Volume 42:Issue 4(2017)
- Journal:
- Trends in biochemical sciences
- Issue:
- Volume 42:Issue 4(2017)
- Issue Display:
- Volume 42, Issue 4 (2017)
- Year:
- 2017
- Volume:
- 42
- Issue:
- 4
- Issue Sort Value:
- 2017-0042-0004-0000
- Page Start:
- 255
- Page End:
- 273
- Publication Date:
- 2017-04
- Subjects:
- endothelial cells -- galectins -- glycans -- lymphoid cells -- myeloid cells
Biochemistry -- Periodicals
572 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09680004 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.tibs.2016.11.003 ↗
- Languages:
- English
- ISSNs:
- 0968-0004
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 9049.546000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 8779.xml