For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
24
views
37
references
 Top references
cited by
2
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      672
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Detection of galectins during malignant transformation of oral cells

      review-article

      Read this article at

      ScienceOpenPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Oral cancer is a common neoplasm world-wide. The incidence and mortality have increased over the past decades. It is characterized by poor prognosis and a low survival rate despite sophisticated surgical and radiotherapeutic modalities. Galectins are detected in a wide variety of tissues. The expression of galectins is modulated during the differentiation of individual cells and during the development of organisms and tissues, being altered in different physiological or pathological conditions including, carcinogenesis. In this review, we will discuss the role of galectins during the malignant transformation of oral cells, in order to understand their mechanisms of the action in a several cellular activities and test systems. Certainly, such information will contribute for understanding oral cancer pathogenesis.

          Related collections

          Most cited references37

          • Record: found
          • Abstract: found
          • Article: not found

          Galectins as modulators of tumour progression.

          Fu-Tong Liu, Gabriel Rabinovich (2005)
          Galectins are a family of animal lectins with diverse biological activities. They function both extracellularly, by interacting with cell-surface and extracellular matrix glycoproteins and glycolipids, and intracellularly, by interacting with cytoplasmic and nuclear proteins to modulate signalling pathways. Current research indicates that galectins have important roles in cancer; they contribute to neoplastic transformation, tumour cell survival, angiogenesis and tumour metastasis. They can modulate the immune and inflammatory responses and might have a key role helping tumours to escape immune surveillance. How do the different members of the Galectin family contribute to these diverse aspects of tumour biology?
          Article 0 comments Cited 381 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Galectin-3: an open-ended story.

            Jerka Dumić, Sanja Dabelic, Mirna Flögel (2006)
            Galectins, an ancient lectin family, are characterized by specific binding of beta-galactosides through evolutionary conserved sequence elements of carbohydrate-recognition domain (CRD). A structurally unique member of the family is galectin-3; in addition to the CRD it contains a proline- and glycine-rich N-terminal domain (ND) through which is able to form oligomers. Galectin-3 is widely spread among different types of cells and tissues, found intracellularly in nucleus and cytoplasm or secreted via non-classical pathway outside of cell, thus being found on the cell surface or in the extracellular space. Through specific interactions with a variety of intra- and extracellular proteins galectin-3 affects numerous biological processes and seems to be involved in different physiological and pathophysiological conditions, such as development, immune reactions, and neoplastic transformation and metastasis. The review attempts to summarize the existing information on structural, biochemical and intriguing functional properties of galectin-3.
            Article 0 comments Cited 304 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Galectin-1: a small protein with major functions.

              Robert Kiss, Florence Lefranc, Marie Le Mercier … (2006)
              Galectins are a family of carbohydrate-binding proteins with an affinity for beta-galactosides. Galectin-1 (Gal-1) is differentially expressed by various normal and pathological tissues and appears to be functionally polyvalent, with a wide range of biological activity. The intracellular and extracellular activity of Gal-1 has been described. Evidence points to Gal-1 and its ligands as one of the master regulators of such immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host-pathogen interactions. Gal-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Gal-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Gal-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Gal-1 expression is what should be developed for therapeutic applications against cancer progression. Gal-1 is thus a promising molecular target for the development of new and original therapeutic tools.
              Article 0 comments Cited 171 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Dent Res J (Isfahan)
                Journal ID (iso-abbrev): Dent Res J (Isfahan)
                Journal ID (publisher-id): DRJ
                Title: Dental Research Journal
                Publisher: Medknow Publications & Media Pvt Ltd (India )
                ISSN (Print): 1735-3327
                ISSN (Electronic): 2008-0255
                Publication date (Print): Jul-Aug 2013
                Volume: 10
                Issue: 4
                Pages: 428-433
                Affiliations
                [1 ]Department of Pathology, Federal University of São Paulo, UNIFESP, SP, Brazil
                [2 ]Department of Biosciences, Federal University of São Paulo, UNIFESP, SP, Brazil
                Author notes
                Address for correspondence: Dr. Daniel A. Ribeiro, Departamento de Biociências, Universidade Federal de São Paulo – UNIFESP, Av. Ana Costa, 95, Vila Mathias, Santos – SP, 11060 - 001, Brazil. E-mail: daribeiro@ 123456unifesp.br
                Article
                Publisher ID: DRJ-10-428
                PMC ID: 3793403
                PubMed ID: 24130575
                SO-VID: 6776b5bd-1a9e-4009-984e-acd392ee3cf7
                Copyright © Copyright: © Dental Research Journal
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : October 2012
                Date accepted : January 2013
                Categories
                Subject: Review Article

                ScienceOpen disciplines: Dentistry
                Keywords: galectin,in vivo,in vitro,oral cancer
                Data availability:
                ScienceOpen disciplines: Dentistry
                Keywords: galectin, in vivo, in vitro, oral cancer

                Comments

                Comment on this article

                Similar content672

                See all similar

                Cited by2

                See all cited by

                Most referenced authors815

                See all reference authors