For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
35
views
76
references
 Top references
cited by
301
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
1 collections
    0
    shares
      1,086
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found

      Reprogramming glucose metabolism in cancer: can it be exploited for cancer therapy?

      Author(s): 1
      Publication date (Electronic):
      Journal: Nature reviews. Cancer
      Publisher: Springer Nature

      Read this article at

      ScienceOpenPublisherPubMed
          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

          In recent years there has been a growing interest among cancer biologists in cancer metabolism. This Review summarizes past and recent advances in our understanding of the reprogramming of glucose metabolism in cancer cells, which is mediated by oncogenic drivers and by the undifferentiated character of cancer cells. The reprogrammed glucose metabolism in cancer cells is required to fulfil anabolic demands. This Review discusses the possibility of exploiting the reprogrammed glucose metabolism for therapeutic approaches that selectively target cancer cells.

          Related collections

          Most cited references76

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

          Phosphoglycerate dehydrogenase diverts glycolytic flux and contributes to oncogenesis.

          Jason Locasale, Alexandra R. Grassian, Tamar Melman … (2011)
          Most tumors exhibit increased glucose metabolism to lactate, however, the extent to which glucose-derived metabolic fluxes are used for alternative processes is poorly understood. Using a metabolomics approach with isotope labeling, we found that in some cancer cells a relatively large amount of glycolytic carbon is diverted into serine and glycine metabolism through phosphoglycerate dehydrogenase (PHGDH). An analysis of human cancers showed that PHGDH is recurrently amplified in a genomic region of focal copy number gain most commonly found in melanoma. Decreasing PHGDH expression impaired proliferation in amplified cell lines. Increased expression was also associated with breast cancer subtypes, and ectopic expression of PHGDH in mammary epithelial cells disrupted acinar morphogenesis and induced other phenotypic alterations that may predispose cells to transformation. Our findings show that the diversion of glycolytic flux into a specific alternate pathway can be selected during tumor development and may contribute to the pathogenesis of human cancer.
          Article 0 comments Cited 433 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Targeting lactate metabolism for cancer therapeutics.

            Joanne R. Doherty, John L. Cleveland (2013)
            Lactate, once considered a waste product of glycolysis, has emerged as a critical regulator of cancer development, maintenance, and metastasis. Indeed, tumor lactate levels correlate with increased metastasis, tumor recurrence, and poor outcome. Lactate mediates cancer cell intrinsic effects on metabolism and has additional non-tumor cell autonomous effects that drive tumorigenesis. Tumor cells can metabolize lactate as an energy source and shuttle lactate to neighboring cancer cells, adjacent stroma, and vascular endothelial cells, which induces metabolic reprogramming. Lactate also plays roles in promoting tumor inflammation and in functioning as a signaling molecule that stimulates tumor angiogenesis. Here we review the mechanisms of lactate production and transport and highlight emerging evidence indicating that targeting lactate metabolism is a promising approach for cancer therapeutics.
            Article 0 comments Cited 431 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              The SLC2 (GLUT) family of membrane transporters.

              Mike Mueckler, Bernard Thorens (2013)
              GLUT proteins are encoded by the SLC2 genes and are members of the major facilitator superfamily of membrane transporters. Fourteen GLUT proteins are expressed in the human and they are categorized into three classes based on sequence similarity. All GLUTs appear to transport hexoses or polyols when expressed ectopically, but the primary physiological substrates for several of the GLUTs remain uncertain. GLUTs 1-5 are the most thoroughly studied and all have well established roles as glucose and/or fructose transporters in various tissues and cell types. The GLUT proteins are comprised of ∼500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 membrane-spanning domains. In this review we briefly describe the major characteristics of the 14 GLUT family members. Copyright © 2012 Elsevier Ltd. All rights reserved.
              Article 0 comments Cited 419 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (iso-abbrev): Nat. Rev. Cancer
                Title: Nature reviews. Cancer
                Publisher: Springer Nature
                ISSN (Electronic): 1474-1768
                ISSN (Print): 1474-175X
                Publication date (Electronic): October 2016
                Volume: 16
                Issue: 10
                Affiliations
                [1 ] Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607 and Research and Development Section, Jesse Brown VA Medical Center, Chicago, Illinois 60612, USA.
                Article
                Publisher Item ID: nrc.2016.77
                DOI: 10.1038/nrc.2016.77
                PubMed ID: 27634447
                SO-VID: 273195ce-32b2-48cc-a89a-1ba989eb6376
                History

                Data availability:

                Comments

                Comment on this article

                scite_

                Similar content1,086

                See all similar

                Cited by445

                See all cited by

                Most referenced authors1,982

                See all reference authors