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The biology and role of CD44 in cancer progression: therapeutic implications

Chen, Chen, Zhao, Shujie, Karnad, Anand, Freeman, James W.·2018·Journal of Hematology & Oncology
DOI 10.1186/s13045-018-0605-5PMC PMC5946470
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Fig. 1 CD44 protein and gene structure. a Four domains of CD44 glycoprotein are presented with correponding colors: ligand binding domain, variable domain, transmembrane domain, and cytoplasmic tail. b CD44 is encoded by 20 exons in mice but 19 exons in humans. Exon 6 coding for CD44 variant 1 (CD44v1) is lacking in humans. Green color exons are always expressed as a standard form of CD44 (CD44s), and up to nine exon variants can be inserted by alternative splicing. Full-length CD44, CD44s, CD44v3, CD44v6, and CD44v8-10 are shown schematically
Fig. 1 CD44 protein and gene structure. a Four domains of CD44 glycoprotein are presented with correponding colors: ligand binding domain, variable domain, transmembrane domain, and cytoplasmic tail. b CD44 is encoded by 20 exons in mice but 19 exons in humans. Exon 6 coding for CD44 variant 1 (CD44v1) is lacking in humans. Green color exons are always expressed as a standard form of CD44 (CD44s), and up to nine exon variants can be inserted by alternative splicing. Full-length CD44, CD44s, CD44v3, CD44v6, and CD44v8-10 are shown schematicallyCC BY · PubMed Central
Fig. 2 Molecules regulate promoter activity and expression. a Several transcription factors including positive or negative regulators bind to the CD44 promoter region and regulate its activity. b Epithelial splicing regulatory protein 1 (ESRP1) is required for alternative splicing which generates different CD44 variant isoforms
Fig. 2 Molecules regulate promoter activity and expression. a Several transcription factors including positive or negative regulators bind to the CD44 promoter region and regulate its activity. b Epithelial splicing regulatory protein 1 (ESRP1) is required for alternative splicing which generates different CD44 variant isoformsCC BY · PubMed Central
Fig. 3 CD44 promoter activity comparison among different treatment of cytokines groups. TGFβ, HGF, IL-6, IGF1, and EGF treated on CFPAC-1 CD44 low cells. TGFβ transforming growth factor β, HGF hepatocyte growth factor, IL-6 interleukin-6, IGF1 insulin-like growth factor 1, EGF epidermal growth factor
Fig. 3 CD44 promoter activity comparison among different treatment of cytokines groups. TGFβ, HGF, IL-6, IGF1, and EGF treated on CFPAC-1 CD44 low cells. TGFβ transforming growth factor β, HGF hepatocyte growth factor, IL-6 interleukin-6, IGF1 insulin-like growth factor 1, EGF epidermal growth factorCC BY · PubMed Central
Fig. 4 CD44-mediated downstream signaling pathways. CD44s and CD44v6 are shown as representative CD44 isoforms that mediate specific downstream signaling pathways. CD44v6 can recruite ezrin/radixin/moesin (ERM) proteins that promote cytosketal changes and that may interact with VEGFR contributing angiogenesis, cancer cell division, and proliferation. CD44v can act as a coreceptor for the receptor tyrosine kinase c-Met to promote cancer cell invasion. CD44s can change cytoskeleton structure mediating Snail/β-catenin translocation to the nucleus promoting transcrition of the matrix metalloproteinases (MMP) family or urokinase-type plasminogen activator (uPA) expression causing an increase in cancer cell invasion. CD44s can also enhance activation of the PI3K/AKT pathway contributing to cancer cell invasion and proliferation. CD44 modulates Src/MAPK signaling pathway leading to cancer cell division and proliferation. CD44 also causes Hypoxia-inducible factor 1α (HIF1α) binding to nuclear DNA to increase glycolysis, in turn rendering a metabolic shift in cancer cells
Fig. 4 CD44-mediated downstream signaling pathways. CD44s and CD44v6 are shown as representative CD44 isoforms that mediate specific downstream signaling pathways. CD44v6 can recruite ezrin/radixin/moesin (ERM) proteins that promote cytosketal changes and that may interact with VEGFR contributing angiogenesis, cancer cell division, and proliferation. CD44v can act as a coreceptor for the receptor tyrosine kinase c-Met to promote cancer cell invasion. CD44s can change cytoskeleton structure mediating Snail/β-catenin translocation to the nucleus promoting transcrition of the matrix metalloproteinases (MMP) family or urokinase-type plasminogen activator (uPA) expression causing an increase in cancer cell invasion. CD44s can also enhance activation of the PI3K/AKT pathway contributing to cancer cell invasion and proliferation. CD44 modulates Src/MAPK signaling pathway leading to cancer cell division and proliferation. CD44 also causes Hypoxia-inducible factor 1α (HIF1α) binding to nuclear DNA to increase glycolysis, in turn rendering a metabolic shift in cancer cellsCC BY · PubMed Central

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Metadata

Authors
Chen, C., Zhao, S., Karnad, A., & Freeman, J. W.
Venue
Journal of Hematology & Oncology
Publisher
Springer Science and Business Media LLC
Published
2018-05-10
Volume
11
Issue
1
ISSN
1756-8722
DOI
10.1186/s13045-018-0605-5
PMC
PMC5946470
Cited by
1,245
References
2
Language
en
Licence
Funders
  • National Cancer Institute (P30CA054174)
  • U.S. Department of Veterans Affairs (510BX002962)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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