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Related Concept Videos

Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

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The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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E-Cadherin-Deficient Epithelial Cells Are Sensitive to HDAC Inhibitors.

Lyvianne Decourtye-Espiard1, Nicola Bougen-Zhukov1, Tanis Godwin1

  • 1Cancer Genetics Laboratory, Centre for Translational Cancer Research (Te Aho Matatū), Department of Biochemistry, University of Otago, Dunedin 9016, New Zealand.

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|January 11, 2022
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Histone deacetylase (HDAC) inhibitors, particularly entinostat, show promise in treating cancers with CDH1 gene mutations. These drugs inhibit tumor growth by increasing apoptosis in CDH1-deficient cells.

Keywords:
CDH1E-cadherinHDAC inhibitorsHDGCsynthetic lethality

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Area of Science:

  • Cancer Biology
  • Genetics
  • Pharmacology

Background:

  • Germline CDH1 mutations define hereditary diffuse gastric cancer (HDGC).
  • Somatic CDH1 mutations are early events in sporadic diffuse gastric cancer (DGC) and lobular breast cancer (LBC).
  • CDH1 encodes the E-cadherin protein, crucial for cell adhesion.

Purpose of the Study:

  • To investigate the efficacy of histone deacetylase (HDAC) inhibitors in targeting cancer cells with deficient CDH1 expression.
  • To evaluate the potential of HDAC inhibitors for chemoprevention and treatment of CDH1-deficient cancers.

Main Methods:

  • Testing HDAC inhibitors (entinostat, pracinostat, mocetinostat, vorinostat) on human cell lines (MCF10A, NCI-N87) and murine organoids lacking CDH1.
  • Assessing cell growth inhibition, apoptosis, and effects of TP53 deletion.
  • Examining CDH1 expression changes in response to entinostat.

Main Results:

  • CDH1-deficient breast and gastric cancer cells showed increased sensitivity to pan-HDAC inhibitors, leading to greater growth inhibition and apoptosis.
  • While CDH1-null cells responded to class-specific HDAC inhibitors, pan-inhibitors were more robust across different genetic backgrounds.
  • Entinostat demonstrated efficacy in gastric organoids with combined CDH1 and TP53 deletions, unlike other tested inhibitors.
  • Entinostat treatment increased CDH1 expression in heterozygous CDH1 murine organoids.

Conclusions:

  • Entinostat is a potential therapeutic agent for hereditary diffuse gastric cancer (HDGC) and sporadic CDH1-deficient cancers.
  • HDAC inhibitors offer a targeted approach for cancers characterized by CDH1 loss.
  • Further research into entinostat's role in cancer chemoprevention and treatment is warranted.