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Updated: Jul 13, 2026

Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion
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Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion

Published on: April 2, 2020

Regulation of c-Met signaling by the tetraspanin KAI-1/CD82 affects cancer cell migration

Miho Takahashi1, Tsuyoshi Sugiura1, Masakazu Abe1

  • 1Department of Oral and Maxillofacial Surgery, Graduate School of Dental Science, Kyushu University, Fukuoka, Japan.

International Journal of Cancer
|July 11, 2007
PubMed

Insights

The metastasis suppressor CD82 inhibits cancer cell migration by interacting with the HGF receptor c-Met. This complex selectively blocks specific signaling pathways, reducing cell movement.

Area of Science:

  • Molecular biology
  • Cell biology
  • Cancer research

Background:

  • CD82 (KAI-1) is a tetraspanin superfamily member known as a metastasis suppressor.
  • CD82 is proposed to regulate biological activity through associations with cell surface receptors.
  • The hepatocyte growth factor (HGF) receptor c-Met plays a role in cell migration and cancer progression.

Purpose of the Study:

  • To investigate the novel association between CD82 and the c-Met receptor.
  • To determine the functional consequences of CD82-c-Met interaction on HGF-induced signaling and cell migration.
  • To elucidate the specific signaling pathways affected by CD82 in non-small cell lung carcinoma cells.

Main Methods:

  • Ectopic expression of CD82 in non-small cell lung carcinoma cells.
  • Analysis of HGF-induced c-Met tyrosine phosphorylation.
  • Assessment of HGF-induced lamellipodial protrusion and cell migration.
  • Investigation of c-Met signaling pathways, including Ras-Cdc42/Rac, PI3K/Cdc42/Rac, PI3K/Akt, and PI3K/MAPK.
  • Examination of the association between c-Met and signaling adapter proteins (Grb2, p85).

Main Results:

  • A novel association between CD82 and the c-Met receptor was identified.
  • Ectopic CD82 expression suppressed HGF-induced lamellipodial protrusion and cell migration.
  • CD82 selectively attenuated c-Met signaling via Ras-Cdc42/Rac and PI3K/Cdc42/Rac pathways.
  • CD82 did not affect PI3K/Akt or PI3K/MAPK signaling pathways downstream of c-Met.
  • Reduced association of Grb2 and p85 with c-Met was observed in cells expressing CD82.

Conclusions:

  • The CD82-c-Met complex inhibits HGF-induced cancer cell migration.
  • This inhibition occurs through the inactivation of Rho family GTP-binding proteins via c-Met adapter proteins.
  • CD82 acts as a regulator of c-Met signaling, impacting cancer cell motility.

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