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Hierarchy of ADAM12 binding to integrins in tumor cells

Charles Kumar Thodeti1, Camilla Fröhlich, Christian Kamp Nielsen

  • 1Institute of Molecular Pathology, University of Copenhagen, Frederik V's vej 11, DK-2100 Copenhagen, Denmark.

Experimental Cell Research
|August 3, 2005
PubMed

Insights

Alpha9beta1 integrin is the primary receptor for ADAM12 (a disintegrin and metalloprotease), mediating cell adhesion. Other beta1 integrins can compensate when alpha9beta1 is absent, influencing cell spreading via phosphoinositide-3-kinase signaling.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • ADAMs (a disintegrin and metalloprotease) are cell surface proteins with protease and cell-binding functions.
  • Integrins are key mediators of cell adhesion and signaling.

Purpose of the Study:

  • To identify the specific integrin receptors for ADAM12.
  • To investigate the role of integrin activation in ADAM12-mediated cell spreading.

Main Methods:

  • Cell adhesion and spreading assays using various ADAM12 forms and fragments.
  • Analysis of integrin-dependent cell attachment.
  • Investigation of the role of phosphoinositide-3-kinase in integrin signaling.

Main Results:

  • Alpha9beta1 integrin is the principal receptor for ADAM12, mediating tumor cell attachment.
  • Alternative beta1 integrins can mediate attachment when alpha9beta1 is not expressed.
  • Cell spreading on ADAM12 is dependent on integrin activation levels, with phosphoinositide-3-kinase playing a central regulatory role.

Conclusions:

  • ADAM12 utilizes alpha9beta1 integrin as its main receptor, but can engage other beta1 integrins.
  • Integrin activation status critically regulates ADAM12-induced cell spreading, involving phosphoinositide-3-kinase signaling.

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