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Role of multiple β1 integrins in cell adhesion to the disintegrin domains of ADAMs 2 and 3

Experimental Cell Research
Publication Date
DOI: 10.1016/s0014-4827(03)00307-0
  • Adam-Integrin Interactions
  • Disintegrin-Integrin Interactions
  • Fertilin β
  • Cyritestin
  • Murine Fertilization
  • Oviduct
  • Biology


Abstract ADAM disintegrin domains can support integrin-mediated cell adhesion. However, the profile of which integrins are employed for adhesion to a given disintegrin domain remains unclear. For example, we suggested that the disintegrin domains of mouse sperm ADAMs 2 and 3 can interact with the α6β1 integrin on mouse eggs. Others concluded that these disintegrin domains interact instead with the α9β1 integrin. To address these differing results, we first studied adhesion of mouse F9 embryonal carcinoma cells and human G361 melanoma cells to the disintegrin domains of mouse ADAMs 2 and 3. Both cell lines express α6β1 and α9β1 integrins at their surfaces. Antibodies to the α6 integrin subunit inhibited adhesion of both cell lines. An antibody that recognizes human α9 integrin inhibited adhesion of G361 cells. VLO5, a snake disintegrin that antagonizes α4β1 and α9β1 integrins, potently inhibited adhesion of both cell lines. We next explored expression of the α9 integrin subunit in mouse eggs. In contrast to our ability to detect α6β1, we were unable to convincingly detect α9β1 integrin on the surface of mouse eggs. Moreover, treatment of mouse eggs with 250 nm VLO5, which is 250 fold over its ∼IC 50 for inhibition of somatic cell adhesion, had minimal effect on sperm-egg binding or fusion. We did detect α9 integrin protein on epithelial cells of the oviduct. Additional studies showed that antibodies to the α6 and α7 integrins additively inhibited adhesion of mouse trophoblast stem cells and that an antibody to the α4 integrin inhibited adhesion of MOLT-3 cells to these disintegrin domains: Our data suggest that multiple integrins (on the same cell) can participate in adhesion to a given ADAM disintegrin domain and that interactions between ADAMs and integrins may be important for sperm transit through the oviduct.

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