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10.1182/blood-2015-09-668962

http://scihub22266oqcxt.onion/10.1182/blood-2015-09-668962
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suck abstract from ncbi


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pmid26679542
      Blood 2015 ; 126 (25 ): 2658-9
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  • The Rap1-RIAM pathway prefers ?2 integrins #MMPMID26679542
  • Calderwood DA
  • Blood 2015[Dec]; 126 (25 ): 2658-9 PMID26679542 show ga
  • In vitro studies strongly implicate the talin-binding Ras-related protein 1 (Rap1) effector, Rap1-guanosine triphosphate?interacting adapter molecule (RIAM), in integrin activation. Yet, the RIAM knockout mouse is viable and fertile and exhibits no platelet adhesion or aggregation defects, casting doubt on the in vivo role of RIAM. In this issue of Blood, Su et al and Klapproth et al now show that RIAM is required for ?2 integrin?dependent leukocyte adhesion and trafficking in vitro and in vivo, but apparently not for all Rap- and talin-meditated activation of ?1 and ?3 integrins.
  • |Adaptor Proteins, Signal Transducing/*immunology/*metabolism [MESH]
  • |Animals [MESH]
  • |B-Lymphocytes/*immunology [MESH]
  • |CD18 Antigens/*metabolism [MESH]
  • |Chemotaxis, Leukocyte/*immunology/*physiology [MESH]
  • |Leukocytes/*metabolism [MESH]
  • |Membrane Proteins/*immunology/*metabolism [MESH]


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