Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin.

نویسندگان

  • M Udani
  • Q Zen
  • M Cottman
  • N Leonard
  • S Jefferson
  • C Daymont
  • G Truskey
  • M J Telen
چکیده

Sickle red cells bind significant amounts of soluble laminin, whereas normal red cells do not. Solid phase assays demonstrate that B-CAM/LU binds laminin on intact sickle red cells and that red cell B-CAM/LU binds immobilized laminin, whereas another putative laminin binding protein, CD44, does not. Ligand blots also identify B-CAM/LU as the only erythrocyte membrane protein(s) that binds laminin. Finally, transfection of murine erythroleukemia cells with human B-CAM cDNA induces binding of both soluble and immobilized laminin. Thus, B-CAM/LU appears to be the major laminin-binding protein of sickle red cells. Previously reported overexpression of B-CAM/LU by epithelial cancer cells suggests that this protein may also serve as a laminin receptor in malignant tumors.

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Vaso-occlusion is a hallmark of sickle cell disease. Agonist-induced activation of sickle red blood cells (SS RBCs) promotes their adhesion to vascular proteins, potentially contributing to vasoocclusion. Previously, we described a cyclic adenosine monophosphate (cAMP)–dependent increase in SS RBC adhesion to laminin. Here, we investigated whether Rap1, a small guanosine triphosphatase (GTPase)...

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Role of Rap1 in promoting sickle red blood cell adhesion to laminin via BCAM/LU.

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عنوان ژورنال:
  • The Journal of clinical investigation

دوره 101 11  شماره 

صفحات  -

تاریخ انتشار 1998