@article{RN222,
   author = {Welsh, J. D. and Charonko, J. J. and Salmanzadeh, A. and Drahos, K. E. and Shafiee, H. and Stremler, M. A. and Davalos, R. V. and Capelluto, D. G. and Vlachos, P. P. and Finkielstein, C. V.},
   title = {Disabled-2 modulates homotypic and heterotypic platelet interactions by binding to sulfatides},
   journal = {Br J Haematol},
   volume = {154},
   number = {1},
   pages = {122-33},
   note = {1365-2141
Welsh, John D
Charonko, John J
Salmanzadeh, Alireza
Drahos, Karen E
Shafiee, Hadi
Stremler, Mark A
Davalos, Rafael V
Capelluto, Daniel G S
Vlachos, Pavlos P
Finkielstein, Carla V
Journal Article
England
2011/05/05
Br J Haematol. 2011 Jul;154(1):122-33. doi: 10.1111/j.1365-2141.2011.08705.x. Epub 2011 May 3.},
   abstract = {Disabled-2 (Dab2) inhibits platelet aggregation by competing with fibrinogen for binding to the α(IIb) β(3) integrin receptor, an interaction that is modulated by Dab2 binding to sulfatides at the outer leaflet of the platelet plasma membrane. The disaggregatory function of Dab2 has been mapped to its N-terminus phosphotyrosine-binding (N-PTB) domain. Our data show that the surface levels of P-selectin, a platelet transmembrane protein known to bind sulfatides and promote cell-cell interactions, are reduced by Dab2 N-PTB, an event that is reversed in the presence of a mutant form of the protein that is deficient in sulfatide but not in integrin binding. Importantly, Dab2 N-PTB, but not its sulfatide binding-deficient form, was able to prevent sulfatide-induced platelet aggregation when tested under haemodynamic conditions in microfluidic devices at flow rates with shear stress levels corresponding to those found in vein microcirculation. Moreover, the regulatory role of Dab2 N-PTB extends to platelet-leucocyte adhesion and aggregation events, suggesting a multi-target role for Dab2 in haemostasis.},
   keywords = {Adaptor Proteins, Signal Transducing/metabolism/*pharmacology
Apoptosis Regulatory Proteins
Cell Communication/drug effects/physiology
Hemorheology
Humans
Leukocytes/physiology
Microfluidic Analytical Techniques
P-Selectin/metabolism
Platelet Activation/physiology
Platelet Adhesiveness/drug effects/physiology
Platelet Aggregation/*drug effects/physiology
Sulfoglycosphingolipids/*metabolism
Tumor Suppressor Proteins},
   ISSN = {0007-1048},
   DOI = {10.1111/j.1365-2141.2011.08705.x},
   year = {2011},
   type = {Journal Article}
}

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V."],"bibdata":{"bibtype":"article","type":"Journal Article","author":[{"propositions":[],"lastnames":["Welsh"],"firstnames":["J.","D."],"suffixes":[]},{"propositions":[],"lastnames":["Charonko"],"firstnames":["J.","J."],"suffixes":[]},{"propositions":[],"lastnames":["Salmanzadeh"],"firstnames":["A."],"suffixes":[]},{"propositions":[],"lastnames":["Drahos"],"firstnames":["K.","E."],"suffixes":[]},{"propositions":[],"lastnames":["Shafiee"],"firstnames":["H."],"suffixes":[]},{"propositions":[],"lastnames":["Stremler"],"firstnames":["M.","A."],"suffixes":[]},{"propositions":[],"lastnames":["Davalos"],"firstnames":["R.","V."],"suffixes":[]},{"propositions":[],"lastnames":["Capelluto"],"firstnames":["D.","G."],"suffixes":[]},{"propositions":[],"lastnames":["Vlachos"],"firstnames":["P.","P."],"suffixes":[]},{"propositions":[],"lastnames":["Finkielstein"],"firstnames":["C.","V."],"suffixes":[]}],"title":"Disabled-2 modulates homotypic and heterotypic platelet interactions by binding to sulfatides","journal":"Br J Haematol","volume":"154","number":"1","pages":"122-33","note":"1365-2141 Welsh, John D Charonko, John J Salmanzadeh, Alireza Drahos, Karen E Shafiee, Hadi Stremler, Mark A Davalos, Rafael V Capelluto, Daniel G S Vlachos, Pavlos P Finkielstein, Carla V Journal Article England 2011/05/05 Br J Haematol. 2011 Jul;154(1):122-33. doi: 10.1111/j.1365-2141.2011.08705.x. Epub 2011 May 3.","abstract":"Disabled-2 (Dab2) inhibits platelet aggregation by competing with fibrinogen for binding to the α(IIb) β(3) integrin receptor, an interaction that is modulated by Dab2 binding to sulfatides at the outer leaflet of the platelet plasma membrane. The disaggregatory function of Dab2 has been mapped to its N-terminus phosphotyrosine-binding (N-PTB) domain. Our data show that the surface levels of P-selectin, a platelet transmembrane protein known to bind sulfatides and promote cell-cell interactions, are reduced by Dab2 N-PTB, an event that is reversed in the presence of a mutant form of the protein that is deficient in sulfatide but not in integrin binding. Importantly, Dab2 N-PTB, but not its sulfatide binding-deficient form, was able to prevent sulfatide-induced platelet aggregation when tested under haemodynamic conditions in microfluidic devices at flow rates with shear stress levels corresponding to those found in vein microcirculation. Moreover, the regulatory role of Dab2 N-PTB extends to platelet-leucocyte adhesion and aggregation events, suggesting a multi-target role for Dab2 in haemostasis.","keywords":"Adaptor Proteins, Signal Transducing/metabolism/*pharmacology Apoptosis Regulatory Proteins Cell Communication/drug effects/physiology Hemorheology Humans Leukocytes/physiology Microfluidic Analytical Techniques P-Selectin/metabolism Platelet Activation/physiology Platelet Adhesiveness/drug effects/physiology Platelet Aggregation/*drug effects/physiology Sulfoglycosphingolipids/*metabolism Tumor Suppressor Proteins","issn":"0007-1048","doi":"10.1111/j.1365-2141.2011.08705.x","year":"2011","bibtex":"@article{RN222,\n author = {Welsh, J. D. and Charonko, J. J. and Salmanzadeh, A. and Drahos, K. E. and Shafiee, H. and Stremler, M. A. and Davalos, R. V. and Capelluto, D. G. and Vlachos, P. P. and Finkielstein, C. V.},\n title = {Disabled-2 modulates homotypic and heterotypic platelet interactions by binding to sulfatides},\n journal = {Br J Haematol},\n volume = {154},\n number = {1},\n pages = {122-33},\n note = {1365-2141\nWelsh, John D\nCharonko, John J\nSalmanzadeh, Alireza\nDrahos, Karen E\nShafiee, Hadi\nStremler, Mark A\nDavalos, Rafael V\nCapelluto, Daniel G S\nVlachos, Pavlos P\nFinkielstein, Carla V\nJournal Article\nEngland\n2011/05/05\nBr J Haematol. 2011 Jul;154(1):122-33. doi: 10.1111/j.1365-2141.2011.08705.x. Epub 2011 May 3.},\n abstract = {Disabled-2 (Dab2) inhibits platelet aggregation by competing with fibrinogen for binding to the α(IIb) β(3) integrin receptor, an interaction that is modulated by Dab2 binding to sulfatides at the outer leaflet of the platelet plasma membrane. The disaggregatory function of Dab2 has been mapped to its N-terminus phosphotyrosine-binding (N-PTB) domain. Our data show that the surface levels of P-selectin, a platelet transmembrane protein known to bind sulfatides and promote cell-cell interactions, are reduced by Dab2 N-PTB, an event that is reversed in the presence of a mutant form of the protein that is deficient in sulfatide but not in integrin binding. Importantly, Dab2 N-PTB, but not its sulfatide binding-deficient form, was able to prevent sulfatide-induced platelet aggregation when tested under haemodynamic conditions in microfluidic devices at flow rates with shear stress levels corresponding to those found in vein microcirculation. Moreover, the regulatory role of Dab2 N-PTB extends to platelet-leucocyte adhesion and aggregation events, suggesting a multi-target role for Dab2 in haemostasis.},\n keywords = {Adaptor Proteins, Signal Transducing/metabolism/*pharmacology\nApoptosis Regulatory Proteins\nCell Communication/drug effects/physiology\nHemorheology\nHumans\nLeukocytes/physiology\nMicrofluidic Analytical Techniques\nP-Selectin/metabolism\nPlatelet Activation/physiology\nPlatelet Adhesiveness/drug effects/physiology\nPlatelet Aggregation/*drug effects/physiology\nSulfoglycosphingolipids/*metabolism\nTumor Suppressor Proteins},\n ISSN = {0007-1048},\n DOI = {10.1111/j.1365-2141.2011.08705.x},\n year = {2011},\n type = {Journal Article}\n}\n\n","author_short":["Welsh, J. D.","Charonko, J. J.","Salmanzadeh, A.","Drahos, K. E.","Shafiee, H.","Stremler, M. A.","Davalos, R. V.","Capelluto, D. G.","Vlachos, P. P.","Finkielstein, C. 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