scholarly journals Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP-ribosylation of small molecular weight GTP-binding protein, rho.

1993 ◽  
Vol 61 ◽  
pp. 157
Author(s):  
Tomoko Tominaga ◽  
Katsuji Sugie ◽  
Masakazu Hirata ◽  
Narito Morii ◽  
Shuh Narumiya
Keyword(s):  
Molecular Weight ◽  
Binding Protein ◽  
Small Molecular Weight ◽  
Gtp Binding Protein ◽  
Adp Ribosylation ◽  
Gtp Binding

BCL-2α encodes a novel small molecular weight GTP binding protein

1990 ◽  
Vol 30 ◽  
pp. 145-153 ◽  
Author(s):  
Subrata Haldar ◽  
Christine Beatty ◽  
Carlo M. Croce
Keyword(s):  
Molecular Weight ◽  
Binding Protein ◽  
Small Molecular Weight ◽  
Gtp Binding Protein ◽  
Gtp Binding

Distribution and Regulation of RAB3C, a Small Molecular Weight GTP-Binding Protein

1994 ◽  
Vol 200 (3) ◽  
pp. 1257-1263 ◽  
Author(s):  
Y.C. Su ◽  
L.S. Kao ◽  
Y.Y. Chu ◽  
Y. Liang ◽  
M.H. Tsai ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Binding Protein ◽  
Small Molecular Weight ◽  
Gtp Binding Protein ◽  
Gtp Binding

Rap1b Association with the Platelet Cytoskeleton Occurs in the Absence of Glycoproteins IIb/IIIa

1998 ◽  
Vol 79 (04) ◽  
pp. 832-836 ◽  
Author(s):  
Thomas Fischer ◽  
Christina Duffy ◽  
Gilbert White
Keyword(s):  
Molecular Weight ◽  
Divalent Cation ◽  
Binding Proteins ◽  
Binding Protein ◽  
Platelet Membrane ◽  
Low Molecular Weight ◽  
Membrane Glycoproteins ◽  
Gtp Binding Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding

SummaryPlatelet membrane glycoproteins (GP) IIb/IIIa and rap1b, a 21 kDa GTP binding protein, associate with the triton-insoluble, activation-dependent platelet cytoskeleton with similar rates and divalent cation requirement. To examine the possibility that GPIIb/IIIa was required for rap1b association with the cytoskeleton, experiments were performed to determine if the two proteins were linked under various conditions. Chromatography of lysates from resting platelets on Sephacryl S-300 showed that GPIIb/IIIa and rap1b were well separated and distinct proteins. Immunoprecipitation of GPIIb/IIIa from lysates of resting platelets did not produce rap1b or other low molecular weight GTP binding proteins and immunoprecipitation of rap1b from lysates of resting platelets did not produce GPIIb/IIIa. Finally, rap1b was associated with the activation-dependent cytoskeleton of platelets from a patient with Glanzmann’s thrombasthenia who lacks surface expressed glycoproteins IIb and IIIa. Based on these findings, we conclude that no association between GPIIb/IIIa and rap1b is found in resting platelets and that rap1b association with the activation-dependent cytoskeleton is at least partly independent of GPIIb/IIIa.

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