Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin.

@article{Ushiyama1993StructuralAF,
  title={Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin.},
  author={S Ushiyama and Thomas M. Laue and Kevin Lawrence Moore and Harold P Erickson and Rodger P McEver},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 20},
  pages={15229-37}
}
P-selectin is an adhesion receptor for leukocytes on thrombin-activated platelets and endothelial cells. It contains a NH2-terminal carbohydrate-recognition domain, an epidermal growth factor motif, nine consensus repeats, a transmembrane domain, and a cytoplasmic tail. We expressed two soluble forms of P-selectin, one truncated after the ninth repeat (tPS) and the other lacking the transmembrane domain due to alternative RNA splicing (asPS). When visualized by electron microscopy, each was a… CONTINUE READING
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