PF-4/CXCL4 and CXCL4L1 exhibit distinct subcellular localization and a differentially regulated mechanism of secretion.

@article{Lasagni2007PF4CXCL4AC,
  title={PF-4/CXCL4 and CXCL4L1 exhibit distinct subcellular localization and a differentially regulated mechanism of secretion.},
  author={Laura Lasagni and Renaud Gr{\'e}pin and Benedetta Mazzinghi and Elena Lazzeri and Claudia Meini and Costanza Sagrinati and F Leonarda Liotta and F. Frosali and Elisa Ronconi and Nathalie Alain-Courtois and Lara Ballerini and Giuseppe Stefano Netti and Enrico Maggi and Francesco Annunziato and Mario Serio and Sergio Romagnani and Andreas Bikfalvi and Paola Romagnani},
  journal={Blood},
  year={2007},
  volume={109 10},
  pages={4127-34}
}
PF-4/CXCL4 is a member of the CXC chemokine family, which is mainly produced by platelets and known for its pleiotropic biological functions. Recently, the proteic product of a nonallelic variant gene of CXCL4 was isolated from human platelets and named as CXCL4L1. CXCL4L1 shows only 4.3% amino acid divergence in the mature protein, but exhibits a 38% amino acid divergence in the signal peptide region. We hypothesized that this may imply a difference in the cell type in which CXCL4L1 is… CONTINUE READING
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