Platelet factor 4

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Platelet factor 4 (chemokine (C-X-C motif) ligand 4)
PDB rendering based on 1f9q.
Available structures: 1f9q, 1f9r, 1f9s, 1pfm, 1pfn, 1rhp
Identifiers
Symbol(s) PF4; CXCL4; MGC138298; SCYB4
External IDs OMIM: 173460 MGI: 1888711 HomoloGene: 87791
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5196 56744
Ensembl ENSG00000163737 ENSMUSG00000029373
Uniprot P02776 Q3TVN6
Refseq NM_002619 (mRNA)
NP_002610 (protein)		 NM_019932 (mRNA)
NP_064316 (protein)
Location Chr 4: 75.07 - 75.07 Mb Chr 5: 91.85 - 91.85 Mb
Pubmed search [1] [2]

Platelet factor 4 (PF4) is a small cytokine belonging to the CXC chemokine family that is also known as chemokine (C-X-C motif) ligand 4 (CXCL4) . This chemokine is released from alpha-granules of activated platelets during platelet aggregation, and promotes blood coagulation by moderating the effects of heparin-like molecules. Due to these roles, it is predicted to play a role in wound repair and inflammation.[1] It is usually found in a complex with proteoglycan. PF4 is chemotactic for neutrophils, fibroblasts and monocytes, and interacts with a splice variant of the chemokine receptor CXCR3, known as CXCR3B.[2] The gene for human PF4 is located on human chromosome 4.[3]

Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair (Eisman et al., 1990).[supplied by OMIM][4]

Contents

[edit] References

  1. ^ Eisman R, Surrey S, Ramachandran B, Schwartz E, Poncz M (1990). "Structural and functional comparison of the genes for human platelet factor 4 and PF4alt". Blood 76 (2): 336–44. PMID 1695112. 
  2. ^ Lasagni L, Francalanci M, Annunziato F, Lazzeri E, Giannini S, Cosmi L, Sagrinati C, Mazzinghi B, Orlando C, Maggi E, Marra F, Romagnani S, Serio M, Romagnani P (2003). "An alternatively spliced variant of CXCR3 mediates the inhibition of endothelial cell growth induced by IP-10, Mig, and I-TAC, and acts as functional receptor for platelet factor 4". J Exp Med 197 (11): 1537–49. doi:10.1084/jem.20021897. PMID 12782716. 
  3. ^ O'Donovan N, Galvin M, Morgan J (1999). "Physical mapping of the CXC chemokine locus on human chromosome 4". Cytogenet Cell Genet 84 (1-2): 39–42. doi:10.1159/000015209. PMID 10343098. 
  4. ^ Entrez Gene: PF4 platelet factor 4 (chemokine (C-X-C motif) ligand 4).

[edit] Further reading

  • Bikfalvi A, Gimenez-Gallego G (2004). "The control of angiogenesis and tumor invasion by platelet factor-4 and platelet factor-4-derived molecules.". Semin. Thromb. Hemost. 30 (1): 137–44. doi:10.1055/s-2004-822978. PMID 15034805. 
  • Maurer AM, Zhou B, Han ZC (2007). "Roles of platelet factor 4 in hematopoiesis and angiogenesis.". Growth Factors 24 (4): 242–52. PMID 17381065. 
  • Deuel TF, Keim PS, Farmer M, Heinrikson RL (1977). "Amino acid sequence of human platelet factor 4.". Proc. Natl. Acad. Sci. U.S.A. 74 (6): 2256–8. PMID 267922. 
  • Walz DA, Wu VY, de Lamo R, et al. (1978). "Primary structure of human platelet factor 4.". Thromb. Res. 11 (6): 893–8. PMID 601757. 
  • Nath N, Lowery CT, Niewiarowski S (1975). "Antigenic and antiheparin properties of human platelet factor 4 (PF4).". Blood 45 (4): 537–50. PMID 803847. 
  • Hermodson M, Schmer G, Kurachi K (1977). "Isolation, crystallization, and primary amino acid sequence of human platelet factor 4.". J. Biol. Chem. 252 (18): 6276–9. PMID 893407. 
  • Maione TE, Gray GS, Petro J, et al. (1990). "Inhibition of angiogenesis by recombinant human platelet factor-4 and related peptides.". Science 247 (4938): 77–9. PMID 1688470. 
  • Eisman R, Surrey S, Ramachandran B, et al. (1990). "Structural and functional comparison of the genes for human platelet factor 4 and PF4alt.". Blood 76 (2): 336–44. PMID 1695112. 
  • Han ZC, Bellucci S, Tenza D, Caen JP (1990). "Negative regulation of human megakaryocytopoiesis by human platelet factor 4 and beta thromboglobulin: comparative analysis in bone marrow cultures from normal individuals and patients with essential thrombocythaemia and immune thrombocytopenic purpura.". Br. J. Haematol. 74 (4): 395–401. PMID 2140694. 
  • Poncz M, Surrey S, LaRocco P, et al. (1987). "Cloning and characterization of platelet factor 4 cDNA derived from a human erythroleukemic cell line.". Blood 69 (1): 219–23. PMID 3098319. 
  • Griffin CA, Emanuel BS, LaRocco P, et al. (1987). "Human platelet factor 4 gene is mapped to 4q12----q21.". Cytogenet. Cell Genet. 45 (2): 67–9. PMID 3622011. 
  • Senior RM, Griffin GL, Huang JS, et al. (1983). "Chemotactic activity of platelet alpha granule proteins for fibroblasts.". J. Cell Biol. 96 (2): 382–5. PMID 6187750. 
  • Morgan FJ, Begg GS, Chesterman CN (1980). "Complete covalent structure of human platelet factor 4.". Thromb. Haemost. 42 (5): 1652–60. PMID 6445090. 
  • Deuel TF, Senior RM, Chang D, et al. (1981). "Platelet factor 4 is chemotactic for neutrophils and monocytes.". Proc. Natl. Acad. Sci. U.S.A. 78 (7): 4584–7. PMID 6945600. 
  • Brown KJ, Parish CR (1994). "Histidine-rich glycoprotein and platelet factor 4 mask heparan sulfate proteoglycans recognized by acidic and basic fibroblast growth factor.". Biochemistry 33 (46): 13918–27. PMID 7524669. 
  • Mayo KH, Roongta V, Ilyina E, et al. (1995). "NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramer.". Biochemistry 34 (36): 11399–409. PMID 7547867. 
  • Barker S, Mayo KH (1995). "Quarternary structure amplification of protein folding differences observed in 'native' platelet factor-4.". FEBS Lett. 357 (3): 301–4. PMID 7835432. 
  • Zhang X, Chen L, Bancroft DP, et al. (1994). "Crystal structure of recombinant human platelet factor 4.". Biochemistry 33 (27): 8361–6. PMID 8031770. 
  • Horne MK (1993). "The effect of secreted heparin-binding proteins on heparin binding to platelets.". Thromb. Res. 70 (1): 91–8. PMID 8511754. 
  • Kolset SO, Mann DM, Uhlin-Hansen L, et al. (1996). "Serglycin-binding proteins in activated macrophages and platelets.". J. Leukoc. Biol. 59 (4): 545–54. PMID 8613703. 

[edit] See also

[edit] External links

v • d • e
Cytokines: chemokines
CCL
CXCL
CX3CL
XCL
v • d • e
Glycoproteins: proteoglycans
Aggrecan - Biglycan - Decorin - Platelet factor 4 - Syndecan 1 - Versican
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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