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Title: Cxcl7  
Author: World Heritage Encyclopedia
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Subject: Outline of immunology, Beta-thromboglobulin, Chromosome 4 (human), Immunotherapy, Cytokines
Publisher: World Heritage Encyclopedia


Pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)
PDB rendering based on 1f9p.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Chemokine (C-X-C motif) ligand 7 (CXCL7) is a human gene.[1]

The encoded protein, Chemokine (C-X-C motif) ligand is a small cytokine belonging to the CXC chemokine family. It is an isoform of Beta-Thromboglobulin or Pro-Platelet basic protein (PPBP).[2]

It is a protein that is released in large amounts from platelets following their activation.[3] It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.[4][5]


  1. ^ "Entrez Gene: PPBP pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)". 
  2. ^ Hristov M, Zernecke A, Bidzhekov K; et al. (March 2007). "Importance of CXC chemokine receptor 2 in the homing of human peripheral blood endothelial progenitor cells to sites of arterial injury". Circ. Res. 100 (4): 590–7.  
  3. ^ Majumdar S, Gonder D, Koutsis B, Poncz M (1991). "Characterization of the human beta-thromboglobulin gene. Comparison with the gene for platelet factor 4". J Biol Chem 266 (9): 5785–9.  
  4. ^ Castor C, Miller J, Walz D (1983). "Structural and biological characteristics of connective tissue activating peptide (CTAP-III), a major human platelet-derived growth factor". Proc Natl Acad Sci USA 80 (3): 765–9.  
  5. ^ Castor C, Furlong A, Carter-Su C (1985). "Connective tissue activation: stimulation of glucose transport by connective tissue activating peptide III". Biochemistry 24 (7): 1762–7.  

Further reading

  • Begg GS, Pepper DS, Chesterman CN, Morgan FJ (1978). "Complete covalent structure of human beta-thromboglobulin.". Biochemistry 17 (9): 1739–44.  
  • Kaplan KL, Broekman MJ, Chernoff A; et al. (1979). "Platelet alpha-granule proteins: studies on release and subcellular localization.". Blood 53 (4): 604–18.  
  • Tunnacliffe A, Majumdar S, Yan B, Poncz M (1992). "Genes for beta-thromboglobulin and platelet factor 4 are closely linked and form part of a cluster of related genes on chromosome 4.". Blood 79 (11): 2896–900.  
  • Cohen AB, Stevens MD, Miller EJ; et al. (1992). "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets.". Am. J. Physiol. 263 (2 Pt 1): L249–56.  
  • Morris SW, Nelson N, Valentine MB; et al. (1992). "Assignment of the genes encoding human interleukin-8 receptor types 1 and 2 and an interleukin-8 receptor pseudogene to chromosome 2q35.". Genomics 14 (3): 685–91.  
  • Majumdar S, Gonder D, Koutsis B, Poncz M (1991). "Characterization of the human beta-thromboglobulin gene. Comparison with the gene for platelet factor 4.". J. Biol. Chem. 266 (9): 5785–9.  
  • Wenger RH, Hameister H, Clemetson KJ (1991). "Human platelet basic protein/connective tissue activating peptide-III maps in a gene cluster on chromosome 4q12-q13 along with other genes of the beta-thromboglobulin superfamily.". Hum. Genet. 87 (3): 367–8.  
  • Hjemdahl P, Perneby C, Theodorsson E; et al. (1992). "A new assay for beta-thromboglobulin in urine.". Thromb. Res. 64 (1): 33–43.  
  • Brandt E, Van Damme J, Flad HD (1991). "Neutrophils can generate their activator neutrophil-activating peptide 2 by proteolytic cleavage of platelet-derived connective tissue-activating peptide III.". Cytokine 3 (4): 311–21.  
  • Clark-Lewis I, Moser B, Walz A; et al. (1991). "Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide.". Biochemistry 30 (12): 3128–35.  
  • Walz A, Baggiolini M (1990). "Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases.". J. Exp. Med. 171 (2): 449–54.  
  • Holt JC, Harris ME, Holt AM; et al. (1986). "Characterization of human platelet basic protein, a precursor form of low-affinity platelet factor 4 and beta-thromboglobulin.". Biochemistry 25 (8): 1988–96.  
  • Walz A, Baggiolini M (1989). "A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils.". Biochem. Biophys. Res. Commun. 159 (3): 969–75.  
  • Wenger RH, Wicki AN, Walz A; et al. (1989). "Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library.". Blood 73 (6): 1498–503.  
  • Castor CW, Walz DA, Ragsdale CG; et al. (1989). "Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets.". Biochem. Biophys. Res. Commun. 163 (2): 1071–8.  
  • Holt JC, Rabellino EM, Gewirtz AM; et al. (1988). "Occurrence of platelet basic protein, a precursor of low affinity platelet factor 4 and beta-thromboglobulin, in human platelets and megakaryocytes.". Exp. Hematol. 16 (4): 302–6.  
  • Castor CW, Furlong AM, Carter-Su C (1985). "Connective tissue activation: stimulation of glucose transport by connective tissue activating peptide III.". Biochemistry 24 (7): 1762–7.  
  • McLaren KM, Pepper DS (1983). "Immunological localisation of beta-thromboglobulin and platelet factor 4 in human megakaryocytes and platelets.". J. Clin. Pathol. 35 (11): 1227–31.  
  • Castor CW, Miller JW, Walz DA (1983). "Structural and biological characteristics of connective tissue activating peptide (CTAP-III), a major human platelet-derived growth factor.". Proc. Natl. Acad. Sci. U.S.A. 80 (3): 765–9.  
  • Malkowski MG, Wu JY, Lazar JB; et al. (1995). "The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution.". J. Biol. Chem. 270 (13): 7077–87.  

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