CXCL7

Pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)
PDB rendering based on 1f9p.
Available structures PDB 1F9P, 1NAP, 1TVX
Identifiers
Symbols	PPBP; B-TG1; Beta-TG; CTAP-III; CTAP3; CTAPIII; CXCL7; LA-PF4; LDGF; MDGF; NAP-2; PBP; SCAR10; SCYB7; TC1; TC2; TGB; TGB1; THBGB; THBGB1
External IDs	OMIM: 121010 MGI: 1888712 HomoloGene: 48122 GeneCards: PPBP Gene
Gene Ontology Molecular function • glucose transmembrane transporter activity • chemokine activity • growth factor activity Cellular component • extracellular region • extracellular region • extracellular space • platelet alpha granule lumen Biological process • platelet degranulation • chemotaxis • immune response • blood coagulation • glucose transport • platelet activation • defense response to bacterium • positive regulation of cell division Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5473	57349
Ensembl	ENSG00000163736	ENSMUSG00000029372
UniProt	P02775	n/a
RefSeq (mRNA)	NM_002704.3	NM_023785.2
RefSeq (protein)	NP_002695.1	NP_076274.1
Location (UCSC)	Chr 4: 74.85 – 74.85 Mb	Chr 5: 91.2 – 91.2 Mb
PubMed search	[1]	[2]

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]

References

1. ^ "Entrez Gene: PPBP pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5473. 
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. doi:10.1161/01.RES.0000259043.42571.68. PMID 17272812. 
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. PMID 1826003. 
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. doi:10.1073/pnas.80.3.765. PMC 393460. PMID 6572368. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=393460. 
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. doi:10.1021/bi00328a029. PMID 4005226. 

Further reading

• Begg GS, Pepper DS, Chesterman CN, Morgan FJ (1978). "Complete covalent structure of human beta-thromboglobulin.". Biochemistry 17 (9): 1739–44. doi:10.1021/bi00602a024. PMID 77677. 
• Kaplan KL, Broekman MJ, Chernoff A, et al. (1979). "Platelet alpha-granule proteins: studies on release and subcellular localization.". Blood 53 (4): 604–18. PMID 426909. 
• 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. PMID 1316786. 
• 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. PMID 1387511. 
• 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. doi:10.1016/S0888-7543(05)80169-7. PMID 1427896. 
• 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. PMID 1826003. 
• 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. doi:10.1007/BF00200921. PMID 1830861. 
• Hjemdahl P, Perneby C, Theodorsson E, et al. (1992). "A new assay for beta-thromboglobulin in urine.". Thromb. Res. 64 (1): 33–43. doi:10.1016/0049-3848(91)90203-9. PMID 1837963. 
• 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. doi:10.1016/1043-4666(91)90499-4. PMID 1873479. 
• 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. doi:10.1021/bi00226a021. PMID 2007144. 
• 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. doi:10.1084/jem.171.2.449. PMC 2187709. PMID 2406364. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2187709. 
• 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. doi:10.1021/bi00356a023. PMID 2423119. 
• 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. doi:10.1016/0006-291X(89)92203-1. PMID 2522778. 
• 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. PMID 2713489. 
• 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. doi:10.1016/0006-291X(89)92330-9. PMID 2783111. 
• 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. PMID 2966071. 
• 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. doi:10.1021/bi00328a029. PMID 4005226. 
• 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. doi:10.1136/jcp.35.11.1227. PMC 497932. PMID 6183294. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=497932. 
• 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. doi:10.1073/pnas.80.3.765. PMC 393460. PMID 6572368. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=393460. 
• 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. doi:10.1074/jbc.270.13.7077. PMID 7706245.