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edit 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; PBP; B-TG1; Beta-TG; CTAP-III; CTAP3; CTAPIII; CXCL7; LA-PF4; LDGF; MDGF; NAP-2; 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 space Biological process • regulation of progression through cell cycle • chemotaxis • immune response • cell proliferation • glucose transport • defense response to bacterium Sources: Amigo / EGO 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 NM_023785 RefSeq (protein) NP_002695 NP_076274 Location (UCSC) Chr 4: 75.07 - 75.07 Mb Chr 5: 91.84 - 91.85 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 ^ "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.  ^ 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.  ^ 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.  ^ 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. PMID 6572368.  ^ 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. PMID 2406364.  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. PMID 6183294.  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. PMID 6572368.  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.  v • d • e PDB Gallery 1f9p: CRYSTAL STRUCTURE OF CONNECTIVE TISSUE ACTIVATING PEPTIDE-III(CTAP-III) COMPLEXED WITH POLYVINYLSULFONIC ACID   1nap: THE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN NEUTROPHIL-ACTIVATING PEPTIDE-2 (M6L) AT 1.9-ANGSTROMS RESOLUTION   1tvx: NEUTROPHIL ACTIVATING PEPTIDE-2 VARIANT FORM M6L WITH FIVE ADDITIONAL AMINO TERMINAL RESIDUES (DSDLY)   This article on a gene on chromosome 4 is a stub. You can help Wikipedia by expanding it. v • d • e v • d • e Cell signaling: cytokines By family Interleukin IL-1 superfamily 1 (1Ra) · 18 · 33 IL-6 like/gp130 using 6  · 11 · 27 · 30 · 31 (+non IL Oncostatin M, Leukemia inhibitory factor, Ciliary neurotrophic factor, Cardiotrophin 1) IL-10 family 10 · 19 · 20 · 22 · 24 · 26 Interferon type III 28 · 29 Common γ-chain family 2/15 · 3 · 4 · 7 · 9 · 13 · 21 IL-12 family 12 · 23 · 27 · 35 Other 5 · 8 · 14 · 16 · 17/25 (A) · 32  · 34 Chemokine CCL 1 · 2 · 3 · 4 · 5 · 6 · 7 · 8 · 9 · 10 · 11 · 12 · 13 · 14 · 15 · 16 · 17 · 18 · 19 · 20 · 21 · 22 · 23 · 24 · 25 · 26 · 27 · 28 CXCL 1 · 2 · 3 · 4 · 5 · 6 · 7 · 8 · 9 · 10 · 11 · 12 · 13 · 14 · 15 · 16 · 17 CX3CL 1 XCL 1 · 2 TNF Main TNF-alpha TNF (ligand) superfamily 4-1BB ligand · B-cell activating factor · FAS ligand · Lymphotoxin · OX40L · RANKL · TRAIL Cluster of differentiation CD70 · CD153 · CD154 Interferon I alpha (Pegylated 2a, Pegylated 2b), beta (1a, 1b) II Gamma III IL-28 · IL-29 Other Monokine · Lymphokine (Lymphotoxin, Transfer factor) · Growth factor · Hematopoietic (Stem cell factor, Colony-stimulating factor) · Autocrine motility factor · Osteopontin By function proinflammatory cytokine (IL-1, TNF-alpha) · Th1 (interferon-gamma and tumor necrosis factor-beta) Th2 (interleukin 4, interleukin 5, interleukin 6, interleukin 10, interleukin 13)