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Platelet basic protein

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(Redirected from CXCL7)

PPBP
Identifiers
AliasesPPBP, B-TG1, Beta-TG, CTAP-III, CTAP3, CTAPIII, CXCL7, LA-PF4, LDGF, MDGF, NAP-2, PBP, SCYB7, TC1, TC2, TGB, TGB1, THBGB, THBGB1, pro-platelet basic protein
External IDsOMIM: 121010; MGI: 1888712; GeneCards: PPBP
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

5473

57349

Ensembl

ENSG00000163736

ENSMUSG00000029372

UniProt

P02775

Q9EQI5

RefSeq (mRNA)

NM_002704

NM_023785

RefSeq (protein)

NP_002695

NP_076274

Location (UCSC)Chr 4: 73.99 – 73.99 MbChr 5: 90.92 – 90.92 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Platelet basic protein (PBP) is a protein that in humans is encoded by the gene PPBP (previously CXCL7).[5] PBP is a precursor protein that is cleaved into multiple distinct active proteins, notable Connective tissue-activating peptide III (CTAP-III), Beta-thromboglobulin (Beta-TG), Neutrophil-activating peptide 2 (NAP-2), TC-1, and TC-2.[6][7] PPBP is first translated into the precursor molecule pro-platelet basic protein (PPBP), the first 34 amino acids of which correspond to the signal peptide, while the remaining amino acid residues at positions 35-128 compose PBP.[6]

PBP is a protein that is released in large amounts from platelets following their activation.[8] It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.[9][10]

Connective tissue-activating peptide III

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Connective tissue-activating peptide III (CTAP-III), also called Low-affinity platelet factor IV (LA-PF4), is a protein that corresponds to positions 44-128 of PPBP.[6] This protein has mitogenic effects: stimulating DNA synthesis and mitosis.[6] It also triggers prostaglandin E2 secretion and synthesis of hyaluronic acid and sulfated glycosaminoglycan.[6]

Neutrophil-activating peptide 2

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Neutrophil-activating peptide 2 (NAP-2) is a chemokine that corresponds to positions 59-128 of PPBP.[6] NAP-2 activates and attracts neutrophils through interaction with the receptors CXCR1 and CXCR2.[6] There are also shorter (and longer) versions of this peptide with similar effects, with NAP-2(1-63) (corresponding to positions 59-121 of PPBP) being the most potent.[6]

TC-1 and TC-2

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TC-1 and TC-2 are antimicrobial proteins corresponding to positions 59-126 and 44-126 of the PPBP protein respectively.[6]

β-Thromboglobulin

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β-Thromboglobulin (β-TG), or beta-thromboglobulin, is a protein that corresponds to positions 48-128 of PPBP.[6] It is secreted by platelets along with platelet factor 4 and platelet-derived growth factor, and forms a homodimer.[6][11][12][13] Along with platelet factor 4 (PF4), β-TG is one of the best-characterized platelet-specific proteins.[14] β-TG and PF4 are stored in platelet alpha granules and are released during platelet activation.[11][14][15] As a result, they are useful markers of platelet activation.[11][14] β-TG also has multiple biological activities, for instance being involved in maturation of megakaryocytes.[16]

Biological actions

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β-TG is a chemoattractant, strongly for fibroblasts and weakly for neutrophils. It is a stimulator of mitogenesis, extracellular matrix synthesis, glucose metabolism, and plasminogen activator synthesis in human fibroblasts.[15]

β-TG also affects megakaryocyte maturation, and thus helps in regulating platelet production.[15]

Clinical uses

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Levels of β-TG is used to index platelet activation. It is measured by ELISA in blood plasma or urine, and often in conjunction with PF4.[15]

Influences

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β-TG levels may increase with age.[17] It is elevated in diabetes mellitus.[18]

β-TG levels have been found to be increased by treatment with the synthetic estrogen ethinylestradiol, though were not significantly increased by the natural estrogen estradiol valerate.[19][20][21][22] Levels of β-TG have also been found to be increased or unchanged during normal pregnancy.[23]

References

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  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000163736 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029372 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ "Entrez Gene: PPBP pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)".
  6. 1 2 3 4 5 6 7 8 9 10 11 "Platelet basic protein". UniProt consortium. Retrieved 2026-10-08.
  7. ↑ 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.
  8. ↑ 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. doi:10.1016/S0021-9258(19)67665-9. PMID 1826003.
  9. ↑ 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. Bibcode:1983PNAS...80..765C. doi:10.1073/pnas.80.3.765. PMC 393460. PMID 6572368.
  10. ↑ 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.
  11. 1 2 3 Sharma G, Berger JS (August 2011). "Platelet activity and cardiovascular risk in apparently healthy individuals: a review of the data". J Thromb Thrombolysis. 32 (2): 201–8. doi:10.1007/s11239-011-0590-9. PMID 21562837. S2CID 23686294.
  12. ↑ Kaplan KL, Owen J (February 1981). "Plasma levels of beta-thromboglobulin and platelet factor 4 as indices of platelet activation in vivo". Blood. 57 (2): 199–202. doi:10.1182/blood.V57.2.199.199. PMID 6160890.
  13. ↑ Pillai MM, Iwata M, Awaya N, Graf L, Torok-Storb B (May 2006). "Monocyte-derived CXCL7 peptides in the marrow microenvironment". Blood. 107 (9): 3520–6. doi:10.1182/blood-2005-10-4285. PMC 1895768. PMID 16391012.
  14. 1 2 3 Cella G, Scattolo N, Girolami A, Sasahara AA (1984). "Are platelet factor 4 and beta-thromboglobulin markers of cardiovascular disorders?". Ric Clin Lab. 14 (1) 9: 9–18. doi:10.1007/BF02905035. PMID 6203164. S2CID 58519828.
  15. 1 2 3 4 Cytokines & Cells Online Pathfinder Encyclopaedia → Beta-Thromboglobulin Retrieved on August 17, 2009
  16. ↑ Chung-Eun Ha, N. V. Bhagavan (24 April 2015). Essentials of Medical Biochemistry: With Clinical Cases (2 ed.). Academic Press. pp. 652–. ISBN 978-0-12-416697-4. OCLC 1006915388.
  17. ↑ Martinelli I, Bucciarelli P, Mannucci PM (February 2010). "Thrombotic risk factors: basic pathophysiology". Crit Care Med. 38 (2 Suppl): S3–9. doi:10.1097/CCM.0b013e3181c9cbd9. PMID 20083911. S2CID 34486553.
  18. ↑ Page 121 in: Sterne, Jonathan, Kirkwood, Betty R. (2003). Essential medical statistics. Oxford: Blackwell Science. ISBN 0-86542-871-9.
  19. ↑ Farris M, Bastianelli C, Rosato E, Brosens I, Benagiano G (October 2017). "Pharmacodynamics of combined estrogen-progestin oral contraceptives: 2. effects on hemostasis". Expert Rev Clin Pharmacol. 10 (10): 1129–1144. doi:10.1080/17512433.2017.1356718. PMID 28712325. S2CID 205931204.
  20. ↑ Kluft C, Lansink M (July 1997). "Effect of oral contraceptives on haemostasis variables". Thromb Haemost. 78 (1): 315–26. doi:10.1055/s-0038-1657546. PMID 9198173.
  21. ↑ Kuhl H (1998). "Adverse effects of estrogen treatment: natural vs. synthetic estrogens". In Lippert TH, Mueck AO, Ginsburg J (eds.). Sex Steroids and the Cardiovascular System: The Proceedings of the 1st Interdisciplinary Workshop, Tuebingen, Germany, October 1996. London/New York: Parthenon. pp. 201–210. ISBN 9781850709565.
  22. ↑ Lindberg UB, Crona N, Stigendal L, Teger-Nilsson AC, Silfverstolpe G (February 1989). "A comparison between effects of estradiol valerate and low dose ethinyl estradiol on haemostasis parameters". Thromb Haemost. 61 (1): 65–9. doi:10.1055/s-0038-1646528. PMID 2526387.
  23. ↑ Hellgren M (April 2003). "Hemostasis during normal pregnancy and puerperium". Semin Thromb Hemost. 29 (2): 125–30. doi:10.1055/s-2003-38897. PMID 12709915.

Further reading

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