Platelet basic protein (PPBP)

The protein contains 128 amino acids for an estimated molecular weight of 13894 Da.

 

LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 66%
Model score: 0
No model available.

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No binding partner found

The reference OMIM entry for this protein is 121010

Pro-platelet basic protein; ppbp
Cxc chemokine ligand 7; cxcl7
Small inducible cytokine subfamily b, member 7; scyb7 platelet basic protein, included; pbp, included
Connective tissue-activating peptide iii, included; ctap3, included
Beta-thro

DESCRIPTION

Pro-platelet basic protein (PPBP) is the precursor of the 2 platelet alpha-granule proteins, platelet basic protein (PBP) and connective tissue-activating peptide III (CTAP3). Upon platelet activation they are released and further processed in plasma to beta-thromboglobulin (TGB) and neutrophil-activating peptide-2 (NAP2).

CLONING

By purifying proteins with antibacterial activity from platelet granules, followed by cation exchange chromatography, continuous acid urea polyacrylamide gel electrophoresis, mass spectrometry, and N-terminal sequencing, Krijgsveld et al. (2000) identified the thrombocidins, TC1 and TC2, as variants of the NAP2 and CTAP3 forms of PPBP, respectively. TC1 and TC2 differ from NAP2 and CTAP3 by a C-terminal truncation of 2 amino acids (ala and asp) and by their bactericidal and fungicidal properties, which apparently do not involve pore formation.

GENE FUNCTION

CTAP3 is a platelet-derived growth factor that stimulates a variety of specific metabolic and cellular activities including mitogenesis, extracellular matrix synthesis, glucose metabolism, and plasminogen activator synthesis in human fibroblast cultures (Castor et al., 1983; Castor et al., 1985). Using mass spectrometry, Aivado et al. (2007) generated serum proteome profiles from 122 patients with myelodysplastic syndrome (MDS), 72 non-MDS patients with cytopenia, and 24 controls, and identified a profile that distinguished MDS from non-MDS cytopenias. Peptide mass fingerprinting and quadrupole SELDI-TOF mass spectrometry identified 2 differential proteins, CXCL4 (PF4) and CXCL7, both of which had significantly decreased serum levels in MDS. The decrease was confirmed with independent antibody assays, and subtype analyses revealed decreased serum levels of these 2 proteins in advanced MDS. Aivado et al. (2007) suggested that there may be a concerted disturbance of transcription or translation of these chemokines in advanced MDS.

GENE STRUCTURE

Majumdar et al. (1991) compared beta-thromboglobulin with platelet factor-4 (PF4; 173460). The TGB gene is 1,139 bp long and, like other members of the small inducible gene (SIG) family, it is divided into 3 exons.

MAPPING

By PCR analysis of human/hamster somatic cell hybrids, Majumdar et al. (1991) demonstrated that the TGB gene, like the PF4 gene, is located on chromosome 4. Southern blot analysis of genomic DNA suggested that, as with the PF4 gene, there are multiple copies of the TGB gene in the human genome. Wenger et al. (1991) mapped the CTAP3 gene to chromosome 4q12-q13 by in situ hybridization. Tunnacliffe et al. (1992) stated that all of the CXC SIGs map to chromosome 4. By pulsed field gel electrophoresis (PFGE), Tunnacliffe et al. (1992) demonstrated that the TGB genes (which are duplicate) are closely linked to the duplicated PF4 genes and to other previously mapped CXC SIGs, namely, IL8 (146930), GRO1 (155730), GRO2 (139110), and GRO3 (139111), on a single 700-kb restriction fragment located in bands 4q12-q13. The only CXC SIG not linked to this cluster is that encoding gamma-interferon-induced 10-kD protein (SCYB10; 147310), which is located in band 4q21. By analysis of lambda genomic clones, Tunnacliffe et al. (1992) demonstrated that the TGB1 and PF4 genes are separated by less than 7 kb, and the TGB2 and PF4-alternate (PF4V1; 173461) genes by approximately 5 kb. Within each TGB/PF4 duplication, the TGB-like gene is upstream of its lin ... More on the omim web site

Subscribe to this protein entry history

Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 121010 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).