DPP3

DPP3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3FVY, 3T6B, 3T6J, 5E2Q, 5EHH, 5E33, 5E3C, 5E3A, 5EGY
Identifiers
Aliases	DPP3 , DPPIII, dipeptidyl peptidase 3
External IDs	OMIM: 606818 MGI: 1922471 HomoloGene: 40210 GeneCards: DPP3
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q13.2 Start 66,480,013 bp [1] End 66,509,657 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19|19 A Start 4,957,257 bp [2] End 4,978,315 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte rectum islet of Langerhans secondary oocyte stromal cell of endometrium right adrenal gland gallbladder monocyte body of stomach gastrocnemius muscle Top expressed in yolk sac lip primitive streak esophagus neural tube lacrimal gland seminal vesicula renal corpuscle proximal tubule spermatocyte More reference expression data BioGPS n/a
Gene ontology Molecular function zinc ion binding peptidase activity aminopeptidase activity protein binding hydrolase activity metallopeptidase activity dipeptidyl-peptidase activity metal ion binding Cellular component plasma membrane extracellular exosome cytoplasm nuclear speck cytosol Biological process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10072 75221 Ensembl ENSG00000254986 ENSMUSG00000063904 UniProt Q9NY33 Q99KK7 RefSeq (mRNA) NM_130443 NM_001256670 NM_005700 NM_133803 NM_001360711 RefSeq (protein) NP_001243599 NP_005691 NP_569710 NP_598564 NP_001347640 Location (UCSC) Chr 11: 66.48 – 66.51 Mb Chr 19: 4.96 – 4.98 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene. ^{[5] [6]}

This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized. ^[7]

Dipeptidyl-peptidase 3 has been found to act as a myocardial depressant factor. Procizumab, a specific antibody for dipeptidyl-peptidase 3, was found to improve cardiac and renal function in a mouse model of heart failure. ^[8] In human studies, higher levels of circulating DPP3 protein in cardiogenic shock patients indicated a more severe disease course, with a higher risk of refractory cardiogenic shock and death. ^{[9] [10]}

References

1. GRCh38: Ensembl release 89: ENSG00000254986 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000063904 – 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. Fukasawa KM, Fukasawa K, Harada M (Jun 2000). "Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12→q13.1 by in situ hybridization". Cytogenet Cell Genet. 88 (1–2): 99–100. doi:10.1159/000015498. PMID   10773679. S2CID   202603.
6. "DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-05-16.
7. "DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-05-16.
8. Deniau, Benjamin; Rehfeld, Linda; Santos, Karine; Dienelt, Anke; Azibani, Feriel; Sadoune, Malha; Kounde, Paul R.; Samuel, Jane L.; Tolpannen, Heli; Lassus, Johan; Harjola, Veli-Pekka; Vodovar, Nicolas; Bergmann, Andreas; Hartmann, Oliver; Mebazaa, Alexandre (February 2020). "Circulating dipeptidyl peptidase 3 is a myocardial depressant factor: dipeptidyl peptidase 3 inhibition rapidly and sustainably improves haemodynamics". European Journal of Heart Failure. 22 (2): 290–299. doi:10.1002/ejhf.1601. ISSN   1388-9842. PMID   31472040.
9. Harjola, Veli-Pekka; Lassus, Johan; Sionis, Alessandro; Køber, Lars; Tarvasmäki, Tuukka; Spinar, Jindrich; Parissis, John; Banaszewski, Marek; Silva-Cardoso, Jose; Carubelli, Valentina; Di Somma, Salvatore; Tolppanen, Heli; Zeymer, Uwe; Thiele, Holger; Nieminen, Markku S (May 2015). "Clinical picture and risk prediction of short-term mortality in cardiogenic shock". European Journal of Heart Failure. 17 (5): 501–509. doi:10.1002/ejhf.260. hdl: 11573/910722 . ISSN   1388-9842. PMID   25820680.
10. Takagi, Koji; Blet, Alice; Levy, Bruno; Deniau, Benjamin; Azibani, Feriel; Feliot, Elodie; Bergmann, Andreas; Santos, Karine; Hartmann, Oliver; Gayat, Etienne; Mebazaa, Alexandre; Kimmoun, Antoine (February 2020). "Circulating dipeptidyl peptidase 3 and alteration in haemodynamics in cardiogenic shock: results from the OptimaCC trial". European Journal of Heart Failure. 22 (2): 279–286. doi:10.1002/ejhf.1600. ISSN   1388-9842. PMID   31472039.

Further reading

• Kar NC, Pearson CM (1978). "Dipeptidyl peptidases in human muscle disease". Clin. Chim. Acta. 82 (1–2): 185–92. doi:10.1016/0009-8981(78)90042-6. PMID   618680.
• Grdisa M, Vitale L (1991). "Types and localization of aminopeptidases in different human blood cells". Int. J. Biochem. 23 (3): 339–45. doi:10.1016/0020-711X(91)90116-5. PMID   2044841.
• Swanson AA, Davis RM, Meinhardt NC (1985). "Proteases in human lenses and their possible significance". Curr. Eye Res. 4 (1): 43–8. doi:10.3109/02713688508999965. PMID   2858361.
• Vanha-Perttula T (1989). "Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties". Clin. Chim. Acta. 177 (2): 179–95. doi:10.1016/0009-8981(88)90140-4. PMID   2906822.
• Shimamori Y, Watanabe Y, Fujimoto Y (1989). "Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion". Biochem. Med. Metab. Biol. 40 (3): 305–10. doi:10.1016/0885-4505(88)90133-8. PMID   3233187.
• Abramić M, Zubanović M, Vitale L (1988). "Dipeptidyl peptidase III from human erythrocytes". Biol. Chem. Hoppe-Seyler. 369 (1): 29–38. doi:10.1515/bchm3.1988.369.1.29. PMID   3348886.
• Shimamori Y, Watanabe Y, Fujimoto Y (1987). "Purification and characterization of dipeptidyl aminopeptidase III from human placenta". Chem. Pharm. Bull. 34 (8): 3333–40. doi: 10.1248/cpb.34.3333 . PMID   3791505.
• Swanson AA, Davis RM, McDonald JK (1984). "Dipeptidyl peptidase III of human cataractous lenses. Partial purification". Curr. Eye Res. 3 (2): 287–91. doi:10.3109/02713688408997211. PMID   6368131.
• Jones TH, Kapralou A (1982). "A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes". Anal. Biochem. 119 (2): 418–23. doi:10.1016/0003-2697(82)90607-8. PMID   7041700.
• Vitale L, Zubanović M, Abramić M (1982). "Properties and distribution of aminopeptidase and dipeptidyl aminopeptidase III of human erythrocytes". Acta Biol. Med. Ger. 40 (10–11): 1489–95. PMID   7044004.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Fukasawa K, Fukasawa KM, Kanai M, et al. (1998). "Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression". Biochem. J. 329 ( Pt 2) (Pt 2): 275–82. doi:10.1042/bj3290275. PMC   1219041 . PMID   9425109.
• Simaga S, Babić D, Osmak M, et al. (1998). "Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue". Eur. J. Cancer. 34 (3): 399–405. doi:10.1016/S0959-8049(97)00401-2. PMID   9640230.
• Akiyama T, Harada S, Kojima F, et al. (1998). "Fluostatins A and B, new inhibitors of dipeptidyl peptidase III, produced by Streptomyces sp. TA-3391. I. Taxonomy of producing strain, production, isolation, physico-chemical properties and biological properties". J. Antibiot. 51 (6): 553–9. doi: 10.7164/antibiotics.51.553 . PMID   9711218.
• Fukasawa K, Fukasawa KM, Iwamoto H, et al. (1999). "The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme". Biochemistry. 38 (26): 8299–303. doi:10.1021/bi9904959. PMID   10387075.
• Hashimoto J, Yamamoto Y, Kurosawa H, et al. (2000). "Identification of dipeptidyl peptidase III in human neutrophils". Biochem. Biophys. Res. Commun. 273 (2): 393–7. doi:10.1006/bbrc.2000.2827. PMID   10873616.
• Abramić M, Schleuder D, Dolovcak L, et al. (2001). "Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences". Biol. Chem. 381 (12): 1233–43. doi:10.1515/BC.2000.151. PMID   11209758. S2CID   22245963.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.

External links

• DPP3 human gene location in the UCSC Genome Browser .
• DPP3 human gene details in the UCSC Genome Browser .