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

DPP3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDPP3, DPPIII, dipeptidyl peptidase 3
External IDsOMIM: 606818; MGI: 1922471; HomoloGene: 40210; GeneCards: DPP3; OMA:DPP3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 MbChr 19: 4.96 – 4.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000254986Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000063904Ensembl, 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

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