Dipeptidyl peptidase-4

Source: Wikipedia, the free encyclopedia.
DPP4
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Ensembl
UniProt
RefSeq (mRNA)

NM_001935

NM_001159543
NM_010074

RefSeq (protein)

NP_001926
NP_001366533
NP_001366534
NP_001366535

NP_001153015
NP_034204

Location (UCSC)Chr 2: 161.99 – 162.07 MbChr 2: 62.16 – 62.24 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dipeptidyl peptidase-4 (DPP4 or DPPIV), also known as adenosine deaminase complexing protein 2 or CD26 (

FAP, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner,[6]
and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV].

Function

The protein encoded by the DPP4 gene is an

polypeptides. Peptide bonds involving the cyclic amino acid proline cannot be cleaved by the majority of proteases and an N-terminal X-proline "shields" various biopeptides.[7]
Extracellular proline-specific proteases therefore play an important role in the regulation of these biopeptides.

DPP-4 is known to cleave a broad range of

vasoactive peptides.[8][9] The cleaved substrates lose their biological activity in the majority of cases, but in the case of the chemokine RANTES and neuropeptide Y, DPP-4 mediated cleavage leads to a shift in the receptor subtype binding.[8]

DPP4 plays a major role in

DPP-4 also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.

Animal studies

Animal studies suggest its pathogenetic role in development of fibrosis of various organs, such as liver and kidney.[15][16]

Clinical significance

CD26/DPPIV plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others.[17]

A class of

dipeptidyl peptidase-4 inhibitors works by inhibiting the action of this enzyme, thereby prolonging incretin effect in vivo.[18]

Middle East respiratory syndrome coronavirus has been found to bind to DPP4. It is found on the surface of cells in the airways (such as the lungs) and kidneys. Scientists may be able to use this to their advantage by blocking the virus's entry into the cell.[19]

DPP4,[20] or its Mycobacterial homologue MtDPP,[21] might play a role in the pathogenesis of tuberculosis via cleavage of the chemokine C-X-C motif chemokine ligand 10 (CXCL10).

See also

  • Development of dipeptidyl peptidase-4 inhibitors
  • Berberine

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000197635 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035000 - 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. PMID 8101391
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  20. PMID 30026741
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Further reading

External links