Dipeptidyl peptidase-4

Dipeptidyl-peptidase 4 (CD26, adenosine deaminase complexing protein 2)
Ribbon diagram of human DPP-4. From PDB 1PFQ.
Available structures: 1j2e, 1n1m, 1nu6, 1nu8, 1pfq, 1r9m, 1r9n, 1rwq, 1tk3, 1tkr, 1u8e, 1w1i, 1wcy, 1x70, 2ajl, 2bgn, 2bgr, 2bub, 2fjp, 2g5p, 2g5t, 2g63, 2hha, 2i03, 2iit, 2iiv, 2ogz, 2oph, 2oqi, 2oqv, 2p8s
Identifiers
Symbol(s)	DPP4; ADABP; ADCP2; CD26; DPPIV; TP103
External IDs	OMIM: 102720 MGI: 94919 Homologene: 3279
Gene ontology Molecular Function: • aminopeptidase activity • dipeptidyl-peptidase IV activity • prolyl oligopeptidase activity Cellular Component: • membrane • integral to membrane • intercellular canaliculus Biological Process: • proteolysis • immune response
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	1803	13482
Ensembl	ENSG00000197635	ENSMUSG00000035000
Uniprot	P27487	Q3TR43
Refseq	NM_001935 (mRNA) NP_001926 (protein)	NM_010074 (mRNA) NP_034204 (protein)
Location	Chr 2: 162.56 - 162.64 Mb	Chr 2: 62.13 - 62.21 Mb
Pubmed search	[1]	[2]

The enzyme DPP-4 also part of the CD26 surface region is associated with immune regulation, signal transduction and apoptosis. It is a rather indiscriminate enzyme for which at least 62 substrates are known. Furthermore it appears to work as a suppressor in the development of cancer and tumours. Dipeptidyl peptidase-4 plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1. DPP-4 also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.

Clinical significance

A new class of oral hypoglycemics called dipeptidyl peptidase-4 inhibitors work by inhibiting the action of this enzyme, thereby prolonging incretin effect in vivo.

External links

• MeSH Dipeptidyl-Peptidase+IV
• Banting and Best Diabetes Centre at UT dp_iv

Further reading

• Ansorge S, Bühling F, Kähne T, et al. (1997). "CD26/dipeptidyl peptidase IV in lymphocyte growth regulation.". Adv. Exp. Med. Biol. 421: 127-40. PMID 9330689.
• Reinhold D, Kähne T, Steinbrecher A, et al. (2003). "The role of dipeptidyl peptidase IV (DP IV) enzymatic activity in T cell activation and autoimmunity.". Biol. Chem. 383 (7-8): 1133-8. PMID 12437097.
• Sato K, Dang NH (2003). "CD26: a novel treatment target for T-cell lymphoid malignancies? (Review).". Int. J. Oncol. 22 (3): 481-97. PMID 12579300.
• de Meester I, Lambeir AM, Proost P, Scharpé S (2003). "Dipeptidyl peptidase IV substrates. An update on in vitro peptide hydrolysis by human DPPIV.". Adv. Exp. Med. Biol. 524: 3-17. PMID 12675218.
• Koch S, Anthonsen D, Skovbjerg H, Sjöström H (2003). "On the role of dipeptidyl peptidase IV in the digestion of an immunodominant epitope in celiac disease.". Adv. Exp. Med. Biol. 524: 181-7. PMID 12675238.
• Pro B, Dang NH (2005). "CD26/dipeptidyl peptidase IV and its role in cancer.". Histol. Histopathol. 19 (4): 1345-51. PMID 15375776.

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