Dipeptidyl peptidase-4
From Wikipedia, the free encyclopedia
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Dipeptidyl-peptidase 4 (CD26, adenosine deaminase complexing protein 2)
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| Ribbon diagram of human DPP-4. From PDB 1PFQ. |
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| 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 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| 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) |
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| 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. [1] Furthermore it appears to work as a suppressor in the development of cancer and tumours. [2] 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.
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[edit] 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.
[edit] References
- ^ Merck's March Madness - Forbes.com
- ^ Pro B, Dang N (2004). "CD26/dipeptidyl peptidase IV and its role in cancer". Histol Histopathol 19 (4): 1345–51. PMID 15375776.
Masur K et al. (2006). "DPPIV inhibitors extend GLP-2 mediated tumour promoting effects on intestinal cancer cells". Regul Pept. 137 (3): 147–55. doi:. PMID 16908079.
Wesley UV et al. (2005). "Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway". Cancer Res. 65 (4): 1325–34. doi:. PMID 15735018.
[edit] External links
[edit] 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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