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Dipeptidyl peptidase-4 (DPP4), also known as adenosine deaminase complexing protein 2 (ADA) or CD26 (cluster of differentiation 26) is a protein which in humans is encoded by the DPP4 gene.[1]
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The protein encoded by the DPP4 gene is an antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides.
It is a rather indiscriminate enzyme for which at least 62 substrates are known.[2] The substrates of CD26/DPPIV are proline(or alanine)-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides.
DPP-4 plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1.[3]
Furthermore it appears to work as a suppressor in the development of cancer and tumours.[4][5][6]
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 being increased in some neoplasms and decreased in others.[7]
DPP-4 also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.
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.[8]
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