Dipeptidyl peptidase-4: Difference between revisions

<languages />

<translate>

{{Short description|Mammalian protein found in humans}}

'''Dipeptidyl peptidase-4''' ('''DPP4''' or '''DPPIV'''), also known as '''adenosine deaminase complexing protein 2''' or '''CD26''' ([[cluster of differentiation]] 26) is a [[protein]] that, in humans, is encoded by the ''DPP4'' [[gene]]. DPP4 is related to [[FAP (gene)|FAP]], [[DPP8]], and [[DPP9]]. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner, and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV].

The protein encoded by the ''DPP4'' gene is an [[enzyme]] expressed on the surface of most cell types and is associated with immune regulation, [[signal transduction]], and [[apoptosis]]. It is a type II transmembrane [[glycoprotein]], but a soluble form, which lacks the intracellular and transmembrane part, is present in blood plasma and various body fluids. DPP-4 is a [[serine]] [[exopeptidase]] that cleaves X-proline or X-alanine [[dipeptide]]s from the [[N-terminus]] of [[polypeptide]]s. 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. 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 [[Substrate (biochemistry)|substrates]] including [[growth factor]]s, [[chemokine]]s, [[neuropeptide]]s, and [[vasoactive]] peptides. 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.

DPP4 plays a major role in [[glucose]] metabolism. It is responsible for the degradation of [[incretin]]s such as [[glucagon-like peptide-1|GLP-1]]. Furthermore, it appears to work as a suppressor in the development of some [[tumors]].

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

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 [[neoplasm]]s and decreased in others.

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

[[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.

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

*[[Development of dipeptidyl peptidase-4 inhibitors]]

*[[Berberine]]

{{refbegin | 2}}

* {{cite book | vauthors = Ansorge S, Bühling F, Kähne T, Lendeckel U, Reinhold D, Täger M, Wrenger S | title = Cellular Peptidases in Immune Functions and Diseases | chapter = CD26/Dipeptidyl Peptidase IV in Lymphocyte Growth Regulation | series = Advances in Experimental Medicine and Biology | volume = 421 | pages = 127–40 | year = 1997 | pmid = 9330689 | doi = 10.1007/978-1-4757-9613-1_17 | isbn = 978-1-4757-9615-5 }}

{{refend}}

* The [[:en:MEROPS|MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=S09.003 S09.003]

* {{MeshName|Dipeptidyl-Peptidase+IV}}

* {{UTGlucagon|dpp4}}

{{PDB Gallery|geneid=1803}}

{{Clusters of differentiation}}

{{Clusters of differentiation by lineage}}

{{Portal bar|Biology|border=no}}

{{二次利用|date= 8 March 2024}}

[[Category:EC 3.4.14]]

[[Category:Proteases]]

</translate>