Dipeptidyl peptidase-4 - Revision history

Fire: Marked this version for translation

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Marked this version for translation

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	<languages />		<languages />
	<translate>		<translate>
			<!--T:1-->
	{{Short description\|Mammalian protein found in humans}}		{{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].		'''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].

	== Function ==		== Function == <!--T:2-->
	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.		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.

			<!--T:3-->
	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.		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.

			<!--T:4-->
	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]].		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]].

			<!--T:5-->
	DPP-4 also binds the enzyme [[adenosine deaminase]] specifically and with high affinity. The significance of this interaction has yet to be established.		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 == <!--T:6-->

			<!--T:7-->
	Animal studies suggest its pathogenetic role in development of [[fibrosis]] of various organs, such as liver and kidney.		Animal studies suggest its pathogenetic role in development of [[fibrosis]] of various organs, such as liver and kidney.

	== Clinical significance ==		== Clinical significance == <!--T:8-->

			<!--T:9-->
	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.		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.

			<!--T:10-->
	A class of [[oral hypoglycemics]] called [[dipeptidyl peptidase-4 inhibitors]] works by inhibiting the action of this enzyme, thereby prolonging [[incretin]] effect ''in vivo''.		A class of [[oral hypoglycemics]] called [[dipeptidyl peptidase-4 inhibitors]] works by inhibiting the action of this enzyme, thereby prolonging [[incretin]] effect ''in vivo''.

			<!--T:11-->
	[[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.		[[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.

			<!--T:12-->
	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]]).		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]]).

	== See also ==		== See also == <!--T:13-->
	*[[Development of dipeptidyl peptidase-4 inhibitors]]		*[[Development of dipeptidyl peptidase-4 inhibitors]]
	*[[Berberine]]		*[[Berberine]]

	== Further reading ==		== Further reading == <!--T:14-->
	{{refbegin \| 2}}		{{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 }}		* {{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 }}
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	{{refend}}		{{refend}}

	== External links ==		== External links == <!--T:15-->
	* 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]		* 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}}		* {{MeshName\|Dipeptidyl-Peptidase+IV}}
	* {{UTGlucagon\|dpp4}}		* {{UTGlucagon\|dpp4}}

			<!--T:16-->
	{{PDB Gallery\|geneid=1803}}		{{PDB Gallery\|geneid=1803}}

			<!--T:17-->
	{{Clusters of differentiation}}		{{Clusters of differentiation}}
	{{Clusters of differentiation by lineage}}		{{Clusters of differentiation by lineage}}
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	{{Portal bar\|Biology\|border=no}}		{{Portal bar\|Biology\|border=no}}

			<!--T:18-->
	{{二次利用\|date= 8 March 2024}}		{{二次利用\|date= 8 March 2024}}
	[[Category:EC 3.4.14]]		[[Category:EC 3.4.14]]
	[[Category:Proteases]]		[[Category:Proteases]]
	</translate>		</translate>

Fire at 13:43, 11 March 2024

2024-03-11T13:43:27Z

← Older revision		Revision as of 22:43, 11 March 2024
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			<languages />
			<translate>
	{{Short description\|Mammalian protein found in humans}}		{{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].		'''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].
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	[[Category:EC 3.4.14]]		[[Category:EC 3.4.14]]
	[[Category:Proteases]]		[[Category:Proteases]]
			</translate>

Fire: /* External links */

2024-03-11T13:41:14Z

External links

← Older revision		Revision as of 22:41, 11 March 2024
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	== External links ==		== External links ==
	* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=S09.003 S09.003]		* 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}}		* {{MeshName\|Dipeptidyl-Peptidase+IV}}
	* {{UTGlucagon\|dpp4}}		* {{UTGlucagon\|dpp4}}

Fire at 13:36, 11 March 2024

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	* {{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 }}		* {{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 }}
	* {{cite journal \| vauthors = Reinhold D, Kähne T, Steinbrecher A, Wrenger S, Neubert K, Ansorge S, Brocke S \| title = The role of dipeptidyl peptidase IV (DP IV) enzymatic activity in T cell activation and autoimmunity \| journal = Biological Chemistry \| volume = 383 \| issue = 7–8 \| pages = 1133–8 \| year = 2003 \| pmid = 12437097 \| doi = 10.1515/BC.2002.123 \| s2cid = 30027839 }}		* {{cite journal \| vauthors = Reinhold D, Kähne T, Steinbrecher A, Wrenger S, Neubert K, Ansorge S, Brocke S \| title = The role of dipeptidyl peptidase IV (DP IV) enzymatic activity in T cell activation and autoimmunity \| journal = Biological Chemistry \| volume = 383 \| issue = 7–8 \| pages = 1133–8 \| year = 2003 \| pmid = 12437097 \| doi = 10.1515/BC.2002.123 \| s2cid = 30027839 }}
	* {{cite journal \| vauthors = Sato K, Dang NH \| title = CD26: a novel treatment target for T-cell lymphoid malignancies? (Review) \| journal = International Journal of Oncology \| volume = 22 \| issue = 3 \| pages = 481–97 \| date = March 2003 \| pmid = 12579300 \| doi = 10.3892/ijo.22.3.481 \| doi-broken-date = 31 January 2024 }}
	* {{cite book \| vauthors = de Meester I, Lambeir AM, Proost P, Scharpé S \| chapter = Dipeptidyl Peptidase IV Substrates \| title = Dipeptidyl Aminopeptidases in Health and Disease \| volume = 524 \| pages = 3–17 \| year = 2003 \| pmid = 12675218 \| doi = 10.1007/0-306-47920-6_1 \| isbn = 0-306-47717-3 \| series = Advances in Experimental Medicine and Biology }}		* {{cite book \| vauthors = de Meester I, Lambeir AM, Proost P, Scharpé S \| chapter = Dipeptidyl Peptidase IV Substrates \| title = Dipeptidyl Aminopeptidases in Health and Disease \| volume = 524 \| pages = 3–17 \| year = 2003 \| pmid = 12675218 \| doi = 10.1007/0-306-47920-6_1 \| isbn = 0-306-47717-3 \| series = Advances in Experimental Medicine and Biology }}
	* {{cite book \| vauthors = Koch S, Anthonsen D, Skovbjerg H, Sjöström H \| chapter = On the role of dipeptidyl peptidase IV in the digestion of an immunodominant epitope in celiac disease \| volume = 524 \| pages = 181–7 \| year = 2003 \| pmid = 12675238 \| doi = 10.1007/0-306-47920-6_22 \| isbn = 0-306-47717-3 \| series = Advances in Experimental Medicine and Biology \| title = Dipeptidyl Aminopeptidases in Health and Disease }}		* {{cite book \| vauthors = Koch S, Anthonsen D, Skovbjerg H, Sjöström H \| chapter = On the role of dipeptidyl peptidase IV in the digestion of an immunodominant epitope in celiac disease \| volume = 524 \| pages = 181–7 \| year = 2003 \| pmid = 12675238 \| doi = 10.1007/0-306-47920-6_22 \| isbn = 0-306-47717-3 \| series = Advances in Experimental Medicine and Biology \| title = Dipeptidyl Aminopeptidases in Health and Disease }}

Fire at 13:35, 11 March 2024

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

	~~== References ==~~
	~~{{Reflist}}~~

	== Further reading ==		== Further reading ==

Fire at 13:17, 11 March 2024

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	{{Short description\|Mammalian protein found in humans}}		{{Short description\|Mammalian protein found in humans}}
	~~{{Infobox_gene}}~~

	'''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].		'''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].

Fire at 12:30, 11 March 2024

2024-03-11T12:30:49Z

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

Fire: Created page with "{{cs1 config|name-list-style=vanc}} {{Short description|Mammalian protein found in humans}} {{Infobox_gene}} '''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, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner, a..."

2024-03-11T12:30:38Z

Created page with "{{cs1 config|name-list-style=vanc}} {{Short description|Mammalian protein found in humans}} {{Infobox_gene}} '''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, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner, a..."

New page

{{cs1 config|name-list-style=vanc}}
{{Short description|Mammalian protein found in humans}}
{{Infobox_gene}}

'''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].

== Function ==
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 ==

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

== 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 [[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]]).

== See also ==
*[[Development of dipeptidyl peptidase-4 inhibitors]]
*[[Berberine]]

== References ==
{{Reflist}}

== Further reading ==
{{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 }}
* {{cite journal | vauthors = Reinhold D, Kähne T, Steinbrecher A, Wrenger S, Neubert K, Ansorge S, Brocke S | title = The role of dipeptidyl peptidase IV (DP IV) enzymatic activity in T cell activation and autoimmunity | journal = Biological Chemistry | volume = 383 | issue = 7–8 | pages = 1133–8 | year = 2003 | pmid = 12437097 | doi = 10.1515/BC.2002.123 | s2cid = 30027839 }}
* {{cite journal | vauthors = Sato K, Dang NH | title = CD26: a novel treatment target for T-cell lymphoid malignancies? (Review) | journal = International Journal of Oncology | volume = 22 | issue = 3 | pages = 481–97 | date = March 2003 | pmid = 12579300 | doi = 10.3892/ijo.22.3.481 | doi-broken-date = 31 January 2024 }}
* {{cite book | vauthors = de Meester I, Lambeir AM, Proost P, Scharpé S | chapter = Dipeptidyl Peptidase IV Substrates | title = Dipeptidyl Aminopeptidases in Health and Disease | volume = 524 | pages = 3–17 | year = 2003 | pmid = 12675218 | doi = 10.1007/0-306-47920-6_1 | isbn = 0-306-47717-3 | series = Advances in Experimental Medicine and Biology }}
* {{cite book | vauthors = Koch S, Anthonsen D, Skovbjerg H, Sjöström H | chapter = On the role of dipeptidyl peptidase IV in the digestion of an immunodominant epitope in celiac disease | volume = 524 | pages = 181–7 | year = 2003 | pmid = 12675238 | doi = 10.1007/0-306-47920-6_22 | isbn = 0-306-47717-3 | series = Advances in Experimental Medicine and Biology | title = Dipeptidyl Aminopeptidases in Health and Disease }}
* {{cite journal | vauthors = Pro B, Dang NH | title = CD26/dipeptidyl peptidase IV and its role in cancer | journal = Histology and Histopathology | volume = 19 | issue = 4 | pages = 1345–51 | date = October 2004 | pmid = 15375776 | doi = 10.14670/HH-19.1345 }}
{{refend}}

== External links ==
* The [[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}}
{{Proteases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}

{{二次利用|date= 8 March 2024}}
[[Category:EC 3.4.14]]
[[Category:Proteases]]