3.4.14.5: dipeptidyl-peptidase IV
This is an abbreviated version!
For detailed information about dipeptidyl-peptidase IV, go to the full flat file.
Reaction
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
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Synonyms
(GLP1)-degrading enzyme, ACT3, ADA binding protein, ADA-binding protein, ADABP, adenosine deaminase binding protein, Adenosine deaminase complexing protein, adenosine deaminase-binding protein, amino acyl-prolyl dipeptidyl aminopeptidase, aminopeptidase, glycylproline, Bile canaliculus domain-specific membrane glycoprotein, CD26, CD26 peptidase, CD26/dipeptidyl peptidase, CD26/DP IV, DAP IV, DapB, dapUm, dipeptidyl aminopeptidase IV, dipeptidyl dipeptidase IV, dipeptidyl peptidase 4, dipeptidyl peptidase 8, dipeptidyl peptidase 9, dipeptidyl peptidase IV, dipeptidyl peptidase-4, dipeptidyl peptidase-IV, dipeptidyl-aminopeptidase IV, dipeptidyl-peptidase 4, dipeptidyl-peptidase IV (CD26), dipeptidyl-peptide hydrolase, dipeptidylpeptidase 4a, dipeptidylpeptidase 4b, dipeptidylpeptidase IV, dipeptidylpeptidase IV/CD26, dipeptidylpeptidase-IV, DP IV, DP-IV, DPIV, DPP, DPP IV, DPP IV/CD26, DPP-4, DPP-IV, DPP4, DPP8, DPP9, DPPIV, DppIVA, DppIVB, glucagon-like peptide 1-degrading enzyme, Gly-Pro-naphthylamidase, glycoprotein GP110, glycylproline aminopeptidase, glycylproline-dipeptidyl-aminopeptidase, glycylprolyl aminopeptidase, glycylprolyl dipeptidylaminopeptidase, GP110 glycoprotein, h-DPPIV, hDPPIV, leukocyte antigen CD26, lymphocyte, antigen CD26, More, omega DPPIV, omega enzyme, omega gene product, Pep X, peptidase, dipeptidyl, IV, PepX, postproline dipeptidyl aminopeptidase IV, prolyl-dipeptidyl-aminopeptidase, sipeptidyl peptidase IV, T cell triggering molecule Tp103, T-cell activation antigen CD26, THAM, Thymocyte-activating molecule, TP103, type IV dipeptidyl aminopeptidase, WC10, X-PDAP, X-prolyl dipeptidyl aminopeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro-dipeptidyl-aminopeptidase
ECTree
Source Tissue
Source Tissue on EC 3.4.14.5 - dipeptidyl-peptidase IV
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in artery DPIV represents 92% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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mRNA expression in ipsilateral and contralateral cortices. At day 3 post-ischemia, dipeptidyl peptidase IV, 8 and aminopeptidase N are identified in activated microglia and macrophages in the ipsilateral cortex. Seven days post artery occlusion, dipeptidyl peptidase IV immunoreactivity is found in the perikarya of surviving cortical neurons of the ipsilateral hemisphere. At the same time point, dipeptidyl peptidase IV, 8 and aminopeptidase N are targeted in astroglial cells. Total dipeptidyl peptidase IV, 8 and 9 activities remain constant in both hemispheres until day 3 post experimental ischemia, but are increased to 165% in the ipsilateral cortex at day 7
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in colon DPIV represents 33% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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in contrast to the normal cornea where DPPIV activity is absent and the tear fluid where it is low, during continuous wearing of contact lenses or repeated irradiation of the cornea with UVB rays, slight DPPIV activity appeared first in the superficial layers of the corneal epithelium, while later increased activity is present in the whole epithelium.This parallels elevated DPPIV activity in the tear fluid
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in duodenum DPIV represents 89% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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HCEC
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in heart DPIV represents 71% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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CD26
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neuroectodermal melanoma cell line, proliferating and quiescent populations
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neuroectodermal glioma cell line, proliferating and quiescent populations
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in ileum DPIV represents 94% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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brush border membrane
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casein-induced, intraperitoneal polymorphonuclear
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acinar cells of mucous glands
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levels of tissue DPP-4 are reduced in nasal tissue of human subjects with chronic rhinosinusitis
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the enzyme is coexpressed with fibroblast activation protein in adult humans
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from cord blood
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malt from green barley
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neuroectodermal, melanoma cell line, proliferating and quiescent populations
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squamous lung carcinoma, enzymic activity is restricted to the connective tissue stroma surrounding the dipeptidyl peptidase IV-negative tumor foci
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CEM, C8166, Molt4/C8, MT-4
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in contrast to the normal cornea where DPPIV activity is absent and the tear fluid where it is low, during continuous wearing of contact lenses or repeated irradiation of the cornea with UVB rays, slight DPPIV activity appeared first in the superficial layers of the corneal epithelium, while later increased activity is present in the whole epithelium.This parallels elevated DPPIV activity in the tear fluid
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neuroectodermal glioma cell line, proliferating and quiescent populations
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neuroectodermal cell line, low activity in proliferating population, quiescent population
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neuroectodermal glioma cell line, proliferating and quiescent populations
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in vein DPIV represents 80% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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cell surface
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DPP4 activity is higher in whole blood than in the blood plasma
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DPP4 activity is higher in whole blood than in the blood plasma
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664313, 677897, 678622, 678658, 679663, 679668, 680234, 696134, 697297, 697436, 697489, 697519, 697522, 697550, 697551, 697764, 698213, 698335, 700399, 702623, 702941, 703552, 703784, 705754 brenda
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679662, 679663, 696134, 697556, 697561, 697763, 697770, 697773, 699445, 699748, 699944, 699985, 700399, 700400, 700615 brenda
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in blood plasma DPIV represents 78% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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664313, 664847, 678597, 678634, 678658, 681319, 681325, 696134, 696136, 696668, 696746, 697764, 699445, 699748, 702514, 702623, 704840 brenda
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activity is increased in sera from individuals with angiotensin-converting enzyme inhibitor-associated angioedema compared with angiotensin-converting enzyme inhibitor-exposed control subjects without angioedema
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high activity
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endothelium
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in brain DPIV represents 22% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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commercial solution of human serum albumin
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glomerular endothelial cells
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of spleen, lung, brain and vessels supplying the liver
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DPP-IV is localized only in epithelial cells of vessels of the blood-brain barrier and on ependyma
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fibroblasts from patients with Fabry disease and a healthy person
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lung-derived and skin-derived
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normal, 3T3, and transformed, 3T12
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from umbilical cord blood
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high activity
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brush-border
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microvillar membrane
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high activity
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membrane-bound
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highly expressed in kidney
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most densely located in the kidney
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in kidney DPIV represents 92% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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brush border membrane
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brush-border membrane
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dipeptidyl peptidase IV is expressed in the renal microcirculation. Inhibition of this ecto-enzyme causes arterial peptide YY1-36 to more effectively enhance angiotensin II-induced renal vasoconstriction in genetically susceptible kidneys
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36207, 36215, 36220, 36223, 36234, 36240, 649274, 649275, 649282, 649285, 652293, 663901, 664847, 682253 brenda
cortex
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microvillar membrane
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brush-border membrane
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in liver DPIV represents 94% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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endothelium
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fetal lung-derived cells. Surface and total dipeptidyl peptidase activities of P cells are correspondingly 7-8 and 3-10 times higher than those of SK-MES-1 and A549 cells
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in lung DPIV represents 94% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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in lymph nodes DPIV represents 62% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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normal and cells of chronic lymphocytic leukemia of the T type. The enzyme is absent in T cells bearing the Fc receptor for IgM
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nitrogen-stimulated. Increase in specific activity of the enzyme is characteristic of a new population of cells
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extoenzyme in cell membrane
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increased enzyme activity in chronic lymphocytic leukemia
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overexpression
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in pancreas DPIV represents 14% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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the enzyme is coexpressed with fibroblast activation protein in adult humans
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acinar cells of salivary glands
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membrane-bound enzyme loses its transmembrane domain upon release into the serum
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of hepatoma bearing rats
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in skin DPIV represents 79% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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maximally expressed in mid-villus cells, substantial activity in the crypt cells, primarily associated with brush border membranes in all segments, in the proximal intestine, a significant amount of the enzyme is associated with the cytosol fraction. Cytosol and brush border membrane forms are immunologically identical
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brush-border membrane
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endothelium
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in spleen DPIV represents 73% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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mitogen- or anti-CD3-stimulated
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cell surface
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cell surface
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in thymus DPIV represents 93% of the total Gly-L-Pro-4-nitroanilide-hydrolyzing activity
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additional information
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changes in enzyme expression are observed in numerous types of human malignancies as well as in blood plasma of cancer patients
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additional information
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no activity in cell lines SK-MEL-28 and T98G
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additional information
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DPPIV expression is greatly decreased or lost in cells derived from neuroblastoma
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