Ignet

Gene Information

Gene symbol: DPEP3

Gene name: dipeptidase 3

HGNC ID: 23029

Related Genes

#	Gene Symbol	Number of hits
1	ACE	1 hits
2	AOC3	1 hits
3	APLP2	1 hits
4	INS	1 hits
5	MME	1 hits
6	TAC1	1 hits

Related Sentences

#	PMID	Sentence
1	11381288	The development of a sensitive and specific analytical approach for the quantification of bradykinin (BK) has enabled the identification of five metallopeptidases primarily responsible for the metabolism of BK, including angiotensin-converting enzyme (ACE) and neutral endopeptidase 24.11.
2	11381288	These studies advance understanding of the role of endogenous BK in the cardiovascular effects of ACE inhibitors and other metallopeptidase inhibitors.
3	12406165	Neutral endopeptidase (NEP), a cell surface metallopeptidase, degrades substance P.
4	12785004	Neutral endopeptidase (NEP), a membrane-bound metallopeptidase enzyme that degrades neuropeptides, bradykinin, atrial natriuretic factor, enkephalins, and endothelin may regulate response to injury.
5	18413170	Synergistic interaction between semicarbazide-sensitive amine oxidase and angiotensin-converting enzyme in diabetes: functional analysis by gene ontology.
6	18413170	Plasma semicarbazide-sensitive amine oxidase (SSAO) and angiotensin-converting enzyme (ACE) were studied for their correlation with diabetes (DM) complication.
7	18413170	The effect of interaction between SSAO and ACE in DM complication is of interest.
8	18413170	Studying the functional change due to interaction between SSAO and ACE is difficult.
9	18413170	In this work, the author used a new gene ontology technology to predict the functional change resulting from the interaction between SSAO and ACE.
10	18413170	However, the author can also demonstrate that some molecular functions such as proteasome activator activity of SSAO and hydrolase activity, metallopeptidase activity, and zinc ion binding of ACE are suppressed after co-expression.
11	19836835	The peptidases angiotensin-converting enzyme (ACE) and neutral endopeptidase 24.11 (NEP) mediate most of the kinin catabolism in normal cardiac tissue and are the molecular targets of inhibitory drugs that favorably influence diabetic complications.
12	19836835	ACE and NEP activities were significantly decreased in heart membranes 4-8weeks post-streptozotocin (STZ) injection.
13	19836835	However, insulin-dependent diabetes did not modify significantly bradykinin (BK) half-life (t(1/2)) while the effect of both ACE (enalaprilat) and ACE and NEP (omapatrilat) inhibitors on BK degradation progressively decreased, which may be explained by the upregulation of other unidentified metallopeptidase(s).
14	19836835	In vivo insulin treatment restored the activities of both ACE and NEP.
15	19836835	ACE and NEP activities were significantly higher in hearts of young Zucker rats than in those of Sprague-Dawley rats.
16	20400513	Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation.
17	20400513	Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear.
18	20400513	Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease.
19	20400513	We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid.
20	20400513	Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%.
21	20400513	To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage.
22	20400513	In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP.
23	20400513	These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes.