Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity

Ajami, Katerina; Abbott, Catherine A.; McCaughan, Geoffrey W.; Gorrell, Mark D.

doi:10.1016/j.bbaexp.2004.03.010

Cited by 129 publications

(141 citation statements)

References 41 publications

Supporting

Mentioning

132

Contrasting

Order By: Relevance

“…the shorter version of DPP9 was initially identified by Olsen and Wagtmann [20]. Cloning and expression of this short DPP9 version (863 aa) in mammalian cell culture verified that DPP9-short is active and is localized to the cytosol [19,21]. Importantly, DPP9-short was recently purified from bovine testes, confirming the endogenous expression of this short DPP9 isoform [34].…”

Section: Introductionmentioning

confidence: 84%

“…60 % amino acid identity), are only emerging. Both peptidases are ubiquitously expressed on mRNa levels in various organs and tissues and cell lines [18][19][20][21][22]. Changes in the levels of these peptidases appear to be critical for cell survival, as both overexpression or application of DPP8/9 inhibitors lead to cell death in several cell lines [23][24][25].…”

Section: Introductionmentioning

confidence: 99%

“…Interestingly, the major DPP9 RNa transcript of 4.4 kb contains two possible translation initiation sites, which could generate a longer version (892 aa) and a shorter version (863 aa) of DPP9 [8,19,20]. In recent years, it was a matter of debate whether both DPP9 isoforms, long and short, are expressed on protein level in cells and whether they are active.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus

Justa-Schuch

Möller

Geiss‐Friedlander

2014

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 84%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus

Justa-Schuch

Möller

Geiss‐Friedlander

2014

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

show abstract

“…However, the intracellular functions of DPP9 are less clear. DPP9 has two forms and a broad tissue distribution 12. Waumans et al 24.…”

Section: Discussionmentioning

confidence: 99%

“…Alterations in dipeptidyl peptidase‐IV (DPP4) enzymatic activity are characteristic of malignant trans‐formation. Through its well‐characterized functionality in regulating the activity of bioactive peptides by removal of the N‐terminal dipeptide, DPP‐IV activity may have profound effects upon metastatic potential and cell growth 12, 13. The inhibition of DPP8/9 in tumor cells decreased the number of viable cells because of a decreased cleavage of pro‐apoptotic NPY,14 also their activity has been found in human monocytes and U937 cells 15.…”

mentioning

confidence: 99%

Contribution of upregulated dipeptidyl peptidase 9 (DPP9) in promoting tumoregenicity, metastasis and the prediction of poor prognosis in non‐small cell lung cancer (NSCLC)

Tang

Shen

et al. 2017

Intl Journal of Cancer

View full text Add to dashboard Cite

Dipeptidyl peptidase 9 (DPP9) is encoded by DPP9, which belongs to the DPP4 gene family. Proteins encoded by these genes have unique peptidase and extra‐enzymatic functions that have been linked to various diseases including cancers. Here, we describe the expression pattern and biological function of DPP9 in non‐small‐cell lung cancer (NSCLC). The repression of DPP9 expression by small interfering RNA inhibited cell proliferation, migration, and invasion. Moreover, we explored the role of DPP9 in regulating epithelial‐mesenchymal transition (EMT). The epithelial markers E‐cadherin and MUC1 were significantly increased, while mesenchymal markers vimentin and S100A4 were markedly decreased in DPP9 knockdown cells. The downregulation of DPP9 in the NSCLC cells induced the expression of apoptosis‐associated proteins both in vitro and in vivo. We investigated the protein expression levels of DPP9 by tissue microarray immunohistochemical assay (TMA‐IHC) (n = 217). Further we found mRNA expression levels of DPP9 in 30 pairs of clinical NSCLC tissues were significantly lower than in the adjacent non‐cancerous tissues. Survival analysis showed that the overexpression of DPP9 was a significant independent factor for poor 5‐year overall survival in patients with NSCLC (p = 0.003). Taken together, DPP9 expression correlates with poor overall survival in NSCLC.

show abstract

Dipeptidyl Peptidase 4 Inhibitors

Weber

Thornberry

2010

Burger's Medicinal Chemistry and Drug Discovery

View full text Add to dashboard Cite

Defective insulin secretion is a hallmark of type 2 diabetes (T2DM), and agents that increase the concentration of circulating insulin have proven beneficial in the treatment of diabetes. Dipeptidyl peptidase 4 (DPP‐4) inhibitors are a new oral approach to T2DM that lower glucose via stabilization of the incretin hormone glucagon‐like peptide 1 (GLP‐1), which has clearly established roles in insulin secretion and inhibition of glucagon production. These agents have been shown to produce clinically meaningful glucose control in a range of patients with type 2 diabetes without many of the liabilities that are associated with other oral therapies, including weight gain, edema, GI intolerability, and hypoglycemia. Accordingly, DPP‐4 inhibitors have excellent potential for use in both monotherapy and combination with established agents. Extensive structure–activity relationship (SAR) studies in many different laboratories have resulted in the identification of a number of clinical candidates. The most advanced of these have recently been approved for the treatment of T2DM, representing the first new oral therapy for treatment of this disease since the introduction of troglitazone in 1998.

show abstract

Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity

Cited by 129 publications

References 41 publications

The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus

The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus

Contribution of upregulated dipeptidyl peptidase 9 (DPP9) in promoting tumoregenicity, metastasis and the prediction of poor prognosis in non‐small cell lung cancer (NSCLC)

Dipeptidyl Peptidase 4 Inhibitors

Contact Info

Product

Resources

About