Biochemical properties and expression profile of human prolyl dipeptidase DPP9

Tang, Hung Kuan; Tang, Hsiang Yun; Hsu, Shih-Hsin; Chu, Yue Ru; Chien, Chia Hui; Shu, Chin Hang; Chen, Xin

doi:10.1016/j.abb.2009.02.015

Cited by 34 publications

(33 citation statements)

References 30 publications

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“…Since DPP9-S is known to form dimers, we asked whether DPP9-l behaves in a similar manner by comparing the elution profile of both enzymes on size exclusion chromatography. In line with previously published results [8,11,31], DPP9-S eluted from the gel filtration column in a single peak corresponding in size to a dimer (Fig. 2b).…”

Section: Dpp9-l Is An Active Peptidasesupporting

confidence: 92%

“…Biochemical examination reveals that similar to other members of the DPP family [6][7][8][9][10][11]42], DPP9-l also forms dimers and is active, with comparable cleavage characteristics to the shorter DPP9 variant. taken together, these results show for the first time that the endogenous pool of DPP9 protein in cells is composed of at least two different versions: DPP9-S and DPP9-l, which share similar biochemical properties.…”

Section: Dpp9-l Is An Active Peptidasementioning

confidence: 93%

“…Four active members of this family are known so far: the two membrane-bound cell-surface members dipeptidyl peptidase IV (DPPIV) and the Fibroblast activation protein alpha (FaP), as well as the two soluble members DPP8 and 1 3 DPP9 (reviewed in [3][4][5][6]). Dimerization is a common feature for members of the S9B/DPPIV family [6][7][8][9][10][11] and is essential for enzymatic activity [12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

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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.

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Section: Dpp9-l Is An Active Peptidasesupporting

confidence: 92%

Section: Dpp9-l Is An Active Peptidasementioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

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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.

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“…The DPP8 sequence contains no N-linked or O-linked glycosylation sites (2) and, despite identification of 2 potential N-glycosylation sites in DPP9, no evidence of glycosylation has been found (3,23,40). Lysine 51 and Lysine 314 in DPP9 have been identified as potential acetylation targets in 2 separate proteomic and mass spectrometric acetylation studies (41,42), but this has not been verified in vivo.…”

Section: Posttranslational Modificationmentioning

confidence: 99%

“…Therefore, identifying the substrates for DPP8 and DPP9 is essential for understanding their biological functions. DPP8 and DPP9 have similar substrate specificities, with both enzymes preferring substrates with an aromatic or branched aliphatic amino acid (46) or basic residue (34,40) in the P2…”

Section: Synthetic Substrates For Activity Determinationmentioning

confidence: 99%

Advances in Understanding the Expression and Function of Dipeptidyl Peptidase 8 and 9

Zhang

Chen

Keane

et al. 2013

Molecular Cancer Research

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DPP8 and DPP9 are recently identified members of the dipeptidyl peptidase IV (DPPIV) enzyme family, which is characterized by the rare ability to cleave a post-proline bond two residues from the N-terminus of a substrate. DPP8 and DPP9 have unique cellular localization patterns, are ubiquitously expressed in tissues and cell lines, and evidence suggests important contributions to various biological processes including: cell behavior, cancer biology, disease pathogenesis, and immune responses. Importantly, functional differences between these two proteins have emerged, such as DPP8 may be more associated with gut inflammation whereas DPP9 is involved in antigen presentation and intracellular signaling. Similarly, the DPP9 connections with H-Ras and SUMO1, and its role in AKT1 pathway downregulation provide essential insights into the molecular mechanisms of DPP9 action. The recent discovery of novel natural substrates of DPP8 and DPP9 highlights the potential role of these proteases in energy metabolism and homeostasis. This review focuses on the recent progress made with these post-proline dipeptidyl peptidases and underscores their emerging importance.

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DPP8/9 are not Required to Cleave Most Proline‐Containing Peptides

Bhattacharjee

Bachovchin

2023

Israel Journal of Chemistry

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Small molecule inhibitors of the intracellular serine peptidases DPP8 and DPP9 (DPP8/9) activate the NLRP1 and CARD8 inflammasomes, but the key DPP8/9 substrates have not yet been identified. DPP8/9 cleave after proline to remove N-terminal dipeptides from peptides or proteins, and studies using pseudo-peptide reporter substrates have suggested that these enzymes may play key roles in the catabolism of many proline-containing peptides generated by the proteasome. Here, we evaluated the degradation of a wide array of actual peptides in cell lysates, and discovered that DPP8/9 are not in fact involved in the processing of the vast majority of proline-containing peptides. Overall, these results indicate that DPP8/9 have a much more limited substrate scope than previously thought, and likely specifically cleave some critically important, but as yet unknown, intracellular peptide or protein that regulates inflammasome activation.

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Biochemical properties and expression profile of human prolyl dipeptidase DPP9

Cited by 34 publications

References 30 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

Advances in Understanding the Expression and Function of Dipeptidyl Peptidase 8 and 9

DPP8/9 are not Required to Cleave Most Proline‐Containing Peptides

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