The Multifunctional Post-proline Dipeptidyl Peptidase, DPP9, in Mice, Cell Biology and Immunity

  title={The Multifunctional Post-proline Dipeptidyl Peptidase, DPP9, in Mice, Cell Biology and Immunity},
  author={Margaret G. Gall and Mark D. Gorrell},
Dipeptidyl peptidase 9 (DPP9) is a ubiquitous intracellular post-proline protease of the DPP4 (S9b) family of atypical serine proteases. Emerging data support roles for DPP9 in intracellular signalling, particularly in the epidermal growth factor receptor pathway, in immune cells, particularly in macrophages and antigen processing, and in energy metabolism. The focus of this review is the roles of DPP9 in regulating physiological and cellular processes. Such data is derived from a genetically… 
The dipeptidyl peptidase-4 inhibitory effect of flavonoids is hindered in protein rich environments.
The obtained results showed that the inhibitory effect of flavonoids against DPP-4 was hindered in protein rich environments, like that occurring in blood, and indicated the need for experimental refinement in drug discovery for blood targets.
A comprehensive review on the antidiabetic activity of flavonoids targeting PTP1B and DPP-4: a structure-activity relationship analysis
A comprehensive review of the literature of both synthetic and natural isolated flavonoids as inhibitors of PTP1B and DPP-4 activities is made, including their type of inhibition and experimental conditions, and structure-activity relationship, covering a total of 351 compounds.
DPP9: Comprehensive In Silico Analyses of Loss of Function Gene Variants and Associated Gene Expression Signatures in Human Hepatocellular Carcinoma
DPP9 is important for survival and that the DPP4 protease family, particularly DPP9, is important in the pathogenesis of human HCC, according to comprehensive data mining.
Associations Between DPP9 Expression, Survival and Gene Expression Signature in Human Hepatocellular Carcinoma: Comprehensive In Silico Analyses
This comprehensive data mining suggests that DPP9 is essential for human survival and the DPP4 protease family is important in cancer pathogenesis.


Advances in Understanding the Expression and Function of Dipeptidyl Peptidase 8 and 9
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
Biochemical properties and expression profile of human prolyl dipeptidase DPP9.
Dipeptidyl peptidase 9 enzymatic activity influences the expression of neonatal metabolic genes.
Dipeptidyl peptidase 8/9‐like activity in human leukocytes
It is shown that DPP activity, attributable to DPP8/9 is present in human PBMC and this activity was confirmed by DPPIV/CD26 immunocapture experiments.
A Novel Role of Dipeptidyl Peptidase 9 in Epidermal Growth Factor Signaling
It is found that DPP9 and DPP8, but not DPP4 or FAP, associate with H-Ras, a key signal molecule of the EGF receptor signaling pathway, suggesting an important signaling role of DPP 9 in the regulation of survival and proliferation pathways.
The dipeptidyl peptidase IV family in cancer and cell biology
This article examines, in detail, the current understanding of the biological involvement of the dipeptidyl peptidase IV gene family and their overall potential as therapeutic targets.
Identification of novel dipeptidyl peptidase 9 substrates by two‐dimensional differential in‐gel electrophoresis
This work identified the dipeptide Val‐Ala as a consensus site for DPP9 cleavage that was not recognized by DPP8, suggesting different in vivo roles for these closely related enzymes.
Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders.
The functional interactions of DPIV and FAP with extracellular matrix confer roles for these proteins in cancer biology and DPIV has become a novel target for Type II diabetes therapy.
Expression and enzymatic activity of dipeptidyl peptidase-IV in human astrocytic tumours are associated with tumour grade.
This is the first report showing that non-malignant brain tissue contains a DPP-IV-like enzymatic activity, while the substantial part of the activity in glioma is due to increased D PP-IV/CD26, localized in both the vascular and parenchymal compartments.