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The In Vivo Expression of Dipeptidyl Peptidases 8 and 9
- Denise M. T. Yu, Katerina Ajami, +8 authors M. Gorrell
- Biology, MedicineThe journal of histochemistry and cytochemistry…
- 1 November 2009
DP8 and DP9 mRNA were ubiquitous in day 17 mouse embryo, with greatest expression in epithelium (skin and gastrointestinal tract) and brain, and their expression in lymphocytes and epithelia indicates potential for roles in the digestive and immune systems.
Targeted Inactivation of Dipeptidyl Peptidase 9 Enzymatic Activity Causes Mouse Neonate Lethality
The first gene knock-in mouse with a serine to alanine point mutation at the DPP9 active site (S729A) is made, suggesting that DPP 9 enzymatic activity is essential for early neonatal survival in mice.
Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs☆
The new FAP enzyme assay is the first to be thoroughly characterised and shows that FAP activity is measurable in most organs and at high levels in some, particularly liver fibrosis.
The pro‐fibrotic role of dipeptidyl peptidase 4 in carbon tetrachloride‐induced experimental liver injury
- X. M. Wang, Lauren E. Holz, +13 authors M. Gorrell
- Biology, MedicineImmunology and cell biology
- 1 May 2017
The data suggest that DPP4 is pro‐fibrotic in CCl4‐induced liver fibrosis and that the mechanisms of DPP 4 pro-f fibrotic action include energy metabolism, B cells, NK cells and CD4+ cells.
Chapter 5:Targeting Dipeptidyl Peptidase-4 (DPP-4) and Fibroblast Activation Protein (FAP) for Diabetes and Cancer Therapy
An overall understanding of DPP-4 and FAP structure–function relationships, distribution, and enzymatic and extra-enzymatic biological roles provides an insight into their therapeutic usefulness as disease targets.
Neuropeptide Y is a physiological substrate of fibroblast activation protein: Enzyme kinetics in blood plasma and expression of Y2R and Y5R in human liver cirrhosis and hepatocellular carcinoma
- P. F. Wong, Margaret G. Gall, W. Bachovchin, G. McCaughan, F. Keane, M. Gorrell
- Biology, MedicinePeptides
- 31 January 2016
This study is the first to characterize the physiological substrate repertoire of the DPP activity of endogenous FAP present in plasma and reveal a potential function for FAP in neuropeptide regulation within liver and cancer biology.
Dipeptidyl peptidase 9 enzymatic activity influences the expression of neonatal metabolic genes.
- Yiqian Chen, Margaret G. Gall, +4 authors M. Gorrell
- Biology, MedicineExperimental cell research
- 1 March 2016
The success of dipeptidyl peptidase 4 (DPP4) inhibition as a type 2 diabetes therapy has encouraged deeper examination of the post-proline DPP enzymes. DPP9 has been implicated in immunoregulation,…
The Multifunctional Post-proline Dipeptidyl Peptidase, DPP9, in Mice, Cell Biology and Immunity
Roles for DPP9 in regulating physiological and cellular processes, including immunity, metabolism and cancer, are supported by emerging data and derived from a genetically modified mouse strain and from manipulations of cell lines.
Fibroblast activation protein enzyme deficiency prevents liver steatosis, insulin resistance and glucose intolerance and increases fibroblast growth factor-21 in diet induced obese mice
This is the first study to show that specific genetic ablation of FAP activity or protein protects against DIO-driven glucose intolerance, hyperinsulinaemia, insulin resistance, hypercholesterolaemia and liver steatosis in mice and provide mechanistic insights.
Immune regeneration in irradiated mice is not impaired by the absence of DPP9 enzymatic activity
No differences in myeloid or lymphoid lineage reconstitution between WT and DPP9S729A donors are observed, indicating that hematopoietic stem cell (HSC) engraftment and self-renewal is not diminished by the absence of D PP9 enzymatic activity.