The In Vivo Expression of Dipeptidyl Peptidases 8 and 9

@article{Yu2009TheIV,
  title={The In Vivo Expression of Dipeptidyl Peptidases 8 and 9},
  author={Denise M. T. Yu and Katerina Ajami and Margaret G. Gall and Joo-Ung Park and C. S. Lee and Kathryn A Evans and Eileen A. McLaughlin and Melissa R. Pitman and Catherine A Abbott and Geoffrey W McCaughan and Mark D. Gorrell},
  journal={Journal of Histochemistry \& Cytochemistry},
  year={2009},
  volume={57},
  pages={1025 - 1040}
}
The dipeptidyl peptidase IV (DPIV) enzyme family contains both potential and proven therapeutic targets. Recent reports indicate the presence of DP8 and DP9 in peripheral blood lymphocytes, testis, lung, and brain. For a more comprehensive understanding of DP8 and DP9 tissue and cellular expression, mRNA and enzyme activity were examined. Many organs from C57BL/6 wild-type and DPIV gene-knockout mice were examined; DP8/9 enzyme activity was detected in the immune system, brain, testis, muscle… 

Figures and Tables from this paper

Expression profiling of dipeptidyl peptidase 8 and 9 in breast and ovarian carcinoma cell lines.
TLDR
A potential role for DP8 and DP9 in breast and ovarian cancer is suggested and further investigations in this area are required.
Regulation of dipeptidyl peptidase 8 and 9 expression in activated lymphocytes and injured liver.
TLDR
These expression patterns point to biological roles for DPP8 and DPP9 in lymphocyte activation and apoptosis and in hepatocytes during liver disease 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
Expression, subcellular localisation, and possible roles of dipeptidyl peptidase 9 (DPP9) in murine macrophages
TLDR
Compared the messenger RNA expression profile of DPP9 to that of the related DPP8 and DPPIV in murine haematopoietic and lymphatic tissues and the colocalisation of D PP9 with endocytosed DQ‐OVA demonstrated in endosomes of J774 cells might suggest the role of DP9 in peptide processing within endosomal/vesicular compartment.
Expression and prognostic assessment of dipeptidyl peptidase IV and related enzymes in B-cell chronic lymphocytic leukemia
TLDR
This study characterized the expression of all DPIV-like enzymes in chronic lymphocytic leukemia (CLL) and demonstrated the constitutive expression of DPIV, DP8, DP9, DPII and PEP RNA and protein and shows that DP8 mRNA expression is significantly up-regulated in CLL compared to normal tonsil B-lymphocytes.
The effect of CD26‐deficiency on dipeptidyl peptidase 8 and 9 expression profiles in a mouse model of Crohn's disease
TLDR
CD induction generated gene, protein and enzymatic changes of DP8 and DP9 so their involvement in inflammation development and/or healing process is implicated, especially in CD26−/−, and the question of their subcellular localization should be revised.
The dipeptidyl peptidase IV family in cancer and cell biology
TLDR
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.
Targeted Inactivation of Dipeptidyl Peptidase 9 Enzymatic Activity Causes Mouse Neonate Lethality
TLDR
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.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 59 REFERENCES
Regulation of Expression and Function of Dipeptidyl Peptidase 4 (DP4), DP8/9, and DP10 in Allergic Responses of the Lung in Rats
  • J. Schade, M. Stephan, S. Hörsten
  • Biology
    The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
  • 2008
TLDR
Surprisingly, results show not only that the induction of experimental asthma increases DP4 enzymatic activity in the bronchoalveolar lavage fluid and parenchyma, but also that DP8/9 enzymatics activity is regulated and, as well as the expression of DP10, primarily found in theBronchial epithelium of the airways, suggesting a pathophysiologically significant role in asthma.
Enzyme Activity and Immunohistochemical Localization of Dipeptidyl Peptidase 8 and 9 in Male Reproductive Tissues
TLDR
The mRNA expression pattern of dipeptidyl peptidase (DPP) 8 and DPP9, two DPP4 homologs, was studied previously and showed a broad tissue distribution and was found associated with spermatozoids embedded in the epithelium, just before their release into the lumen, and in spermatids.
Expression and enzymatic activity of dipeptidyl peptidase-IV in human astrocytic tumours are associated with tumour grade.
TLDR
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.
Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders
TLDR
The functional interactions of DPIV and FAP with extracellular matrix confer roles for these proteins in cancer biology, and DP8 and DP9 are widely distributed and indirectly implicated in immune function.
Expression of the rat CD26 antigen (dipeptidyl peptidase IV) on subpopulations of rat lymphocytes.
Dipeptidyl peptidase (DPP) IV in rat organs
TLDR
Immunohistochemistry and activity histochemistry were used to study the localization of dipeptidyl peptidase (DPP) IV in rats, and revealed that certain epitopes were not detectable by immunohists in some organs.
Expression of a novel dipeptidyl peptidase 8 (DPP8) transcript variant, DPP8-v3, in human testis.
TLDR
Similar to DPPIV, DPP8-v3 may play a key role in the immunoregulation of testes and accordingly may influence spermatogenesis and male fertility.
Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8.
TLDR
DPP8, a novel human postproline dipeptidyl aminopeptidase that is homologous to DPPIV and FAP is described and a potential role for DPP8 in T-cell activation and immune function is suggested.
Dipeptidyl peptidase 8/9‐like activity in human leukocytes
TLDR
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.
Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family.
TLDR
It is proposed that the extracellular region of CD26 is analogous to prolyl oligopeptidase in consisting of an alpha/beta hydrolase domain contributed by both N- and C-terminal portions of the polypeptide and a seven-blade beta-propeller domain.
...
1
2
3
4
5
...