13 Result(s)
within
Catherine A. Abbott
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Article
Open AccessDevelopment of a 13C Stable Isotope Assay for Dipeptidyl Peptidase-4 Enzyme Activity A New Breath Test for Dipeptidyl Peptidase Activity
Dipeptidyl peptidase-4 inhibitors (DPP4i) are a class of orally available, small molecule inhibitors for the management of Type-II diabetes. A rapid, real-time, functional breath test for DPP4 enzyme activity ...
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Article
Potential disease biomarkers: dipeptidyl peptidase 4 and fibroblast activation protein
The importance of the dipeptidyl peptidase 4 (DPP4) gene family in regulating critical biochemical pathways continues to emerge. The two most well-studied members of the family, DPP4 and fibroblast activation ...
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Article
Open AccessCytokines regulate complement receptor immunoglobulin expression and phagocytosis of Candida albicans in human macrophages: A control point in anti-microbial immunity
Complement Receptor Immunoglobulin (CRIg), selectively expressed by macrophages, plays an important role in innate immunity by promoting phagocytosis of bacteria. Thus modulation of CRIg on macrophages by cyto...
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Protocol
Studying Permeability in a Commonly Used Epithelial Cell Line: T84 Intestinal Epithelial Cells
The integrity, or barrier function, of the intestinal epithelium is of paramount importance in maintaining good health. This is largely imparted by a single layer of epithelial cells linked by the transmembra...
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Chapter and Conference Paper
Dipeptidyl Peptidases and Inflammatory Bowel Disease
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Chapter and Conference Paper
Prediction of Dipeptidyl Peptidase (DP) 8 Structure by Homology Modelling
The DP8 model produced was very similar to the DPIV structure in the α/β hydrolase domain. Analysis of the active site of the DP8 model revealed significant structural conservation in the catalytic triad between ...
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Chapter and Conference Paper
DPIV/CD26 and FAP in Cancer: A Tale of Contradictions
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Chapter
Dipeptidyl Peptidase IV Gene Family
We have identified three novel members of the DPIV gene family using database mining approaches. Recombinant DP8 shares a post-proline dipeptidyl aminopeptidase activity with the closely related enzymes DPIV a...
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Chapter
Molecular Chimeras and Mutational Analysis in the Prolyl Oligopeptidase Gene Family
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Chapter
Relating Structure to Function in the Beta-Propeller Domain of Dipeptidyl Peptidase IV
Point mutations in human CD26/DP IV were analysed for adenosine deaminase (ADA) binding, monoclonal antibody (mAb) binding and DP IV enzyme activity. Point mutations at either Leu294 or Val341 ablated ADA bind...
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Chapter
Post Proline Cleaving Peptidases Having DP IV Like Enzyme Activity
DP IV has been studied extensively in disease and in the immune system by the use of enzyme assays which detect hydrolysis of Gly-Pro or Ala-Pro substrate. In addition many studies have used inhibitors of DP I...
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Chapter
The Family of CD26/DPIV and Related Ectopeptidases
DPIV is the best understood proteinase that has the rare capability of hydrolysing the prolyl bond (Gorrell et al 2001). Members of several other enzyme families have this capability, including families S28 and M...
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Article
Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene
CD26 is a lymphocyte cell surface antigen which is increased during T -cell activation and is also expressed in other tissues. It is an atypical serine protease belonging to the prolyl oligopeptidase family. C...
