The DOI matches its Crossref record; 123 of the 123 references it cites were found in a registry or an index.
Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders
Abstract
DP (dipeptidyl peptidase) IV is the archetypal member of its six-member gene family. Four members of this family, DPIV, FAP (fibroblast activation protein), DP8 and DP9, have a rare substrate specificity, hydrolysis of a prolyl bond two residues from the N-terminus. The ubiquitous DPIV glycoprotein has proved interesting in the fields of immunology, endocrinology, haematology and endothelial cell and cancer biology and DPIV has become a novel target for Type II diabetes therapy. The crystal structure shows that the soluble form of DPIV comprises two domains, an α/β-hydrolase domain and an eight-blade β-propeller domain. The propeller domain contains the ADA (adenosine deaminase) binding site, a dimerization site, antibody epitopes and two openings for substrate access to the internal active site. FAP is structurally very similar to DPIV, but FAP protein expression is largely confined to diseased and damaged tissue, notably the tissue remodelling interface in chronically injured liver. DPIV has a variety of peptide substrates, the best studied being GLP-1 (glucagon-like peptide-1), NPY (neuropeptide Y) and CXCL12. The DPIV family has roles in bone marrow mobilization. The functional interactions of DPIV and FAP with extracellular matrix confer roles for these proteins in cancer biology. DP8 and DP9 are widely distributed and indirectly implicated in immune function. The DPL (DP-like) glycoproteins that lack peptidase activity, DPL1 and DPL2, are brain-expressed potassium channel modulators. Thus the six members of the DPIV gene family exhibit diverse biological roles.
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Serine peptidases: Classification, structure and function
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Mechanisms underlying the rapid degradation and elimination of the incretin hormones GLP-1 and GIP
Mentlein, R. (2009) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2009.03.005 · Cited by 94
Fecal Dipeptidyl Peptidase-4: An Emergent Biomarker in Inflammatory Bowel Disease
Pinto-Lopes, P., Melo, F., Afonso, J., Pinto-Lopes, R., Rocha, C., Melo, D., Macedo, G., Dias, C. C., Carneiro, F., Magro, F., et al. (2021) · Clinical and Translational Gastroenterology · doi:10.14309/ctg.0000000000000320 · Cited by 11
Metadata
- Authors
- GORRELL, M. D.
- Venue
- Clinical Science
- Publisher
- Portland Press Ltd.
- Published
- 2005-03-22
- Volume
- 108
- Issue
- 4
- Pages
- 277-292
- ISSN
- 0143-5221 (ISSN-L)
- 1470-8736
- OpenAlex
- W2071601558
- Cited by
- 334
- References
- 123
- FWCI
- 7.77
- Type
- journal article
- Language
- en
- Open access
- closed
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