The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Molecular characterization of dipeptidyl peptidase activity in serum: Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X‐Pro dipeptides
Open accessAbstract
Dipeptidyl peptidase IV (DPPIV, EC 3.4.14.5) is a serine type protease with an important modulatory activity on a number of chemokines, neuropeptides and peptide hormones. It is also known as CD26 or adenosine deaminase (ADA; EC 3.5.4.4) binding protein. DPPIV has been demonstrated on the plasmamembranes of T cells and activated natural killer or B cells as well as on a number of endothelial and differentiated epithelial cells. A soluble form of CD26/DPPIV has been described in serum. Over the past few years, several related enzymes with similar dipeptidyl peptidase activity have been discovered, raising questions on the molecular origin(s) of serum dipeptidyl peptidase activity. Among them attractin, the human orthologue of the mouse mahogany protein, was postulated to be responsible for the majority of the DPPIV‐like activity in serum. Using ADA‐affinity chromatography, it is shown here that 95% of the serum dipeptidyl peptidase activity is associated with a protein with ADA‐binding properties. The natural protein was purified in milligram quantities, allowing molecular characterization (N‐terminal sequence, glycosylation type, CD‐spectrum, pH and thermal stability) and comparison with CD26/DPPIV from other sources. The purified serum enzyme was confirmed as CD26.
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Cites
Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
Mentlein, R. (1999) · Regulatory Peptides · doi:10.1016/s0167-0115(99)00089-0 · Cited by 1,272
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Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26
Marguet, D., Baggio, L., Kobayashi, T., Bernard, A.-M., Pierres, M., Nielsen, P. F., Ribel, U., Watanabe, T., Drucker, D. J., & Wagtmann, N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.120069197 · Cited by 538
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Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes.
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CD26, let it cut or cut it down
De Meester, I., Korom, S., Van Damme, J., & Scharpé, S. (1999) · Immunology Today · doi:10.1016/s0167-5699(99)01486-3 · Cited by 451
Self-citationProteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV
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Cited by
Lambeir, A.-M., Durinx, C., Scharpé, S., & De Meester, I. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609354 · Cited by 955
Self-citationEnhancing Incretin Action for the Treatment of Type 2 Diabetes
Drucker, D. J. (2003) · Diabetes Care · doi:10.2337/diacare.26.10.2929 · Cited by 579
Cut to the chase: a review of CD26/dipeptidyl peptidase-4's (DPP4) entanglement in the immune system
Klemann, C., Wagner, L., Stephan, M., & von Hörsten, S. (2016) · Clinical and Experimental Immunology · doi:10.1111/cei.12781 · Cited by 425
Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders
GORRELL, M. D. (2005) · Clinical Science · doi:10.1042/cs20040302 · Cited by 334
Zaruba, M.-M., Theiss, H. D., Vallaster, M., Mehl, U., Brunner, S., David, R., Fischer, R., Krieg, L., Hirsch, E., Huber, B., et al. (2009) · Cell Stem Cell · doi:10.1016/j.stem.2009.02.013 · Cited by 301
Metadata
- Authors
- Durinx, C., Lambeir, A., Bosmans, E., Falmagne, J., Berghmans, R., Haemers, A., Scharpé, S., & De Meester, I.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 2000-09
- Volume
- 267
- Issue
- 17
- Pages
- 5608-5613
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1563993585
- Cited by
- 267
- References
- 44
- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Durinx, C., Lambeir, A., Bosmans, E., Falmagne, J., Berghmans, R., Haemers, A., Scharpé, S., & De Meester, I. (2000). Molecular characterization of dipeptidyl peptidase activity in serum: Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X‐Pro dipeptides. European Journal of Biochemistry. https://doi.org/10.1046/j.1432-1327.2000.01634.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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