Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides

  title={Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides},
  author={Rolf Mentlein},
  journal={Regulatory Peptides},
  • R. Mentlein
  • Published 30 November 1999
  • Biology
  • Regulatory Peptides

Dipeptidyl-peptidase IV and aminopeptidase P: molecular switches of NPY/PYY receptor affinities

Cell-surface and soluble peptidases regulate the biological potency of neuropeptides, peptide hormones and chemokines by activation, partial inactivation and complete inactivation, and DPP IV appears to be of higher importance in humans.

The Role of Dipeptidyl Peptidase IV in the Cleavage of Glucagon Family Peptides

Results suggest that DP-IV plays a major role in the degradation of circulating PACAP38, a critical mediator of lipid and carbohydrate metabolism, and Oxyntomodulin and the growth hormone fragment were identified as new candidate in vivo substrates.

Dipeptidyl peptidase IV inhibition in animal models of diabetes.

DP IV rapidly cleaves the N-terminal dipeptide from a number of metabolic hormones and neuroendocrine factors including NPY, PYY, and the gluco-regulatory peptides glucagonlike peptide-1 (GLP-1), glucose-dependent insulinotropic polypeptides (GIP) and glucagon.

Peptide substrates of dipeptidyl peptidases.

This work wants to present some data on a novel DPP IV substrate, to review some of the recent literature on known substrates, and to discuss the possible truncation of known D PP IV substrates by related dipeptidyl peptidases.

Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides.

It is shown here that 95% of the serum dipeptidyl peptidase activity is associated with a protein with ADA-binding properties, and the purified serum enzyme was confirmed as CD26.

Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer.

Dipeptidyl-Peptidase IV from Bench to Bedside: An Update on Structural Properties, Functions, and Clinical Aspects of the Enzyme DPP IV

The role of DPP IV/CD26 within the immune system is a combination of its exopeptidase activity and its interactions with different molecules to serve as a co-stimulatory molecule to influence T cell activity and to modulate chemotaxis.

Downregulation of Signaling-active IGF-1 by Dipeptidyl Peptidase IV (DPP-IV)

It is reported here that DPP-IV cleaves the first two amino acids from insulin-like growth factor 1 (IGF-1), revealed by mass spectrometry, and the kinetic parameters of the proteolytic cleavage indicate that this reaction is physiologically relevant.

Different modes of dipeptidyl peptidase IV (CD26) inhibition by oligopeptides derived from the N-terminus of HIV-1 Tat indicate at least two inhibitor binding sites.

It is demonstrated that amino acid substitutions at different positions of Tat(1-9) can result in a change of the inhibition type, which gives new insights for the development of more potent and specific peptide-based DP IV inhibitors.

The Nonglycemic Actions of Dipeptidyl Peptidase-4 Inhibitors

Two important incretin hormones, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic peptide (GIP), enhance meal-stimulated insulin secretion from pancreatic β-cells, but are inactivated by DPP-4.



Amino-terminal Truncation of Chemokines by CD26/Dipeptidyl-peptidase IV

Proteolytic processing of RANTES by CD26/dipeptidyl-peptidase IV may constitute an important regulatory mechanism during anti-inflammatory and antiviral responses.

Dipeptidyl-peptidase IV-beta, a novel form of cell-surface-expressed protein with dipeptidyl-peptidase IV activity.

The results suggest that DPP IV-beta is a CD26-like protein which could be characterized by distinct properties.

The degradation of bioactive peptides and proteins by dipeptidyl peptidase IV from human placenta.

Kinetic constants were determined for the degradation of a number of other natural peptides, including substance P, the degradationOf which has been described earlier in a qualitative manner, generally, small peptides are degraded much more rapidly than proteins.

Regulation of the biological activity of glucagon-like peptide 2 in vivo by dipeptidyl peptidase IV

It is demonstrated that glucagon-like peptide 2 (GLP-2), shown to be highly intestinotrophic in mice, promotes an increase in intestinal villus height but has no trophic effect on small bowel weight in rats.

Truncation of Macrophage-derived Chemokine by CD26/ Dipeptidyl-Peptidase IV beyond Its Predicted Cleavage Site Affects Chemotactic Activity and CC Chemokine Receptor 4 Interaction*

NH2-terminal truncation of MDC by CD26/DPP IV has profound biological consequences and may be an important regulatory mechanism during the migration of Th2 lymphocytes and dendritic cells to germinal centers and to sites of inflammation.

Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes.

It is concluded that side effects of inhibition therapy are likely to be mild, and DPP-IV inhibition may be an effective supplement to diet and exercise treatment in attempts to prevent the deterioration of glucose metabolism associated with the Western lifestyle.

The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the collagen-binding site.

It is concluded that the putative collagen binding site of DPP IV is different from the region of the catalytic site containing the exopeptidase activity, which is located at the C-terminal portion of the molecule.

Dipeptidyl‐peptidase IV/CD26 on T cells: analysis of an alternative T‐cell activation pathway

CD26 is a proteolytic enzyme (dipeptidyl‐peptidase IV) with a wide tissue distribution and a unique specificity that was already described 27 years ago but is strongly upregulated following T‐cell activation.