By Ingrid De Meester, Anne-Marie Lambeir, Paul Proost, Simon Scharpé (auth.), Nathan Back, Irun R. Cohen, David Kritchevsky, Abel Lajtha, Rodolfo Paoletti (eds.)
Proceedings of the overseas convention on Dipeptidyl Aminopeptidases, held September 26-28, 2002, in Berlin, Germany.
Dipeptidyl Aminopeptidases exert a effective modulatory position at an interface among immune mechanisms, metabolic responses and neuroendocrine pathways. Experimental types and medical reviews addressing the position of those enzymes and the impression of particular inhibitors pave how one can novel healing thoughts in immunology, rheumatology, oncology, reproductive medication and diabetes.
Leading specialists during this box have contributed to this e-book which provides a cutting-edge view on those enzymes, at a time whilst our realizing in their functionality is growing to be ever extra speedily and healing strategies turn into drawing close. The sections of the publication specialise in numerous issues:
- constitution and serve as of dipeptidyl aminopeptidases,
- DPP IV-like proteins,
- Immune mechanisms and immune problems,
- melanoma and angiogenesis,
- Diabetes and metabolism,
- healing implications.
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Extra resources for Dipeptidyl Aminopeptidases in Health and Disease
The effect appears to be caused by differences in the active sites of the enzymes since the correlation with the electron withdrawing properties of the substituents is maintained. In conclusion: This comparative study revealed both subtle and striking differences between two highly homologous enzymes. The results may provide a starting point for the development of selective inhibitors. They also raise some questions concerning the catalytic machinery of DPP IV that deserve more attention. ACKNOWLEDGEMENTS This work was supported by a research grant from the University of Antwerp and by the National Fund for Scientific Research Flanders.
Heidelberg: Springer-Verlag. 24. , 1998, Rat dipeptidyl peptidase IV (DPP IV) exhibits endopeptidase activity with specificity for denatured fibrillar collagens. FEBS Lett. 428: 152-6. 25. , 2002, Metformin effects on dipeptidylpeptidase IV degradation of glucagon- like peptide-1. Commun. 291: 1302-8. 26. , 1993, Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Pept. 49: 133-44. 27. , 1996, Investigation of glucose-dependent insulinotropic polypeptide-(l-42) and glucagon-like peptide-1-(7-36) degradation in Dipeptidyl Peptidase IV Substrates 28.
3. KINETIC STUDY OF THE IN VITRO TRUNCATION OF BIOACTIVE PEPTIDES BY DIPEPTIDYL-PEPTIDASE IV The in vitro kinetic study of the truncation of bioactive peptides by DPPIV/CD26 resulted in the identification of several excellent substrates with high specificity constants (see figure). Several conclusions concerning the substrate specificity of DPPIV can be drawn from in vitro kinetic studies. The amino acid sequence surrounding the scissile bond is not the only determinant for selectivity. Specific structural features of the substrate influence the catalytic parameters.