Pregled bibliografske jedinice broj: 1266555
Role of dipeptidyl peptidase III in pain regulation through cleavage of neuropeptides
Role of dipeptidyl peptidase III in pain regulation through cleavage of neuropeptides // 7th Croatian Meeting of Chemists and Chemical Engineers and 5th Symposium Vladimir Prelog : Book of Abstracts / Marković, Dean ; Meštrović, Ernest ; Namjesnik, Danijel ; Tomašić, Vesna (ur.).
Zagreb: Hrvatsko kemijsko društvo, 2021. str. 234-234 (poster, nije recenziran, neobjavljeni rad, znanstveni)
CROSBI ID: 1266555 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Role of dipeptidyl peptidase III in pain regulation
through cleavage of neuropeptides
Autori
Karačić, Zrinka ; Šupljika, Filip ; Tomašić Paić, Ana ; Brkljačić, Lidija ; Tomić, Sanja
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, neobjavljeni rad, znanstveni
Izvornik
7th Croatian Meeting of Chemists and Chemical Engineers and 5th Symposium Vladimir Prelog : Book of Abstracts
/ Marković, Dean ; Meštrović, Ernest ; Namjesnik, Danijel ; Tomašić, Vesna - Zagreb : Hrvatsko kemijsko društvo, 2021, 234-234
Skup
27. hrvatski skup kemičara i kemijskih inženjera (27HSKIKI)
Mjesto i datum
Veli Lošinj, Hrvatska, 05.10.2021. - 08.10.2021
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
Dipeptidyl peptidase III ; Neuropeptide ; Hemorphin-4 ; Isothermal titration calorimetry (ITC) ; Enzyme kinetics
Sažetak
Dipeptidyl peptidase III (DPP III) is a zinc- dependent exopeptidase that hydrolyses dipeptides from the N-terminus of endogenous peptides, such as angiotensin II, enkephalins and endomorphins. [1] It is widely expressed in human tissues, but its colocalization with opioid peptides in the central nervous system suggest a role for this enzyme in the mammalian endogenous pain regulation system.[2] To identify new peptide substrates of DPP III, we used HPLC-MS to quantify enzymatic activity of human DPP III towards a selected list of untested neuropeptides, as well as known DPP III substrates. Peptide binding affinity was analysed using isothermal titration calorimetry (ITC), and we measured an entropic contribution characteristic for DPP III for all peptides cleaved by the enzyme. We show here that hemorphin-4, valorphin, Leu-valorphin-Arg and β- casomorphin are cleaved by the enzyme, while vasopressin, hemopressin and β-neoendorphin are not substrates of human DPP III. Hemorphin-4 and valorphin are opioid peptides with antinociceptive properties, derived from proteolytic cleavage of hemoglobin.[3] The value for KD of valorphin is similar to that of angiotensin II, and KD of hemorphin-4 is similar to that of endomorphin-2. In addition, we attempt to directly measure the kinetic parameters for peptide cleavage using HPLC-MS. Our results should help to clarify the role of DPP III in pain regulation. [1] J.M. Chen, A. Barrett, Handbook of Proteolytic Enzymes, Vol. 1, Academic Press, 2004, 809-12. [2] T. Chiba, Y.H. Li, T. Yamane, O. Ogikubo, M. Fukuoka, R. Arai, S. Takahashi, T. Ohtsuka, I. Okhubo, N. Matsui, Peptides 2003, 24, 773-8. [3] F. Nyberg, K. Sanderson, E.-L. Glämsta, Peptide Science, 1997, 43, 147-156.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
HRZZ-IP-2018-01-2936 - Biološka važnost dipeptidil peptidaze III i njezin utjecaj na zdravlje čovjeka (DPP3BioRe) (Tomić, Sanja, HRZZ - 2018-01) ( CroRIS)
Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb,
Institut "Ruđer Bošković", Zagreb
Profili:
Lidija Brkljačić (autor)
Ana Tomašić Paić (autor)
Zrinka Karačić (autor)
Sanja Tomić (autor)
Filip Šupljika (autor)