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Pregled bibliografske jedinice broj: 1266555

Role of dipeptidyl peptidase III in pain regulation through cleavage of neuropeptides


Karačić, Zrinka; Šupljika, Filip; Tomašić Paić, Ana; Brkljačić, Lidija; Tomić, Sanja
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

Poveznice na cjeloviti tekst rada:

27hskiki.hkd.hr

Citiraj ovu publikaciju:

Karačić, Zrinka; Šupljika, Filip; Tomašić Paić, Ana; Brkljačić, Lidija; Tomić, Sanja
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)
Karačić, Z., Šupljika, F., Tomašić Paić, A., Brkljačić, L. & Tomić, S. (2021) Role of dipeptidyl peptidase III in pain regulation through cleavage of neuropeptides. U: Marković, D., Meštrović, E., Namjesnik, D. & Tomašić, V. (ur.)7th Croatian Meeting of Chemists and Chemical Engineers and 5th Symposium Vladimir Prelog : Book of Abstracts.
@article{article, author = {Kara\v{c}i\'{c}, Zrinka and \v{S}upljika, Filip and Toma\v{s}i\'{c} Pai\'{c}, Ana and Brklja\v{c}i\'{c}, Lidija and Tomi\'{c}, Sanja}, year = {2021}, pages = {234-234}, keywords = {Dipeptidyl peptidase III, Neuropeptide, Hemorphin-4, Isothermal titration calorimetry (ITC), Enzyme kinetics}, title = {Role of dipeptidyl peptidase III in pain regulation through cleavage of neuropeptides}, keyword = {Dipeptidyl peptidase III, Neuropeptide, Hemorphin-4, Isothermal titration calorimetry (ITC), Enzyme kinetics}, publisher = {Hrvatsko kemijsko dru\v{s}tvo}, publisherplace = {Veli Lo\v{s}inj, Hrvatska} }
@article{article, author = {Kara\v{c}i\'{c}, Zrinka and \v{S}upljika, Filip and Toma\v{s}i\'{c} Pai\'{c}, Ana and Brklja\v{c}i\'{c}, Lidija and Tomi\'{c}, Sanja}, year = {2021}, pages = {234-234}, keywords = {Dipeptidyl peptidase III, Neuropeptide, Hemorphin-4, Isothermal titration calorimetry (ITC), Enzyme kinetics}, title = {Role of dipeptidyl peptidase III in pain regulation through cleavage of neuropeptides}, keyword = {Dipeptidyl peptidase III, Neuropeptide, Hemorphin-4, Isothermal titration calorimetry (ITC), Enzyme kinetics}, publisher = {Hrvatsko kemijsko dru\v{s}tvo}, publisherplace = {Veli Lo\v{s}inj, Hrvatska} }




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