Publication

Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

Santos Clemente, dos, G., van Waarde, A., F. Antunes, I., Dömling, A. & Elsinga, P. H., 25-Jul-2020, In : International Journal of Molecular Sciences. 21, 15, p. 1-36 36 p., 5291.

Research output: Contribution to journalReview articleAcademicpeer-review

APA

Santos Clemente, dos, G., van Waarde, A., F. Antunes, I., Dömling, A., & Elsinga, P. H. (2020). Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective. International Journal of Molecular Sciences, 21(15), 1-36. [5291]. https://doi.org/10.3390/ijms21155291

Author

Santos Clemente, dos, Gonçalo ; van Waarde, Aren ; F. Antunes, Ines ; Dömling, Alex ; Elsinga, Philip H. / Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective. In: International Journal of Molecular Sciences. 2020 ; Vol. 21, No. 15. pp. 1-36.

Harvard

Santos Clemente, dos, G, van Waarde, A, F. Antunes, I, Dömling, A & Elsinga, PH 2020, 'Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective', International Journal of Molecular Sciences, vol. 21, no. 15, 5291, pp. 1-36. https://doi.org/10.3390/ijms21155291

Standard

Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective. / Santos Clemente, dos, Gonçalo; van Waarde, Aren; F. Antunes, Ines ; Dömling, Alex; Elsinga, Philip H.

In: International Journal of Molecular Sciences, Vol. 21, No. 15, 5291, 25.07.2020, p. 1-36.

Research output: Contribution to journalReview articleAcademicpeer-review

Vancouver

Santos Clemente, dos G, van Waarde A, F. Antunes I, Dömling A, Elsinga PH. Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective. International Journal of Molecular Sciences. 2020 Jul 25;21(15):1-36. 5291. https://doi.org/10.3390/ijms21155291


BibTeX

@article{7ef02e9462554fff9540066541c09ad5,
title = "Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective",
abstract = "Arginase is a widely known enzyme of the urea cycle that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. The action of arginase goes beyond the boundaries of hepatic ureogenic function, being widespread through most tissues. Two arginase isoforms coexist, the type I (Arg1) predominantly expressed in the liver and the type II (Arg2) expressed throughout extrahepatic tissues. By producing L-ornithine while competing with nitric oxide synthase (NOS) for the same substrate (L-arginine), arginase can influence the endogenous levels of polyamines, proline, and NO•. Several pathophysiological processes may deregulate arginase/NOS balance, disturbing the homeostasis and functionality of the organism. Upregulated arginase expression is associated with several pathological processes that can range from cardiovascular, immune-mediated, and tumorigenic conditions to neurodegenerative disorders. Thus, arginase is a potential biomarker of disease progression and severity and has recently been the subject of research studies regarding the therapeutic efficacy of arginase inhibitors. This review gives a comprehensive overview of the pathophysiological role of arginase and the current state of development of arginase inhibitors, discussing the potential of arginase as a molecular imaging biomarker and stimulating the development of novel specific and high-affinity arginase imaging probes.",
keywords = "arginase, nitric oxide, arginase inhibitors, molecular imaging, positron emission tomography (PET)",
author = "{Santos Clemente, dos}, Gon{\c c}alo and {van Waarde}, Aren and {F. Antunes}, Ines and Alex D{\"o}mling and Elsinga, {Philip H.}",
year = "2020",
month = jul,
day = "25",
doi = "10.3390/ijms21155291",
language = "English",
volume = "21",
pages = "1--36",
journal = "International Journal of Molecular Sciences",
issn = "1422-0067",
publisher = "MDPI AG",
number = "15",

}

RIS

TY - JOUR

T1 - Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

AU - Santos Clemente, dos, Gonçalo

AU - van Waarde, Aren

AU - F. Antunes, Ines

AU - Dömling, Alex

AU - Elsinga, Philip H.

PY - 2020/7/25

Y1 - 2020/7/25

N2 - Arginase is a widely known enzyme of the urea cycle that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. The action of arginase goes beyond the boundaries of hepatic ureogenic function, being widespread through most tissues. Two arginase isoforms coexist, the type I (Arg1) predominantly expressed in the liver and the type II (Arg2) expressed throughout extrahepatic tissues. By producing L-ornithine while competing with nitric oxide synthase (NOS) for the same substrate (L-arginine), arginase can influence the endogenous levels of polyamines, proline, and NO•. Several pathophysiological processes may deregulate arginase/NOS balance, disturbing the homeostasis and functionality of the organism. Upregulated arginase expression is associated with several pathological processes that can range from cardiovascular, immune-mediated, and tumorigenic conditions to neurodegenerative disorders. Thus, arginase is a potential biomarker of disease progression and severity and has recently been the subject of research studies regarding the therapeutic efficacy of arginase inhibitors. This review gives a comprehensive overview of the pathophysiological role of arginase and the current state of development of arginase inhibitors, discussing the potential of arginase as a molecular imaging biomarker and stimulating the development of novel specific and high-affinity arginase imaging probes.

AB - Arginase is a widely known enzyme of the urea cycle that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. The action of arginase goes beyond the boundaries of hepatic ureogenic function, being widespread through most tissues. Two arginase isoforms coexist, the type I (Arg1) predominantly expressed in the liver and the type II (Arg2) expressed throughout extrahepatic tissues. By producing L-ornithine while competing with nitric oxide synthase (NOS) for the same substrate (L-arginine), arginase can influence the endogenous levels of polyamines, proline, and NO•. Several pathophysiological processes may deregulate arginase/NOS balance, disturbing the homeostasis and functionality of the organism. Upregulated arginase expression is associated with several pathological processes that can range from cardiovascular, immune-mediated, and tumorigenic conditions to neurodegenerative disorders. Thus, arginase is a potential biomarker of disease progression and severity and has recently been the subject of research studies regarding the therapeutic efficacy of arginase inhibitors. This review gives a comprehensive overview of the pathophysiological role of arginase and the current state of development of arginase inhibitors, discussing the potential of arginase as a molecular imaging biomarker and stimulating the development of novel specific and high-affinity arginase imaging probes.

KW - arginase

KW - nitric oxide

KW - arginase inhibitors

KW - molecular imaging

KW - positron emission tomography (PET)

U2 - 10.3390/ijms21155291

DO - 10.3390/ijms21155291

M3 - Review article

VL - 21

SP - 1

EP - 36

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 15

M1 - 5291

ER -

ID: 130026160