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- OATD-02 / Molecure
An open-label, multicentre, dose-escalation, first-in-human phase I study to evaluate safety, tolerability and antineoplastic activity of OATD-02 (dual arginase 1 and arginase 2 inhibitor) in patients with selected advanced and/or metastatic solid tumors () - Jul 27, 2023 - Abstract #ESMO2023ESMO_2290;
P1
The study is ongoing. Clinical trial information: NCT05759923.
- | paricalcitol / Generic mfg.
Journal: Tubular Elabela-APJ axis attenuates ischemia-reperfusion induced acute kidney injury and the following AKI-CKD transition by protecting renal microcirculation. (Pubmed Central) - Jun 27, 2023
An endogenous tubular ELA-APJ axis regulates renal microvascular blood flow that plays a pivotal role in I/R-induced AKI. Furthermore, improving renal blood flow by inhibiting ARG2 and activating PGE2 is an effective treatment for AKI and prevents the subsequent AKI-CKD transition.
- | OATD-02 / Molecure
Journal: OATD-02 Validates the Benefits of Pharmacological Inhibition of Arginase 1 and 2 in Cancer. (Pubmed Central) - Aug 27, 2022
OATD-02 represents a very promising drug candidate for the combined treatment of tumours, and is the only pharmacological tool that can effectively address the benefits of ARG1/ARG2 inhibition. OATD-02 will enter clinical trials in cancer patients in 2022.
- | Journal: Resolvin D1 Suppresses HO-Induced Senescence in Fibroblasts by Inducing Autophagy through the miR-1299/ARG2/ARL1 Axis. (Pubmed Central) - Dec 27, 2021
Taken together, the miR-1299/ARG2/ARL1 axis emerges as a novel mechanism of the ARG2-induced inhibition of autophagy. Furthermore, these results indicate that miR-1299 and pro-resolving lipids, including RvD1, are likely involved in inhibiting cellular senescence by inducing autophagy.
- | C0021158 / AstraZeneca, Cancer Research UK
Journal, IO biomarker: Structural and functional characterization of C0021158, a high-affinity monoclonal antibody that inhibits Arginase 2 function via a novel non-competitive mechanism of action. (Pubmed Central) - Jul 7, 2021
In silico molecular docking simulations predict that L-arginine is unable to bind effectively when antibody is bound, a prediction supported by isothermal calorimetry experiments using an L-arginine mimetic. Specifically, targeting ARG2 in the tumor microenvironment through the application of C0021158, potentially in combination with standard chemotherapy regimens or alternate immunotherapies, represents a potential new strategy to target immune cold tumors.
- | Journal: Selective inhibition of arginase-2 in endothelial cells but not proximal tubules reduces renal fibrosis. (Pubmed Central) - Jun 10, 2021
Furthermore, arginase inhibition restored kidney nitric oxide (NO) levels, oxidative stress, and mitochondrial function following UUO.These findings indicate that endothelial-Arg2 plays a major role in renal fibrosis via its action on NO and mitochondrial function. Blocking Arg2 activity or expression could be a novel therapeutic approach for prevention of CKD.
- C0021158 / AstraZeneca, Cancer Research UK
[VIRTUAL] Development of a first-in-class Arginase 2 inhibitory monoclonal antibody that restores T cell proliferation in vitro () - Nov 19, 2020 - Abstract #NCRI2020NCRI_103;
Conclusion Specifically, targeting ARG2 in the tumor microenvironment through the application of the novel ARG2 inhibitory antibody C0021158, potentially in combination with standard chemotherapy regimens or alternate immunotherapies, represents a potential new strategy to target immune cold tumors. Impact statement This is the first report of an antibody which can bind to and inhibit the activity of arginase 2 which has been implicated in multiple diseases, in particular those diseases where arginase expression contributes to creating an immune-privileged niche.
- | Journal: Extensive sequence and structural evolution of Arginase 2 inhibitory antibodies enabled by an unbiased approach to affinity maturation. (Pubmed Central) - Sep 8, 2020
The extensive sequence changes resulting from this approach were translated into striking structural changes for parent and affinity-matured antibodies bound to ARG2, with a large reorientation of the binding paratope facilitating increases in contact surface and shape complementarity to the antigen. The considerable gains in therapeutic properties seen from extensive sequence and structural evolution of the parent ARG2 inhibitory antibody clearly illustrate the advantages of the unbiased approach developed, which was key to the identification of high-affinity antibodies with the desired inhibitory potency and specificity.
- | Journal: Homoarginine and inhibition of human arginase activity: kinetic characterization and biological relevance. (Pubmed Central) - Sep 26, 2019
In partial correlation analysis, plasma HOMOARG was not associated with ARG (P = 0.38) or ARG/ORN ratio (P = 0.73) in older adults. Our results suggest that arginase inhibition is unlikely to play a significant role in the reported cardio-protective effects of HOMOARG.
- OATD-02 / OncoArendi
Targeting ARG2 as a novel therapeutic approach for cancer (Poster Area (Hall 4)) - Sep 11, 2019 - Abstract #ESMO2019ESMO_2724;
Thus, OATD-02 is a very promising compound for the treatment of hypoxic tumors which are particularly resistant to therapies. Legal entity responsible for the study: OncoArendi Therapeutics SA.