AZIN2

Last update 08 May 2025

Basic Info

Synonyms

ADC, Antizyme inhibitor 2, ARGDC

+ [11]

Introduction

Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:17900240). Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:17900240). Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (PubMed:20188728).

100 Clinical Results associated with AZIN2

100 Translational Medicine associated with AZIN2

0 Patents (Medical) associated with AZIN2

545

Literatures (Medical) associated with AZIN2

01 Mar 2025·Experimental Dermatology

Altered Arginine Metabolism Affects Proliferation and Radiosensitivity of Keloids

Article

Author: Zhang, Yange ; Xiao, Haitao ; Zhang, Shuyu ; Xu, Xuewen ; Li, Wei ; Zhu, Baochen ; Li, Xiaoqian

ABSTRACTKeloid is characterised by the reprogramming of cellular metabolism, wherein keloid cells adapt their metabolic pathways to meet the demands for energy and biosynthetic precursors. Investigating the intricate relationship between cellular metabolism and the biological behaviour of keloid holds the potential to yield novel therapeutic strategies for keloid. To elucidate the molecular alterations and potential underlying regulatory mechanisms in keloids, we created comprehensive metabolic profiling at the pathway level by analysing metabolomic, transcriptomic and single‐cell RNA‐sequencing data from keloids and adjacent skin. Viability assay and clonogenic assay were performed to validate the function of the metabolic pathway(s) in primary keloid fibroblast cells. Integrated analysis revealed an upregulation of arginine and proline metabolism in keloids. According to single‐cell RNA‐seq data, elevated expression of genes related to arginine and proline metabolism, such as P4HA3, P4HA2, P4HA1, PYCR1, OAT and ASS1, was predominately highly expressed in fibroblast‐2. Fibroblast‐2 displayed more obvious phenotypes of mesenchymal fibroblast. Critical genes from integrated analysis including P4HA3, P4HA2, P4HA1, PYCR1 and AZIN2, and metabolites including fumaric acid and 2‐oxo‐5‐amino‐pentanoic acid showed prognostic relevance with disease‐free survival of keloid. Additionally, an In vitro study showed that arginine deprivation therapy (ADT) inhibited and radiosensitised the proliferation of keloid‐derived fibroblasts. In conclusion, our thorough multiomics study deepens our understanding of the link between arginine and proline metabolism and keloid proliferation and radiosensitivity. Elevated activity of arginine and proline metabolism in mesenchymal fibroblasts may be a potential therapeutic pathway for keloid.

01 Jan 2025·Physiologia Plantarum

LDL2 and PAO5 genes are essential for systemic acquired resistance in Arabidopsis thaliana

Article

Author: Nandi, Ashis Kumar ; Saxena, Shobhita ; Roy, Shweta ; Ahmad, Mir Nasir

AbstractA partly infected plant becomes more resistant to subsequent infections by developing systemic acquired resistance (SAR). Primary infected tissues produce signals that travel to systemic tissues for SAR‐associated priming of defense‐related genes. The mechanism through which mobile signals contribute to long‐lasting infection memory is mostly unknown. RSI1/FLD, a putative histone demethylase, is required for developing SAR. Here, we report that two other FLD homologs, LSD1‐LIKE2 (LDL2) and POLYAMINE OXIDASE 5 (PAO5), are required for SAR development. The mutants of LDL2 and PAO5 are not defective in local resistance but are specifically impaired for SAR. The mutants are defective in salicylic acid accumulation and priming of defence‐related genes such as PR1, FMO1, and SnRK2.8. LDL2 and PAO5 are expressed in systemic tissues upon SAR induction by pathogens or SAR mobile signal azelaic acid. The ldl2 and pao5 mutants generate SAR mobile signals like wild‐type (WT) plants but fail to respond to the signal at the systemic leaves. Both LDL2 and PAO5 proteins contain polyamine oxidase (PAO) domains, suggesting their involvement in polyamine metabolism. Exogenous applications of polyamines such as spermine and spermidine activate SAR in WT and rescue SAR defects of ldl2 and pao5 plants. Inhibition of polyamine biosynthetic gene arginine decarboxylase blocks SAR development. Results altogether demonstrate specific non‐redundant roles of LDL2 and PAO5 in SAR development with their possible involvement in polyamine metabolism.

01 Dec 2024·Plant Science

Spatial organization of putrescine synthesis in plants

Article

Author: Morris, Paul F ; Ahmed, Sheaza ; Avestakh, Arefeh ; Joshi, Kumud ; Kalinoski, Andrea ; Ge, Lingxiao ; Oloyede, Babatunde ; Phuntumart, Vipaporn ; Morris, Paul F.

Three plant pathways for the synthesis of putrescine have been described to date. These are the synthesis of putrescine from ornithine, by ornithine decarboxylase (ODC); the synthesis of putrescine from arginine by arginine decarboxylase, agmatine iminohydrolase (AIH) and N-carbamoylputrescine amidohydrolase (NLP1); and arginine decarboxylase and agmatinase. To address how these pathways are organized in plants, we have used transient expression analysis of these genes in the leaves of Nicotiana benthamiana. Brassicas do not have ODC, but the single ODC gene from rice and one of the soybean genes, were localized to the ER. Transient expression of the rice agmatinase gene showed that it was localized to the mitochondria. In A. thaliana there are five isoforms of AIH and three isoforms of NLP1. Stable GFP-tagged transformants of the longest isoforms of AIH and NLP1 showed that both proteins were localized to the ER, but in tissues with chloroplasts, the localization was concentrated to lamellae adjacent to chloroplasts. Transient expression analyses showed that four of the isoforms of AIH and all of the isoforms of NLP1 were localized to the ER. However, AIH.4 was localized to the chloroplast. Combining these results with other published data, reveal that putrescine synthesis is excluded from the cytoplasm and is spatially localized to the chloroplast, ER, and likely the mitochondria. Synthesis of putrescine in the ER may facilitate cell to cell transport via plasmodesmata, or secretion via vesicles. Differential expression of these pathways may enable putrescine-mediated activation of hormone-responsive genes.

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AZIN2

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