Drug Database
AZ

aztreonam lysine (Cayston / Corus 1020 / AZLI)

✓ Approved

Gilead Sciences, Inc. · Small Molecule · Small Molecule

What is aztreonam lysine?

aztreonam lysine is a small molecule developed by Gilead Sciences, Inc.. It is approved for therapeutic indications via inhaled.

Drug Profile

Brand NamesCayston, Corus 1020, AZLI
CompanyGilead Sciences, Inc.
Drug ClassSmall Molecule
RouteInhaled
StatusApproved

Therapeutic Indications

aztreonam lysine is developed for 3 unique indications across 2 therapeutic areas.

Therapeutic AreaConditionPhase
Infections and infestationsRespiratory tract infection✓ Approved
Infections and infestationsPneumonia pseudomonal✓ Approved
Respiratory, thoracic and mediastinal disordersBronchiectasisPhase III

Related Research Articles

PubMedMolecular cancer2026-09-19

KMT9 drives T cell exclusion and dysfunction by promoting PMN-MDSCs infiltration and ARG1 expression in prostate cancer.

Peñarando Jon J, Willmann Dominica D, Sum Manuela M, Jia Yanhan Y et al.

Immunotherapy has emerged as a revolutionary therapeutic approach to treat cancer showing remarkable clinical responses. However, its efficacy in solid tumours such as prostate cancer (PCa) remains very limited due to a highly immunosuppressive tumour immune microenvironment (TIME) that hampers cytotoxic T cell infiltration and activity. Here, we show that lysine methyltransferase 9 (KMT9) governs the formation of an immunosuppressive TIME in PCa. KMT9 regulates the expression of tumour-secreted myeloid-attracting C-X-C motif chemokine receptor 2 (CXCR2) ligands such as C-X-C motif chemokine ligand 5 (CXCL5) thereby promoting the infiltration of immunosuppressive polymorphonuclear myeloid-derived suppressor cells (PMN-MDSCs) within tumours. These changes collectively result in decreased activation and exclusion of cytotoxic T cells from tumour glands. Furthermore, we demonstrate that KMT9 confers tumour cell-resistance to T cell cytotoxicity by regulating expression of arginase 1 (ARG1). Accordingly, KMT9α ablation results in inhibition of prostate tumour growth accompanied by a massive reduction of PMN-MDSC recruitment and a significant increase in cytotoxic T cell activation and infiltration of the prostate tumour glands. Together, we uncovered KMT9 as a regulator of immune evasion that promotes an immune-excluded TIME in prostate tumours. Furthermore, our findings establish KMT9 as a therapeutic target to reprogram the immunosuppressive landscape and potentially improve the clinical efficacy of current immunotherapies.

PubMedFrontiers in immunology2026-09-18

The role of lysine acylation in metabolic dysregulation and inflammatory responses within the hepatic immune microenvironment of MASLD.

Peng Jingyi J, Yan Ankangxin A, Chen Guanglei G, Gao Xiaojiao X et al.

Metabolic dysfunction-associated steatotic liver disease (MASLD) is a chronic liver disorder characterized by metabolic abnormalities, persistent low-grade inflammation, and alterations in hepatic immune function. In addition to lipid accumulation and dysregulated energy metabolism, metabolism-associated post-translational modifications of proteins may also contribute to the initiation and progression of MASLD. Among these modifications, lysine acylation is regulated by the availability and composition of intracellular acyl-CoA species, as well as the activities of acyltransferases and deacylases, and can modulate metabolic enzyme activity, inflammatory signaling pathways, and gene transcription. This review summarizes the interplay between metabolic dysregulation and lysine acylation in MASLD, with particular emphasis on how gut-derived metabolites, disturbances in hepatic glycolipid metabolism, and alterations in subcellular metabolic environments influence the formation of distinct lysine acylation modifications. Furthermore, from the perspectives of hepatocytes, macrophages, hepatic stellate cells, and liver sinusoidal endothelial cells, we discuss the potential roles of lysine acylation in cellular injury, inflammatory responses, hepatic stellate cell activation, and liver fibrosis. In addition, we highlight the current progress regarding the potential of lysine acylation as a biomarker and therapeutic target, and propose that integrated approaches involving metabolic tracing, spatial omics, and site-specific genome editing may further elucidate the functional significance of key acylation events in MASLD. Overall, lysine acylation is closely associated with metabolic disturbances, hepatic inflammation, and fibrogenic processes in MASLD. A deeper understanding of cell type-specific regulatory acylation sites will facilitate the evaluation of their potential applications as biomarkers and therapeutic targets for MASLD.

PubMedACS omega2026-09-18

Hybrid 3D Printing of Interfacial Polyelectrolyte Complex Formed between Hyaluronic Acid and Poly-L-lysine Hydrogels.

Huang Yi-Chen YC, Li Ming-Chia MC

Hyaluronic acid (HA), a principal component of the extracellular matrix (ECM), exhibits excellent biocompatibility, high water-retention capacity, and inherent biodegradability. α-Poly-L-lysine (PLL), a cationic polypeptide with favorable biocompatibility, is widely employed for surface modification to promote cell adhesion and proliferation. Electrostatic interactions between oppositely charged polyelectrolytes enable the formation of interfacial polyelectrolyte complexes (IPC) in the absence of chemical cross-linking agents. In this study, IPC hydrogels were fabricated from HA and PLL and processed via a combination of hybrid and gravity-compensated embedded three-dimensional (3D) printing techniques to generate both two-dimensional (2D) and 3D scaffolds for tissue engineering applications. Using this approach, anisotropic 2D membranes with submicrometer groove topographies were produced, together with mechanically stable 3D fibrous architectures. The resulting IPC hydrogels retained structural integrity under aqueous conditions, demonstrating high morphological controllability and highlighting their substantial potential as scaffolding materials in tissue engineering.

PubMedVeterinary and animal science2026-09-18

Gut microbial signatures in poultry under low-protein diets and lysine restriction: implications for precision nutrition.

Salahi Ahmad A, El-Ghany Wafaa A Abd WAA

Three key signatures - microbial, nutritional, and epigenetic - are pivotal in nutrigenomics, mediating poultry responses to nutritional signals, such as low-protein diets (LPDs) and lysine restriction (LR). These multidimensional signatures - encompassing bacterial, archaeal, and fungal taxonomy, functional genes, and metabolomic profiles (short-chain fatty acids; SCFAs) - orchestrate host metabolism, immunity, and feed conversion ratio (FCR). This PRISMA-ScR scoping review synthesizes multi-omics evidence showing that LPDs shift cecal fermentation toward saccharolytic pathways, enriching butyrate-producing taxa (Ruminococcaceae, Lachnospiraceae) while suppressing Proteobacteria and toxic proteolytic metabolites (ammonia, branched-chain fatty acids). LR elevates Actinobacteria/Synergistetes, triggers microbial nitrogen limitation, and reconfigures SCFA profiles through cross-feeding, thereby activating host nutrient sensors (mTOR downregulation, GCN2 upregulation) to prioritize immunity and FCR gains. Methanogenic archaea (Methanobrevibacter) fine-tune hydrogen economies, although diet-induced changes require deeper exploration. Key signatures forecast performance, featuring optimized Firmicutes/Bacteroidetes ratios and ureolytic genes (gdhA/glnA) as markers of protein resilience and profiles for breed-specific responses. SCFAs drive epigenetics (HDAC suppression, histone acetylation) and immunometabolism (Treg expansion, NF-κB dampening), bridging microbiome to host benefits via gut-liver interplay. Emerging applications span next-generation probiotics (NGPs) and live biotherapeutic products (LBPs), tailored from signature consortia (L. reuteri + B. velezensis) or archaeal agents, to sustain diet-induced states in antibiotic-free regimens. Major gaps persist in causal multi-omics validation, breed-specific responses, standardized baselines, and archaeal contributions. Integrating LPD/LR with tailored NGPs/LBPs promises precision nutrition strategies that enhance nitrogen utilization, reduce emissions, and improve welfare. Gnotobiotic, FMT, and AI trials are essential for translating microbial signatures into scalable flock-level precision management.

PubMedFrontiers in molecular neuroscience2026-09-18

KAT5: the epigenetic regulator of central nervous system diseases.

Xin Xiaoming X, Wu Lingjuan L, Liu Meichen M, Liu Tian T et al.

Abnormal epigenetic modifications are involved in central nervous system (CNS) diseases. Histones play a crucial role in chromatin structure and function, whose post-translational modifications significantly impact gene expression and chromatin dynamics. Histone acetylation, governed by the balance between histone acetyltransferases (HATs) and histone deacetylases (HDACs), is one of the key modulators of chromatin accessibility and transcriptional activity. Lysine acetyltransferase 5 (KAT5, aka TIP60), a member of the MYST subfamily of HATs, is involved in many cellular processes, including DNA repair, apoptosis, and cell cycle control. Notably, the dysfunction of KAT5 has been implicated in several CNS diseases. In this review, we explored the roles of KAT5 in CNS pathophysiology, emphasizing its involvement in neurological disorders and its potential as a therapeutic target. This review sheds light on the epigenetic mechanisms in CNS diseases mediated by KAT5 and provides valuable information for potential treatment strategies.

PubMedFrontiers in oncology2026-09-18

Inhibition of histone acetyltransferase KAT7 suppresses proliferation and migration of breast cancer cells.

Du Wei W, Xiao Xiaoyu X, Zhang Jiaxin J, Shi Zhongxin Z et al.

Lysine acetyltransferase 7 (KAT7), also known as HBO1 or MYST2, is highly expressed in multiple cancers. This study aims to explore the expression patterns of KAT7 in breast cancer and its impact on phenotypes of breast cancer cells. The expression of KAT7 and the overall survival of patients were analyzed using the online bioinformatics platform GEPIA2. Immunohistochemistry was applied to detect KAT7 protein expression in breast cancer specimens (94 breast cancer tissues and 12 adjacent normal tissues). KAT7 shRNA plasmids were used to inhibit KAT7 expression in MCF-7 and MDAMB231 cells, and this inhibition was verified by western blot analysis. Cell counting kit-8 (CCK8), colony formation, and transwell migration assays were employed to assess the proliferation and migration of breast cancer cells. KAT7 was highly expressed in breast cancer and correlated with poor patient prognosis. KAT7 expression was significantly higher in breast cancer than in adjacent non-cancerous tissue. 67 of 94 breast cancer samples tested positive for KAT7. KAT7 was significantly negatively correlated with estrogen receptor (ER), progesterone receptor (PR), and Ki67, and was significantly positively correlated with human epidermal growth factor receptor 2 (HER2). KAT7 expression is strongly associated with tumor subtypes. Inhibition of KAT7 significantly suppressed growth, clonogenic formation, and migration in MCF-7 and MDAMB231 cells. Our findings demonstrate that KAT7 was highly expressed in breast cancer, and inhibition of KAT7 suppressed proliferation and migration of breast cancer cells.

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