Last update 01 Nov 2024

TPI1

Last update 01 Nov 2024

Basic Info

Synonyms

Methylglyoxal synthase, TIM, TPI

+ [4]

Introduction

It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.

Drugs associated with TPI1

CN117586405

Patent Mining

Target

TPI1

Mechanism-

Active Org.

Lanzhou University

Originator Org.

Lanzhou University

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

RT-001(RetinaPharma)

Target

TPI1

Mechanism

TPI1 inhibitors

Active Org.-

Originator Org.

RetinaPharma Technologies, Inc.

Active Indication-

Inactive Indication

Glaucoma [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with TPI1

100 Translational Medicine associated with TPI1

0 Patents (Medical) associated with TPI1

3,341

Literatures (Medical) associated with TPI1

01 Jan 2025·Talanta

Four-dimensional trapped ion mobility spectrometry proteomics reveals circulating extracellular vesicles encapsulated drivers of nasopharyngeal carcinoma distant dissemination

Article

Author: Qu, Song ; Li, Kaiguo ; Chen, Xuxia ; Chen, Weiling ; Yang, Liu ; Liu, Yang ; Lu, Pingan

Nasopharyngeal carcinoma (NPC) is a head and neck cancer with a high propensity for early metastatic spread. Emerging evidence shows that extracellular vesicles (EVs) are key players in cancer metastasis, but their role in NPC metastasis remains poorly understood. We here present the first description of the proteomic and functional profiles of serum-derived circulating small EVs in metastatic NPC patients. To enhance the capture of low-abundance signaling proteins in EVs, timsTOF-based four-dimensional label-free quantitative proteomics was employed. We found that metastatic NPC patients (M-NPC-EVs) exhibited the highest serum EV levels compared to locoregional patients (L-NPC-EVs) and healthy subjects (Normal-EVs). The proteome of M-NPC-EVs differed substantially from L-NPC-EVs and was functionally enriched in pathways regulating cell polarity and motility, glucose metabolism, and angiogenesis. Functional assays testing individual EV samples demonstrated that M-NPC-EVs pronouncedly enhanced NPC cell migration, invasion, and the formation of lamellipodia and filopodia in vitro, and promoted angiogenesis in subcutaneous Matrigel plugs in vivo. In silico analyses suggested that PTPRA, TPI1 and GPI highly enriched in M-NPC-EVs were putative drivers underlying the motogenic and angiogenic activities of M-NPC-EVs, and their high expression levels were associated with a poor prognosis of NPC patients. The increased expression of PTPRA, TPI1 and GPI in M-NPC-EVs was then validated in an independent cohort consisting of 175 NPC patients (locoregional n = 114; metastatic n = 61). Together, utilizing patient-derived EVs, we mimicked the potential pro-metastatic functions of EVs in NPC patients in vitro and in vivo and provided novel insights into their bioactive cargoes.

31 Dec 2024·Autoimmunity

LDHA-induced histone lactylation mediates the development of osteoarthritis through regulating the transcription activity of TPI1 gene

Article

Author: Qiao, Zongrui ; Xia, Junfeng ; Hao, Xiao ; Zhang, Yin

Osteoarthritis (OA) is a worldwide joint disease, leading to the physical pain, stiffness, and even disability. Lactate dehydrogenase A (LDHA) is known as a lactylation mediator that can regulate histone lactylation of its target genes. However, the role of LDHA-mediated histone H3 lysine 18 lactylation (H3K18la) in OA progression is yet to be clarified. Our study aims at revealing the role and mechanism of LDHA-mediated histone lactylation in the glycolysis of chondrocytes. In this study, we determined at first that the H3K18la level was enhanced in OA. Energy metabolism such as glycolysis is often altered in OA progress. Therefore, we further explored the mechanism mediating glycolysis and thus promoting OA progress. Moreover, glycolysis was enhanced in LPS-induced OA cell model, as evidenced by the increased glucose consumption and lactate production. Furthermore, we silenced LDHA for loss-of-function assays. The results showed that knockdown of LDHA suppressed glycolysis of LPS-induced chondrocytes. In vivo animal study demonstrated that knockout of LDHA recovered cartilage injury of OA mice. Mechanistically, we uncovered that LDHA-mediated H3K18la in TPI1 promoter enhanced the transcription activity of TPI1. Mutation of K69 site was found to ameliorate LPS-induced glycolysis in OA cell model. In conclusion, our study reveals the role of LDHA-mediated H3K18la of TPI1 promoter in OA progress.

01 Dec 2024·Journal of Global Antimicrobial Resistance

Multi-omics analysis explores the impact of ofloxacin pressure on the metabolic state in Escherichia coli

Article

Author: Yao, Hailan ; Feng, Miao ; Wang, Shuowen ; He, Feng ; Xiao, Zonghui ; Yi, Xiaoyu ; Wang, Yichuan

OBJECTIVESThe rising threat of antibiotic resistance poses a significant challenge to public health. The research on the new direction of resistance mechanisms is crucial for overcoming this hurdle. This study examines metabolic changes by comparing sensitive and experimentally induced ofloxacin-resistant Escherichia coli (E. coli) strains using multi-omics analyses, aiming to provide novel insights into bacterial resistance.METHODSAn ofloxacin-resistant E. coli strain was selected by being exposed to high concentration of ofloxacin. Comparative analyses involving transcriptomics, proteomics, and acetylomics were conducted between the wild-type and the ofloxacin-resistant (Re-OFL) strains. Enrichment pathways of differentially expressed genes, proteins and acetylated proteins between the two strains were analysed using gene ontology and Kyoto Encyclopedia of Genes and Genomes method. In addition, the metabolic network of E. coli was mapped using integrated multi-omics analysis strategies.RESULTSWe identified significant differences in 2775 mRNAs, 1062 proteins, and 1015 acetylated proteins between wild-type and Re-OFL strains. Integrated omics analyses revealed that the common alterations enriched in metabolic processes, particularly the glycolytic pathway. Further analyses demonstrated that 14 metabolic enzymes exhibited upregulated acetylation levels and downregulated transcription and protein levels. Moreover, seven of these metabolic enzymes (fba, tpi, gapA, pykA, sdhA, fumA, and mdh) were components related to the glycolytic pathway.CONCLUSIONSThe changes of metabolic enzymes induced by antibiotics seem to be a key factor for E. coli to adapt to the pressure of antibiotics, which shed new light on understanding the adaptation mechanism when responding to ofloxacin pressure.

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TPI1

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