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Last update 23 Jan 2025

TXNDC12

Last update 23 Jan 2025

Basic Info

Synonyms

AGR1, Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19

+ [12]

Introduction

Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol-disulfide oxidase activity.

Drugs associated with TXNDC12

HG-1245

Target

TXNDC12

Mechanism

TXNDC12 modulators

Active Org.-

Originator Org.

Human Genome Sciences, Inc.

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with TXNDC12

100 Translational Medicine associated with TXNDC12

0 Patents (Medical) associated with TXNDC12

147

Literatures (Medical) associated with TXNDC12

01 Nov 2024·Fish & Shellfish Immunology

Insights into the functional properties of thioredoxin domain-containing protein 12 (TXNDC12): Antioxidant activity, immunological expression, and wound-healing effect in yellowtail clownfish (Amphiprion clarkii)

Article

Author: Ganepola, G A N P ; Kodagoda, Y K ; Lee, Sukkyoung ; Lee, Jehee ; Wan, Qiang ; Warnakula, W.A.D.L.R. ; Omeka, W K M ; Ganepola, G.A.N.P. ; Kim, Jeongeun ; Dilshan, M.A.H. ; Kim, Gaeun ; Udayantha, H.M.V. ; Lee, Jihun ; Hanchapola, H A C R ; Rodrigo, D C G ; Rodrigo, D.C.G. ; Omeka, W.K.M. ; Liyanage, D S ; Jeong, Taehyug ; Hanchapola, H.A.C.R. ; Dilshan, M A H ; Kodagoda, Y.K. ; Liyanage, D.S. ; Warnakula, W A D L R ; Udayantha, H M V

Thioredoxin domain-containing protein 12 (TXNDC12) is a member of the thioredoxin-like superfamily that contributes to various thiol-dependent metabolic activities in all living organisms. In this research, the TXNDC12 gene from yellowtail clownfish (Amphiprion clarkii) was structurally characterized using in silico tools, assessed for immunological expression, and evaluated for biological activity using recombinant protein and cellular overexpression. The deduced coding sequence of AcTXNDC12 comprised a 522-bp nucleotide, encoding 173 amino acids with a predicted molecular mass of 19.198 kDa. The AcTXNDC12 protein consists of a⁶⁶WCGAC⁷⁰ active motif and a¹⁷⁰GDEL¹⁷³ signature. The highest tissue-specific expression of AcTXNDC12 was observed in the brain tissue, with significant modulation observed in the blood and gill tissues following stimulation of polyinosinic: polycytidylic acid, lipopolysaccharides (LPS), and Vibrio harveyi. In functional assays, recombinant AcTXNDC12 protein (rAcTXNDC12) showed insulin disulfide reduction activity, 2,2'-azino-di-(3-ethylbenzthiazoline sulfonic acid) decolorization antioxidant capacity, and ferric (Fe³⁺) reducing antioxidant potential. Additionally, a significant reduction in nitric oxide production was observed in AcTXNDC12-overexpressed RAW 264.7 cells upon LPS stimulation. Furthermore, genes associated with the regulation of oxidative stress, including nuclear factor erythroid 2-related factor 2 (Nrf2), catalase (Cat), peroxiredoxin 1 (Prx1), and ribonucleotide reductase catalytic subunit M1 (Rrm1) were significantly upregulated in fathead minnow cells overexpressing AcTXNDC12 in response to H₂O₂ treatment. The scratch wound healing assay demonstrated tissue regeneration and cell proliferation ability upon AcTXNDC12 overexpression. Altogether, the current study elucidated the antioxidant activity, immunological importance, and wound-healing effect of the AcTXNDC12 gene in yellowtail clownfish, providing valuable insights for advancing the aquaculture of A. clarkii fish.

01 Oct 2024·Antioxidants & Redox Signaling

Modulation of Protein Disulfide Isomerase Functions by Localization: The Example of the Anterior Gradient Family

Review

Author: Gavriel, Noa ; Guilbard, Marianne ; Pierre, Arvin S. ; Chevet, Eric ; Igbaria, Aeid ; Ogier-Denis, Eric ; Delom, Frederic

Significance: Oxidative folding within the endoplasmic reticulum (ER) introduces disulfide bonds into nascent polypeptides, ensuring proteins' stability and proper functioning. Consequently, this process is critical for maintaining proteome integrity and overall health. The productive folding of thousands of secretory proteins requires stringent quality control measures, such as the unfolded protein response (UPR) and ER-Associated Degradation (ERAD), which contribute significantly to maintaining ER homeostasis. ER-localized protein disulfide isomerases (PDIs) play an essential role in each of these processes, thereby contributing to various aspects of ER homeostasis, including maintaining redox balance, proper protein folding, and signaling from the ER to the nucleus. Recent Advances: Over the years, there have been increasing reports of the (re)localization of PDI family members and other ER-localized proteins to various compartments. A prime example is the anterior gradient (AGR) family of PDI proteins, which have been reported to relocate to the cytosol or the extracellular environment, acquiring gain of functions that intersect with various cellular signaling pathways. Critical Issues: Here, we summarize the functions of PDIs and their gain or loss of functions in non-ER locations. We will focus on the activity, localization, and function of the AGR proteins: AGR1, AGR2, and AGR3. Future Directions: Targeting PDIs in general and AGRs in particular is a promising strategy in different human diseases. Thus, there is a need for innovative strategies and tools aimed at targeting PDIs; those strategies should integrate the specific localization and newly acquired functions of these PDIs rather than solely focusing on their canonical roles.

01 Aug 2024·Inflammopharmacology

Wogonin preconditioning of MSCs improved their therapeutic efficiency for colitis through promoting glycolysis

Article

Author: Zhou, Xue ; Lai, Xiaorong ; Fang, Rui ; Li, Cuiping ; Lian, Qinghai ; Guo, Xiaolu ; Feng, Jianqi ; Wu, Zhiyong ; Wu, Mengye ; Pan, Ming ; Peng, Yanwen

Inflammatory bowel diseases (IBDs) are prevalent and debilitating diseases with limited clinical treatment strategies. Mesenchymal stem cell (MSCs) are pluripotent stem cells with self-renewal capability and multiple immunomodulatory effects, which make them a promising therapeutic approach for IBDs. Thus, optimization of MSCs regimes is crucial for their further clinical application. Wogonin, a flavonoid-like compound with extensive immunomodulatory and adjuvant effects, has been investigated as a potential pretreatment for MSCs in IBD treatment. In this study, we employed the DSS-induced acute colitis mouse model to compare the therapeutic effectiveness of MSCs in pretreated with or without wogonin and further explore the underlying mechanism. Compared to untreated MSCs, MSC_wogonin (pretreated with wogonin) showed greater effectiveness in the treatment of colitis. Further experiments revealed that wogonin treatment activated the AKT signaling pathway, resulting in higher cellular glycolysis. Inhibition of AKT phosphorylation by perifosine not only decreased glycolysis but impaired the therapeutic efficiency of MSC_wogonin. Consistent with these results, qPCR data indicated that wogonin treatment induced the expression of immunomodulatory molecules IL-10, IDO, and AGR1, which were reduced by perifosine. Together, our data demonstrated that wogonin preconditioning strategy further augmented the therapeutic efficacy of MSCs via promoting glycolysis, which should be a promising strategy for optimizing MSCs therapy in IBDs.

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TXNDC12

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