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Last update 08 May 2025

TRADD

Last update 08 May 2025

Basic Info

Synonyms

Hs.89862, TNFR1-associated DEATH domain protein, TNFRSF1A associated via death domain

+ [3]

Introduction

Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD (PubMed:23955153, PubMed:7758105, PubMed:8612133). Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B (PubMed:7758105, PubMed:8612133). The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity).

Drugs associated with TRADD

WO2024260316

Patent Mining

Target

TRADD

Mechanism

TRADD inhibitors

Active Org.

Nanjing Ruichu Pharmaceutical Co., Ltd

Originator Org.

Nanjing Ruichu Pharmaceutical Co., Ltd

Active Indication

Cardiovascular Diseases [+11]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

CN118496175

Patent Mining

Target

TRADD

Mechanism

TRADD inhibitors

Active Org.

Anhui Medical University

Originator Org.

Anhui Medical University

Active Indication

Infectious Diseases [+2]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with TRADD

100 Translational Medicine associated with TRADD

0 Patents (Medical) associated with TRADD

592

Literatures (Medical) associated with TRADD

01 May 2025·Veterinary Microbiology

Fusobacterium necrophorum mediates the inflammatory response in the interdigital skin and fibroblasts of dairy cows via the TNF-α/TNFR1/NF-κB pathway

Article

Author: Zheng, Jiasan ; Ge, Yansong ; Liu, Meng ; Zhang, Anchi ; Yue, Yang ; Xu, Enshuang

Foot rot is a contagious disease caused by F.necrophorum. It is responsible for economic losses in dairy farming. Studies on foot rot in dairy cows are focused on the isolation and identification of pathogens and treatment methods. Few studies have reported inflammatory changes in tissues and regulatory mechanisms following infection. Here, the effects of F.necrophorum infection on the skin explants and skin fibroblasts between the toes of cattle were analyzed using histopathology and other techniques. F.necrophorum infection increased the epidermal thickness and number of hair follicles and sebaceous glands. Other skin appendages exhibited varying degrees of necrosis, and a significant infiltration of inflammatory cells was noted in the interdigital skin explants. The expressions of pro-inflammatory cytokines (IL-1β and TNF-α) and key genes in the inflammatory signalling pathway (TNFR1 and NF-κB p65) were elevated. Treatment with the TNFR1 inhibitor CAY10500 reduced inflammatory cell infiltration and alleviated TNFR1 and p65 expression. An inflammatory cell model was established using different proportions of F.necrophorum to infect BDF cells. F.necrophorum infection significantly inhibited the proliferation and viability of BDF cells and enhanced the expression of TRADD, TRAF2, TNF-α, and IL-18. CAY10500 reduced the F.necrophorum infection-induced inflammatory response and induced inflammatory responses in interdigital skin explants and BDF cells by inhibiting the TNF-α/TNFR1/NF-κB signaling pathway. In summary, these findings provide new insights into the mechanism of inflammatory responses in dairy cows with foot rot.

01 Apr 2025·International Journal of Biological Macromolecules

Heterotypic interactions among members of the death domain superfamily with implications for p75NTR-mediated co-signaling

Article

Author: Fan, Jing-Song ; Xue, Ying ; Shi, Shuo ; Lin, Zhi ; Su, Xun-Cheng ; Kisiswa, Lilian ; Li, Zhen ; Chen, Cheng ; Yuan, Wensu ; Duan, Yajing

The death domain (DD) superfamily, a group of protein interaction modules, plays a crucial role in regulating downstream signaling pathways through the formation of specific complexes. However, the aggregation-prone behavior of many DD superfamily members in solution limits their interaction studies, and the structural mechanisms underlying oligomeric assembly involving different DD subfamilies are not fully understood. Here, we demonstrate that RIP2-CARD retains its native folding and protein function for interacting with the DD of p75 neurotrophin receptor (p75^NTR) in pure water rather than under acidic conditions of pH 5.0 or lower. Leveraging this pure water system, we uncover the heterotypic interactions among p75^NTR-DD, RIP2-CARD, and TRADD-DD, elucidate their ternary HADDOCK complex structure, and identify a new specific binding interface between RIP2-CARD and TRADD-DD. Using developing cortical neurons with endogenous p75^NTR, we demonstrated that co-signaling of the p75^NTR:TRADD:RIP2 tricomplex may shift the signaling balance towards survival by reducing the efficiency of death pathways. Our findings suggest a mechanism in which p75^NTR serves as a molecular scaffold, assembling diverse signaling components to co-activate multiple signaling cascades at the receptor level.

01 Apr 2025·Acta Pharmacologica Sinica

TRADD-mediated pyroptosis contributes to diabetic cardiomyopathy

Article

Author: Zheng, Yang-Yang ; San, Wen-Qing ; Chen, Yun ; Yang, Sheng-Ju ; Meng, Guo-Liang ; Shi, Jia-Hai ; Peng, Xiao-Lu ; Shen, Dan-Ning ; Zhou, Qian-You

Regulated cell death like pyroptosis is one vital cause of diabetic cardiomyopathy (DCM), which eventually leads to heart failure. Tumor necrosis factor (TNF) receptor-associated death domain protein (TRADD) is an adapter protein with multiple functions that participates in the pathophysiological progress of different cardiovascular disorders via regulating regulated cell death. Studies have shown that TRADD combines with receptor-interacting protein kinase 3 (RIPK3) and facilitates its activation, thereby mediating TNF-induced necroptosis. However, no direct relationship between TRADD and pyroptosis has been identified. In this study, we investigated the role and mechanisms of TRADD in pyroptosis during DCM. We established a streptozotocin (STZ)-induced diabetic mouse model and high glucose (HG)-treated cardiomyocytes model. We showed that the expression levels of TRADD were significantly increased in the hearts of diabetic mice and HG-treated cardiomyocytes. Knockdown of TRADD did not affect blood glucose and triglyceride levels, but significantly improved cardiac function, and attenuated myocardial hypertrophy, fibrosis, and pyroptosis in the heart of diabetic mice. Furthermore, both knockdown of TRADD and application of TRADD inhibitor apostatin-1 (Apt-1, 10 μM) significantly ameliorated cell injury and pyroptosis in HG-treated cardiomyocytes. We demonstrated that HG treatment increased the expression of X-box binding protein 1 (XBP1) and enhanced the binding of XBP1 to the TRADD promoter to elevate TRADD expression in the cardiomyocytes. Collectively, this study provides evidence that TRADD-mediated pyroptosis contributes to DCM, suggesting that strategies to inhibit TRADD activity may be a novel approach for DCM treatment.

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TRADD

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