Tumor Necrosis Factor Alpha Converting Enzyme (TACE) as Possible Therapeutic Target in SARS-CoV-2 Induced Acute Respiratory Distress Syndrome (ARDS)

2020 ◽  
Author(s):  
Joao Batista Junior
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Inflammatory Responses ◽  
Converting Enzyme ◽  
Necrosis Factor Alpha ◽  
Tace Inhibitors ◽  
Factor Alpha ◽  
Activity State ◽  
Necrosis Factor

<div>This study reveals, for the first time, that rosiglitazone and pioglitazone, two thiazolidinedione drugs already approved as therapeutic agents to treat type II diabetes, were found to bind favorably to tumor necrosis factor alpha converting enzyme catalytic site with highlighted binding features.</div><div><br></div>This study suggests that rosiglitazone and pioglitazone, acting as TACE inhibitors agents might avoid or attenuate the hyperexcitability proteolytic activity state of TACE, represent a new potential therapeutic approach to treat SARS-CoV-2 infection-associated severe systemic inflammatory responses observed among severely or critically ill SARS-CoV-2 patients and, consequently, to diminish severe inflammatory‐induced lung injury, ARDS development and death rates.<br><br>

Tumor Necrosis Factor Alpha Converting Enzyme (TACE) as Possible Therapeutic Target in SARS-CoV-2 Induced Acute Respiratory Distress Syndrome (ARDS)

2020 ◽  
Author(s):  
Joao Batista Junior
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Inflammatory Responses ◽  
Converting Enzyme ◽  
Necrosis Factor Alpha ◽  
Tace Inhibitors ◽  
Factor Alpha ◽  
Activity State ◽  
Necrosis Factor

<div>This study reveals, for the first time, that rosiglitazone and pioglitazone, two thiazolidinedione drugs already approved as therapeutic agents to treat type II diabetes, were found to bind favorably to tumor necrosis factor alpha converting enzyme catalytic site with highlighted binding features.</div><div><br></div>This study suggests that rosiglitazone and pioglitazone, acting as TACE inhibitors agents might avoid or attenuate the hyperexcitability proteolytic activity state of TACE, represent a new potential therapeutic approach to treat SARS-CoV-2 infection-associated severe systemic inflammatory responses observed among severely or critically ill SARS-CoV-2 patients and, consequently, to diminish severe inflammatory‐induced lung injury, ARDS development and death rates.<br><br>

scholarly journals Structure and functions of tumor necrosis factor-alpha converting enzyme.

2003 ◽  
Vol 50 (3) ◽  
pp. 625-645 ◽  
Author(s):  
Renata Mezyk ◽  
Monika Bzowska ◽  
Joanna Bereta
Keyword(s):  
Tumor Necrosis Factor ◽  
Substrate Specificity ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Converting Enzyme ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Structure And Functions ◽  
Necrosis Factor

Tumor necrosis factor-alpha converting enzyme (TACE) is the first described and best characterized secretase. In this review the structure and the possible roles for TACE are summarized. The substrate specificity and the regulation of TACE activity as well as redundancy and possible cooperations of distinct secretases are also discussed.

Intracellular maturation and transport of tumor necrosis factor alpha converting enzyme

2003 ◽  
Vol 285 (2) ◽  
pp. 278-285 ◽  
Author(s):  
Franck Peiretti ◽  
Matthias Canault ◽  
Paule Deprez-Beauclair ◽  
Virginie Berthet ◽  
Bernadette Bonardo ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Converting Enzyme ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor

scholarly journals Expression of tumor necrosis factor-alpha–converting enzyme and tumor necrosis factor-alpha in human myocarditis

2000 ◽  
Vol 36 (4) ◽  
pp. 1288-1294 ◽  
Author(s):  
Mamoru Satoh ◽  
Motoyuki Nakamura ◽  
Hidetoshi Satoh ◽  
Hidenori Saitoh ◽  
Ikuo Segawa ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Converting Enzyme ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor

scholarly journals Ectodomain Shedding of Preadipocyte Factor 1 (Pref-1) by Tumor Necrosis Factor Alpha Converting Enzyme (TACE) and Inhibition of Adipocyte Differentiation

2006 ◽  
Vol 26 (14) ◽  
pp. 5421-5435 ◽  
Author(s):  
Yuhui Wang ◽  
Hei Sook Sul
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Adipocyte Differentiation ◽  
Soluble Form ◽  
Dependent Manner ◽  
Converting Enzyme ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor

ABSTRACT Preadipocyte factor 1 (Pref-1), an epidermal growth factor repeat containing transmembrane protein found in the preadipocytes, inhibits adipocyte differentiation in vitro and in vivo. Here, we examined the processing of membrane form of Pref-1A to release the 50-kDa soluble form that inhibits adipocyte differentiation. The ectodomain cleavage of Pref-1 is markedly enhanced by phorbol 12-myristate 13-acetate in a dose- and time-dependent manner. The basal and stimulated cleavage is inhibited by the broad metalloproteinase inhibitor GM6001, a fact that suggests that cleavage of membrane Pref-1A is dependent on a metalloproteinase. Next, we showed that release of soluble Pref-1A is inhibited by TAPI-0 and by a tissue inhibitor of metalloproteinase-3, TIMP-3, that can inhibit tumor necrosis factor alpha converting enzyme (TACE), but not by TIMP-1 or TIMP-2. On the other hand, overexpression of TACE increases Pref-1 cleavage to produce the 50-kDa soluble form. Furthermore, this cleavage was not detected in cells with TACE mutation or with TACE small interfering RNA. TACE-mediated shedding of Pref-1 ectodomain inhibits adipocyte differentiation of 3T3-L1 cells and in Pref-1-null mouse embryo fibroblasts transduced with Pref-1A. Identification of TACE as the major protease responsible for conversion of membrane-bound Pref-1 to the biologically active diffusible form provides a new insight into Pref-1 function in adipocyte differentiation.

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