2013
DOI: 10.1016/j.bbagen.2013.01.013
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Trypanothione: A unique bis-glutathionyl derivative in trypanosomatids

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Cited by 110 publications
(94 citation statements)
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“…In order to shed light into this question and taking into account a potential role for selenoproteins in redox or mitochondrial sulfur-related metabolism, we analyzed the content of representative proteins from thiol-dependent metabolic pathways in parasites isolated from animals infected with the SepSecS-KO and WT cell lines. Thus, we analyzed the expression of trypanothione reductase (TR), a NADPH-dependent flavoenzyme in charge of maintaining trypanothione reduced, which is the major low molecular mass redox co-substrate in trypanosomatids [7]; TXN-Px, a tryparedoxin-dependent peroxiredoxin that catalyzes the decomposition of hydroperoxides very efficiently [40]; TXN, a thioredoxin-like oxidoreductase that plays a key role in protein redox homeostasis [17]; Grx1, a class II glutaredoxin with an essential role in the mitochondrial iron-sulfur biosynthetic pathway [28]; and Grx3, a class II glutaredoxin fused to a thioredoxin domain with putative roles in cytosolic mobilization and/or assembly of iron-sulfur clusters [41,42]. The expression level of none of these proteins differed significantly between SepSecS-KO and WT parasites isolated from infected mice (Fig.…”
Section: Selenoproteins Are Fully Dispensable For the Survival Of Afrmentioning
confidence: 99%
See 1 more Smart Citation
“…In order to shed light into this question and taking into account a potential role for selenoproteins in redox or mitochondrial sulfur-related metabolism, we analyzed the content of representative proteins from thiol-dependent metabolic pathways in parasites isolated from animals infected with the SepSecS-KO and WT cell lines. Thus, we analyzed the expression of trypanothione reductase (TR), a NADPH-dependent flavoenzyme in charge of maintaining trypanothione reduced, which is the major low molecular mass redox co-substrate in trypanosomatids [7]; TXN-Px, a tryparedoxin-dependent peroxiredoxin that catalyzes the decomposition of hydroperoxides very efficiently [40]; TXN, a thioredoxin-like oxidoreductase that plays a key role in protein redox homeostasis [17]; Grx1, a class II glutaredoxin with an essential role in the mitochondrial iron-sulfur biosynthetic pathway [28]; and Grx3, a class II glutaredoxin fused to a thioredoxin domain with putative roles in cytosolic mobilization and/or assembly of iron-sulfur clusters [41,42]. The expression level of none of these proteins differed significantly between SepSecS-KO and WT parasites isolated from infected mice (Fig.…”
Section: Selenoproteins Are Fully Dispensable For the Survival Of Afrmentioning
confidence: 99%
“…Most selenoproteins are redox enzymes containing a catalytic Sec residue. dithiol and devoid of selenocysteine-containing peroxidases [7]. Nonetheless, as most Sec incorporating organisms, the kinetoplastida lineage possesses the entire Sec incorporation machinery dedicated to a small selenoproteome [5].…”
Section: Introductionmentioning
confidence: 99%
“…T(SH) 2 is an essential thiol compound involved in various processes including ROS metabolism, DNA replication, and iron-sulphur cluster assembly as electron donors of TXN and Grx in trypanosomatids (Manta et al 2013). The biosynthesis of T(SH) 2 was originally considered to be catalyzed by two distinct enzymes.…”
Section: Low-molecular-weight Thiolsmentioning
confidence: 99%
“…The trifluoroacetate salts of N 1 ,N 5 -bis(trifluoroacetyl)diethylenetriamine (8), N 1 ,N 8 -bis(trifluoroacetyl)spermidine (10) and N 1 ,N 12 -bis(trifluoroacetyl)spermine (11) were prepared as previously reported. 86 All other reagents were purchased from commercial sources.…”
Section: Synthesis Informationmentioning
confidence: 99%