Nitric Oxide Inhibits Cruzipain, the Major Papain-like Cysteine Proteinase from Trypanosoma cruzi

Venturini, Giorgio; Salvati, Luca; Muolo, Massimo; Colasanti, Marco; Gradoni, Luigi; Ascenzi, Paolo

doi:10.1006/bbrc.2000.2447

Cited by 57 publications

(41 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Recently, it was reported that NO or NO donors can inhibit the catalytic activity of cruzipain, the major papain-like cysteine proteinase in T. cruzi. Analogous to a similar protein in Plasmodium, this dose-dependent effect was attributed to S-nitrosylation of Cys25, a catalytic residue present in the active site of cruzipain (Venturini et al 2000).…”

Section: The Dual Role Of No During T Cruzi Infectionmentioning

confidence: 90%

The effects of nitric oxide on the immune system during Trypanosoma cruzi infection

Gutierrez

Mineo

Pavanelli

et al. 2009

Mem. Inst. Oswaldo Cruz

109

View full text Add to dashboard Cite

show abstract

Section: The Dual Role Of No During T Cruzi Infectionmentioning

confidence: 90%

The effects of nitric oxide on the immune system during Trypanosoma cruzi infection

Gutierrez

Mineo

Pavanelli

et al. 2009

Mem. Inst. Oswaldo Cruz

109

View full text Add to dashboard Cite

show abstract

“…This dosedependent effect has been assigned to the nitrosylation of the Cys catalytic residue (Venturini et al, 2000a;Venturini et al, 2000b). Considering these antiparasitic effects of NO…”

Section: The Role Of Myoglobin During Parasite Infection Under Normoxmentioning

confidence: 99%

“…• by mediating chemical modifications of proteins, which is directly killing or decreasing parasite growth (Brunet, 2001;Venturini et al, 2000a;Venturini et al, 2000b), Ascenzi et al proposed that in this case the degradation of NO…”

Section: The Role Of Myoglobin During Parasite Infection Under Normoxmentioning

confidence: 99%

Unmasking the Janus face of myoglobin in health and disease

Hendgen‐Cotta

Flögel

Kelm

et al. 2010

Journal of Experimental Biology

View full text Add to dashboard Cite

SummaryFor more than 100 years, myoglobin has been among the most extensively studied proteins. Since the first comprehensive review on myoglobin function as a dioxygen store by Millikan in 1939 and the discovery of its structure 50 years ago, multiple studies have extended our understanding of its occurrence, properties and functions. Beyond the two major roles, the storage and the facilitation of dioxygen diffusion, recent physiological studies have revealed that myoglobin acts as a potent scavenger of nitric oxide (NO • ) representing a control system that preserves mitochondrial respiration. In addition, myoglobin may also protect the heart against reactive oxygen species (ROS), and, under hypoxic conditions, deoxygenated myoglobin is able to reduce nitrite to NO • leading to a downregulation of the cardiac energy status and to a decreased heart injury after reoxygenation. Thus, by controlling the NO • bioavailability via scavenging or formation, myoglobin serves as part of a sensitive dioxygen sensory system. In this review, the physiological relevance of these recent findings are delineated for pathological states where NO • and ROS bioavailability are known to be critical determinants for the outcome of the disease, e.g. ischemia/reperfusion injury. Detrimental and beneficial effects of the presence of myoglobin are discussed for various states of tissue oxygen tension within the heart and skeletal muscle. Furthermore, the impact of myoglobin on parasite infection, rhabdomyolysis, hindlimb and liver ischemia, angiogenesis and tumor growth are considered.

show abstract

“…S-nitrosylation of specific cysteine residues in microbial proteases and Zn-dependent DNA-binding proteins accompanies the antimicrobial activities of RNI against coxsackievirus, HIV, Leishmania, Plasmodium, Trypanosoma, and Salmonella (7,(9)(10)(11)(12)(13)(14). Despite the widespread role of RNI as antimicrobial and regulatory molecules (15), however, no systematic identification of S-nitroso proteins in any organism has been described.…”

mentioning

confidence: 99%

S-nitroso proteome ofMycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense

Rhee

Erdjument‐Bromage

Tempst

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

158

139

View full text Add to dashboard Cite

The immune response to Mycobacterium tuberculosis (Mtb) includes expression of nitric oxide (NO) synthase (NOS)2, whose products can kill Mtb in vitro with a molar potency greater than that of many conventional antitubercular agents. However, the targets of reactive nitrogen intermediates (RNIs) in Mtb are unknown. One major action of RNIs is protein S-nitrosylation. Here, we describe, to our knowledge, the first proteomic analysis of S-nitrosylation in a whole organism after treating Mtb with bactericidal concentrations of RNIs. The 29 S-nitroso proteins identified are all enzymes, mostly serving intermediary metabolism, lipid metabolism, and͞or antioxidant defense. Many are essential or implicated in virulence, including defense against RNIs. For each of two target enzymes tested, lipoamide dehydrogenase and mycobacterial proteasome ATPase, S-nitrosylation caused enzyme inhibition. Moreover, endogenously biotinylated proteins were driven into mixed disulfide complexes. Targeting of metabolic enzymes and antioxidant defenses by means of protein S-nitrosylation and mixed disulfide bonding may contribute to the antimycobacterial actions of RNIs.nitric oxide ͉ biotin ͉ lipoamide dehydrogenase ͉ mycobacterial proteasome ATPase

show abstract

Nitric Oxide Inhibits Cruzipain, the Major Papain-like Cysteine Proteinase from Trypanosoma cruzi

Cited by 57 publications

References 46 publications

The effects of nitric oxide on the immune system during Trypanosoma cruzi infection

The effects of nitric oxide on the immune system during Trypanosoma cruzi infection

Unmasking the Janus face of myoglobin in health and disease

S-nitroso proteome ofMycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense

Contact Info

Product

Resources

About