Molecular characterization and serodiagnostic evaluation of the Echinococcus ortleppi recombinant glutaredoxin 1 protein for cystic echinococcosis in buffalo (Bubalus bubalis)

Article

Author: Yashica, K. A. ; Balaji, R. ; Rialch, A. ; Samanta, S. ; Silamparasan, M. ; Jawalagatti, V. ; Anandu, S. ; Gupta, S. C. ; Tewari, Anup Kumar

Cystic echinococcosis (CE), caused by the metacestode of Echinococcus granulosus sensu lato (s.l.), adversely affects the physiol. of the vital organs in which they grow.Condemnation of meat causes substantial economic loss to the livestock industry.Conventionally the infection is detected by necropsy as serol. diagnosis of the infection in livestock is ambiguous.Identification of specific diagnostic antigens would be a substitute for the cyst fluid antigens which lack adequate diagnostic sensitivity and specificity.BLAST anal. supported by the negligible pairwise nucleotide distance of the 389 nt COX1, 489 nt NAD1, and 425 nt ITS1 with the related sequences of E. ortleppi ascertained the association of E. ortleppi with CE in buffaloes.Given the extensive distribution of glutaredoxin 1 in every developmental stage of Echinococcus granulosus s.l that makes it an ideal serodiagnostic antigen for CE, we expressed the 14 kDa E. ortleppi glutaredoxin 1 (rEoGrx1) protein in E. coli BL21 (DE3) and tested a total of 225 sera samples, including 126 sera samples from the necropsy-pos. buffalo, by the rEoGrx1 IgG-ELISA.The ELISA could detect a total of 82/126 sera samples as pos.The diagnostic sensitivity and specificity of the rEoGrx1 IgG-ELISA were 65.1% and 51.5%, resp.The protein showed serol. cross-reaction against Fasciola gigantica, Toxoplasma gondii, and Sarcocystis sp.The in silico bioinformatics anal. of the E. ortleppi, F. gigantica, and T. gondii glutaredoxin sequences revealed fully conserved amino acids at positions 11 and 21, the substitution of conserved amino acids at positions 14 and 6, and semi-conserved substitutions at positions 3 and 4, resp.The findings partly explain the mol. basis of the serol. cross-reactivity of the protein.

01 Nov 2014·Bio-Medical Materials and EngineeringQ4 · ENGINEERING & TECHNOLOGY

Protective effect and mechanism of glutaredoxin 1 on coronary arteries endothelial cells damage induced by high glucose

Q4 · ENGINEERING & TECHNOLOGY

Article

Author: Gao, Han ; Sun, Yan ; Gonzalez Penedo, Manuel Francisco ; Yu, Haitao ; Zhang, Chunjing ; Qi, Xiaodan ; Burkhart, Timothy A. ; Shi, Yan ; Liu, Feng ; Liu, Xiucai ; Wu, Qi ; Wang, Ying ; Ma, Shao-dong ; Li, Shuyan

In recent years, diabetes and its associated complications have become a major public health concern. The cardiovascular risk increases significantly in diabetes patients. It is a complex disease characterized by multiple metabolic derangements and is known to impair cardiac function by disrupting the balance between pro-oxidants and antioxidants at the cellular level. The subsequent generation of reactive oxygen species (ROS) and accompanying oxidative stress are hallmarks of the molecular mechanisms responsible for cardiovascular disease. Protein thiols act as redox-sensitive switches and are believed to be a key element in maintaining the cellular redox balance. The redox state of protein thiols is regulated by oxidative stress and redox signaling and is important to cellular functions. The potential of the thiol–disulfide oxidoreductase enzymes (thioredoxin and glutaredoxin systems) in defense against oxidative stress has been noted previously. Increasing evidence demonstrates that glutaredoxin 1 (Grx1), a cytosolic enzyme responsible for the catalysis of protein deglutathionylation, plays distinct roles in inflammation and apoptosis by inducing changes in the cellular redox system. This study investigates whether and how Grx1 protects coronary artery vascular endothelial cells against high glucose (HG) induced damage. Results indicate that the activation of eNOS/NO system is regulated by Grx 1 and coupled with inhibition of JNK and NF-κB signaling pathway which could alleviate the oxidative stress and apoptosis damage in coronary arteries endothelial cells induced by HG.

Antioxidants

Administration of Glutaredoxin-1 Attenuates Liver Fibrosis Caused by Aging and Non-Alcoholic Steatohepatitis

Article

Author: Bachschmid, Markus M. ; Matsui, Reiko ; Gower, Adam C. ; Minetti, Erika T. ; Tsukahara, Yuko ; Chong, Brian S. H. ; Ferran, Beatriz

Liver fibrosis is a sign of non-alcoholic fatty liver disease progression towards steatohepatitis (NASH) and cirrhosis and is accelerated by aging. Glutaredoxin-1 (Glrx) controls redox signaling by reversing protein S-glutathionylation, induced by oxidative stress, and its deletion causes fatty liver in mice. Although Glrx regulates various pathways, including metabolism and apoptosis, the impact of Glrx on liver fibrosis has not been studied. Therefore, we evaluated the role of Glrx in liver fibrosis induced by aging or by a high-fat, high-fructose diet. We found that: (1) upregulation of Glrx expression level inhibits age-induced hepatic apoptosis and liver fibrosis. In vitro studies indicate that Glrx regulates Fas-induced apoptosis in hepatocytes; (2) diet-induced NASH leads to reduced expression of Glrx and higher levels of S-glutathionylated proteins in the liver. In the NASH model, hepatocyte-specific adeno-associated virus-mediated Glrx overexpression (AAV-Hep-Glrx) suppresses fibrosis and apoptosis and improves liver function; (3) AAV-Hep-Glrx significantly inhibits transcription of Zbtb16 and negatively regulates immune pathways in the NASH liver. In conclusion, the upregulation of Glrx is a potential therapeutic for the reversal of NASH progression by attenuating inflammatory and fibrotic processes.

100 Deals associated with CM-YJH01

R&D Status

10 top R&D records.

to view more data

Indication	Highest Phase	Country/Location	Organization	Date
Idiopathic Pulmonary Fibrosis	Discovery	United States	Celdara Medical LLC	-
Idiopathic Pulmonary Fibrosis	Discovery	United States	Pulmatrix, Inc.	-

Clinical Result

Indication

Phase

Evaluation

View All Results

Translational Medicine

Boost your research with our translational medicine data.

view full example data

Deal

Boost your decision using our deal data.

view full example data

Core Patent

Boost your research with our Core Patent data.

view full example data

Clinical Trial

Identify the latest clinical trials across global registries.

view full example data

Approval

Accelerate your research with the latest regulatory approval information.

view full example data

Biosimilar

Competitive landscape of biosimilars in different countries/locations. Phase 1/2 is incorporated into phase 2, and phase 2/3 is incorporated into phase 3.

view full example data

Regulation

Understand key drug designations in just a few clicks with Synapse.

view full example data

Chat with Hiro

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis


No Data

CM-YJH01

Overview

Basic Info

Related

R&D Status

Clinical Result

Translational Medicine

Deal

Core Patent

Clinical Trial

Approval

Biosimilar

Regulation