scholarly journals Characterization of CAA0225, a Novel Inhibitor Specific for Cathepsin L, as a Probe for Autophagic Proteolysis

2009 ◽  
Vol 32 (3) ◽  
pp. 475-479 ◽  
Author(s):  
Katsuyuki Takahashi ◽  
Takashi Ueno ◽  
Isei Tanida ◽  
Naoko Minematsu-Ikeguchi ◽  
Mitsuo Murata ◽  
...  
Keyword(s):  
Cathepsin L

In Silico Identification and Molecular Characterization of Extracellular Cathepsin L Proteases from Giardia duodenalis

2020 ◽  
Vol 17 (4) ◽  
pp. 342-351
Author(s):  
Sergio A. Durán-Pérez ◽  
José G. Rendón-Maldonado ◽  
Lucio de Jesús Hernandez-Diaz ◽  
Annete I. Apodaca-Medina ◽  
Maribel Jiménez-Edeza ◽  
...  
Keyword(s):  
In Silico ◽  
Cathepsin L ◽  
Three Dimensional ◽  
Giardia Duodenalis ◽  
Evolutionary Genetics ◽  
Extracellular Proteins ◽  
In Silico Identification ◽  
Dimensional Models ◽  
Three Dimensional Models

Background: The protozoan Giardia duodenalis, which causes giardiasis, is an intestinal parasite that commonly affects humans, mainly pre-school children. Although there are asymptomatic cases, the main clinical features are chronic and acute diarrhea, nausea, abdominal pain, and malabsorption syndrome. Little is currently known about the virulence of the parasite, but some cases of chronic gastrointestinal alterations post-infection have been reported even when the infection was asymptomatic, suggesting that the cathepsin L proteases of the parasite may be involved in the damage at the level of the gastrointestinal mucosa. Objective: The aim of this study was the in silico identification and characterization of extracellular cathepsin L proteases in the proteome of G. duodenalis. Methods: The NP_001903 sequence of cathepsin L protease from Homo sapienswas searched against the Giardia duodenalisproteome. The subcellular localization of Giardia duodenaliscathepsin L proteases was performed in the DeepLoc-1.0 server. The construction of a phylogenetic tree of the extracellular proteins was carried out using the Molecular Evolutionary Genetics Analysis software (MEGA X). The Robetta server was used for the construction of the three-dimensional models. The search for possible inhibitors of the extracellular cathepsin L proteases of Giardia duodenaliswas performed by entering the three-dimensional structures in the FINDSITEcomb drug discovery tool. Results: Based on the amino acid sequence of cathepsin L from Homo sapiens, 8 protein sequences were identified that have in their modular structure the Pept_C1A domain characteristic of cathepsins and two of these proteins (XP_001704423 and XP_001704424) are located extracellularly. Threedimensional models were designed for both extracellular proteins and several inhibitory ligands with a score greater than 0.9 were identified. In vitrostudies are required to corroborate if these two extracellular proteins play a role in the virulence of Giardia duodenalisand to discover ligands that may be useful as therapeutic targets that interfere in the mechanism of pathogenesis generated by the parasite. Conclusion: In silicoanalysis identified two proteins in the Giardia duodenalisprotein repertoire whose characteristics allowed them to be classified as cathepsin L proteases, which may be secreted into the extracellular medium to act as virulence factors. Three-dimensional models of both proteins allowed the identification of inhibitory ligands with a high score. The results suggest that administration of those compounds might be used to block the endopeptidase activity of the extracellular cathepsin L proteases, interfering with the mechanisms of pathogenesis of the protozoan parasite Giardia duodenalis.

scholarly journals Molecular Characterization of a Novel Cathepsin L in Macrobrachium nipponense and Its Function in Ovary Maturation

2022 ◽  
Vol 12 ◽  
Author(s):  
Sufei Jiang ◽  
Yiwei Xiong ◽  
Wenyi Zhang ◽  
Junpeng Zhu ◽  
Dan Cheng ◽  
...  
Keyword(s):  
Cathepsin L ◽  
Cysteine Proteases ◽  
Macrobrachium Nipponense ◽  
Reading Frame ◽  
Physiological Processes ◽  
Gonad Somatic Index ◽  
Oriental River Prawn ◽  
Ovary Maturation

Cathepsin L genes, which belonged to cysteine proteases, were a series of multifunctional protease and played important roles in a lot of pathological and physiological processes. In this study, we analyzed the characteristics a cathepsin L (named Mn-CL2) in the female oriental river prawn, Macrobrachium nipponense which was involved in ovary maturation. The Mn-CL2 was1,582 bp in length, including a 978 bp open reading frame that encoded 326 amino acids. The Mn-CL2 was classified into the cathepsin L group by phylogenetic analysis. Real-time PCR (qPCR) analysis indicated that Mn-CL2 was highly expressed in the hepatopancreas and ovaries of female prawns. During the different ovarian stages, Mn-CL2 expression in the hepatopancreas and ovaries peaked before ovarian maturation. In situ hybridization studies revealed that Mn-CL2 was localized in the oocyte of the ovary. Injection of Mn-CL2 dsRNA significantly reduced the expression of vitellogenin. Changes in the gonad somatic index also confirmed the inhibitory effects of Mn-CL2 dsRNA on ovary maturation. These results suggest that Mn-CL2 has a key role in promoting ovary maturation.

scholarly journals Characterization of a novel cathepsin L-like protease from Taenia solium metacestodes for the immunodiagnosis of porcine cysticercosis

2019 ◽  
Vol 267 ◽  
pp. 9-16 ◽  
Author(s):  
Nancy León-Janampa ◽  
Ruddy Liendo ◽  
Robert H. Gilman ◽  
Carlos Padilla ◽  
Hector H. García ◽  
...  
Keyword(s):  
Cathepsin L ◽  
Taenia Solium ◽  
Porcine Cysticercosis

Molecular cloning and characterization of a cathepsin L-like cysteine protease of Angiostrongylus cantonensis

2020 ◽  
Vol 153 ◽  
pp. 1136-1146
Author(s):  
Huifang Bai ◽  
Yizhen Cao ◽  
Yunqiu Chen ◽  
Lingmin Zhang ◽  
Chunyun Wu ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Cysteine Protease ◽  
Cathepsin L ◽  
Angiostrongylus Cantonensis

Partial Characterization of a Novel Cathepsin L-like Protease from Fasciola hepatica

2000 ◽  
Vol 277 (1) ◽  
pp. 79-82 ◽  
Author(s):  
Susan J. Hawthorne ◽  
Maurice Pagano ◽  
David W. Halton ◽  
Brian Walker
Keyword(s):  
Fasciola Hepatica ◽  
Cathepsin L ◽  
Partial Characterization

Expression and characterization of cathepsin L-like cysteine protease from Philasterides dicentrarchi

2014 ◽  
Vol 63 (2) ◽  
pp. 359-365 ◽  
Author(s):  
Sang Phil Shin ◽  
Sang Yoon Han ◽  
Jee Eun Han ◽  
Jin Woo Jun ◽  
Ji Hyung Kim ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Cathepsin L

Characterization of cathepsin L secreted by Sf21 insect cells

2005 ◽  
Vol 444 (1) ◽  
pp. 7-14 ◽  
Author(s):  
Gary D. Johnson ◽  
Weiping Jiang
Keyword(s):  
Insect Cells ◽  
Cathepsin L
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