نتایج جستجو برای: Cathepsin L1

تعداد نتایج: 39626  

Journal: :Infection and immunity 1996
J P Dalton S McGonigle T P Rolph S J Andrews

Two cathepsin L proteinases, cathepsin L1 and cathepsin L2, secreted by liver flukes may be involved in tissue penetration, nutrition, and protection from immune attack. To ascertain the immunoprophylactic potential of these proteinases, and of another molecule, liver fluke hemoglobin (Hb), we performed vaccine trials in cattle. In the first vaccine trial various doses of cathepsin L1 were test...

Journal: :Atlas of Genetics and Cytogenetics in Oncology and Haematology 2011

Journal: :Infection and immunity 1996
J P Dalton K A Clough M K Jones P J Brindley

Adult Schistosoma mansoni parasites synthesize and secrete both cathepsin L and cathepsin B cysteine proteinases. These cysteine proteinase activities, believed to be involved in hemoglobin digestion by adult schistosomes, were characterized by using specific fluorogenic peptide substrates and zymography. Both cathepsin L- and B-like activities with pH optima of 5.2 and 6.2, respectively, predo...

Journal: :The Journal of biological chemistry 2004
Peter R Collins Colin M Stack Sandra M O'Neill Sean Doyle Thecla Ryan Gerard P Brennan Angela Mousley Michael Stewart Aaron G Maule John P Dalton Sheila Donnelly

The secretion and activation of the major cathepsin L1 cysteine protease involved in the virulence of the helminth pathogen Fasciola hepatica was investigated. Only the fully processed and active mature enzyme can be detected in medium in which adult F. hepatica are cultured. However, immunocytochemical studies revealed that the inactive procathepsin L1 is packaged in secretory vesicles of epit...

2016
Suman Kumar Nandy Alpana Seal

Cystatin superfamily is a large group of evolutionarily related proteins involved in numerous physiological activities through their inhibitory activity towards cysteine proteases. Despite sharing the same cystatin fold, and inhibiting cysteine proteases through the same tripartite edge involving highly conserved N-terminal region, L1 and L2 loop; cystatins differ widely in their inhibitory aff...

2005
Salih Kuk Mustafa Kaplan Aykut Ozdarendeli Sukru Tonbak Suleyman Felek Ahmet Kalkan

Cathepsin L1 (CatL1) is one of the major molecules in the excretory-secretory products of Fasciola hepatica and is secreted by all stages of the developing parasite; it is involved in tissue penetration, immune evasion, feeding and pathogenesis. Our aim in this study was to clone and characterise the F. hepatica CatL1 gene from a Turkish isolate. This is the first report of cDNA encoding CatL1 ...

2011
Nobuhiko KATUNUMA

Specific inhibitors for individual cathepsins have been developed based on their tertiary structures of X-ray crystallography. Cathepsin B-specific inhibitors, CA-074 and CA-030, and cathepsin L specific inhibitors, CLIK-148 and CLIK-195, were designed as the epoxysuccinate derivatives. Cathepsin S inhibitor, CLIK-060, and cathepsin K inhibitor, CLIK-166, were synthesized. These inhibitors can ...

Journal: :International journal for parasitology 2003
John P Dalton Sandra O Neill Colin Stack Peter Collins Alan Walshe Mary Sekiya Sean Doyle Grace Mulcahy Deborah Hoyle Eric Khaznadji Nathalie Moiré Gerard Brennan Angela Mousley Natalia Kreshchenko Aaron G Maule Sheila M Donnelly

Fasciola hepatica secretes cathepsin L proteases that facilitate the penetration of the parasite through the tissues of its host, and also participate in functions such as feeding and immune evasion. The major proteases, cathepsin L1 (FheCL1) and cathepsin L2 (FheCL2) are members of a lineage that gave rise to the human cathepsin Ls, Ks and Ss, but while they exhibit similarities in their subst...

Background: Cysteine proteases of the liver fluke, Fasciola hepatica, participate in catabolism of proteins, migration of the fluke through host tissues and combat host immune system. Objectives: In this study, we evaluated proteolytic activity of F. hepatica recombinant cathepsin L1 (rCL1) against gelatin and collagen as common substrat...

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