Acid Protease in Nepenthes

1969 ◽  
Vol 66 (4) ◽  
pp. 431-439 ◽  
Author(s):  
SHIZUKO AMAGASE ◽  
SHIGERU NAKAYAMA ◽  
AKIRA TSUGITA
Keyword(s):  
1981 ◽  
Vol 13 (3) ◽  
pp. 165-169 ◽  
Author(s):  
P. Aleksieva ◽  
A. Djerova ◽  
B. Tchorbanov ◽  
I. Grigorov

1988 ◽  
Vol 106 (6) ◽  
pp. 1879-1884 ◽  
Author(s):  
K McCoy ◽  
S Gal ◽  
R H Schwartz ◽  
M M Gottesman

The major excreted protein of malignantly transformed mouse fibroblasts (MEP), which is the precursor to lysosomal cathepsin L, was used to study the effect of exogenous acid proteases on antigen processing. When MEP and native pigeon cytochrome c were added to Chinese hamster ovary (CHO) cells expressing transfected major histocompatability complex class II gene products, the antigen-specific T-cell hybridoma 2B4 did not respond to the antigen. MEP appears to destroy the antigen in an acid compartment of the presenting cell because: (a) MEP is only active as a protease under acid conditions; (b) mannose 6-phosphate inhibited the internalization of MEP and blocked its effect on antigen processing; (c) the destruction required the simultaneous entry of the antigen and MEP into the cells; and (d) cytochrome c fragment 66-104 which does not need to be processed stimulated 2B4 in the presence of MEP. These results support the hypothesis that antigen processing requires internalization of the antigen into an acidic compartment, and they provide a new model for the investigation of the contribution of acid proteases to the reduced immunocompetence of tumor-bearing animals.


1972 ◽  
Vol 36 (13) ◽  
pp. 2351-2356 ◽  
Author(s):  
Shuichi Kaminogawa ◽  
Kunio Yamauchi
Keyword(s):  

2011 ◽  
Vol 44 (3) ◽  
pp. 334-338 ◽  
Author(s):  
Aurean D'Eça Júnior ◽  
Anderson França Silva ◽  
Fernanda Costa Rosa ◽  
Sílvio Gomes Monteiro ◽  
Patrícia de Maria Silva Figueiredo ◽  
...  

INTRODUCTION: Candida yeasts are commensals; however, if the balance of normal flora is disrupted or the immune defenses are compromised, Candida species can cause disease manifestations. Several attributes contribute to the virulence and pathogenicity of Candida, including the production of extracellular hydrolytic enzymes, particularly phospholipase and proteinase. This study aimed to investigate the in vitro activity of phospholipases and acid proteinases in clinical isolates of Candida spp. METHODS: Eighty-two isolates from hospitalized patients collected from various sites of origin were analyzed. Phospholipase production was performed in egg yolk medium and the production of proteinase was verified in a medium containing bovine serum albumin. The study was performed in triplicate. RESULTS: Fifty-six (68.3%) of isolates tested were phospholipase positive and 16 (44.4%) were positive for proteinase activity. C. tropicalis was the species with the highest number of positive isolates for phospholipase (91.7%). Statistically significant differences were observed in relation to production of phospholipases among species (p<0,0001) and among the strains from different sites of origin (p=0.014). Regarding the production of acid protease, the isolates of C. parapsilosis tested presented a larger number of producers (69.2%). Among the species analyzed, the percentage of protease producing isolates did not differ statistically (χ2=1.9 p=0.5901 (χ2=1.9 p=0.5901). CONCLUSIONS: The majority of C. non-albicans and all C. albicans isolates were great producers of hydrolytic enzymes and, consequently, might be able to cause infection under favorable conditions.


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