Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease
We found that, as in African trypanosomes, endogenous phospholipase A1 (Plase A1) activity can catalyse extensive deacylation of phospholipids upon cell death in all life stages of Trypanosoma cruzi. A major lysosomal Plase A1 was purified and characterized. The enzyme products can explain the lesio...
Guardado en:
| Publicado: |
2001
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v355_n3_p765_Wainszelbaum http://hdl.handle.net/20.500.12110/paper_02646021_v355_n3_p765_Wainszelbaum |
| Aporte de: |
| id |
paper:paper_02646021_v355_n3_p765_Wainszelbaum |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_02646021_v355_n3_p765_Wainszelbaum2023-06-08T15:23:12Z Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease Epimastigotes Phosphatidylcholine Phospholipids Trypanosomiasis Catalysis Cells Phospholipids Tissue Pathogenesis Enzymes phosphatidylcholine phospholipase A1 phospholipid phospholipase A phospholipid animal cell article catalysis cell death Chagas disease deacylation enzyme activity enzyme purification epimastigote life cycle lysosome nonhuman pathogenesis priority journal Trypanosoma cruzi trypanosomiasis animal Chagas disease enzymology human isolation and purification lysosome metabolism parasitology pathogenicity physiology Animalia Protozoa Trypanosoma Trypanosoma cruzi Animals Catalysis Chagas Disease Humans Lysosomes Phospholipases A Phospholipids Trypanosoma cruzi We found that, as in African trypanosomes, endogenous phospholipase A1 (Plase A1) activity can catalyse extensive deacylation of phospholipids upon cell death in all life stages of Trypanosoma cruzi. A major lysosomal Plase A1 was purified and characterized. The enzyme products can explain the lesions surrounding degenerating T. cruzi cells in host tissues. Thus Plase A1 emerges as a target to block pathogenesis in trypanosomal infections. 2001 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v355_n3_p765_Wainszelbaum http://hdl.handle.net/20.500.12110/paper_02646021_v355_n3_p765_Wainszelbaum |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Epimastigotes Phosphatidylcholine Phospholipids Trypanosomiasis Catalysis Cells Phospholipids Tissue Pathogenesis Enzymes phosphatidylcholine phospholipase A1 phospholipid phospholipase A phospholipid animal cell article catalysis cell death Chagas disease deacylation enzyme activity enzyme purification epimastigote life cycle lysosome nonhuman pathogenesis priority journal Trypanosoma cruzi trypanosomiasis animal Chagas disease enzymology human isolation and purification lysosome metabolism parasitology pathogenicity physiology Animalia Protozoa Trypanosoma Trypanosoma cruzi Animals Catalysis Chagas Disease Humans Lysosomes Phospholipases A Phospholipids Trypanosoma cruzi |
| spellingShingle |
Epimastigotes Phosphatidylcholine Phospholipids Trypanosomiasis Catalysis Cells Phospholipids Tissue Pathogenesis Enzymes phosphatidylcholine phospholipase A1 phospholipid phospholipase A phospholipid animal cell article catalysis cell death Chagas disease deacylation enzyme activity enzyme purification epimastigote life cycle lysosome nonhuman pathogenesis priority journal Trypanosoma cruzi trypanosomiasis animal Chagas disease enzymology human isolation and purification lysosome metabolism parasitology pathogenicity physiology Animalia Protozoa Trypanosoma Trypanosoma cruzi Animals Catalysis Chagas Disease Humans Lysosomes Phospholipases A Phospholipids Trypanosoma cruzi Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease |
| topic_facet |
Epimastigotes Phosphatidylcholine Phospholipids Trypanosomiasis Catalysis Cells Phospholipids Tissue Pathogenesis Enzymes phosphatidylcholine phospholipase A1 phospholipid phospholipase A phospholipid animal cell article catalysis cell death Chagas disease deacylation enzyme activity enzyme purification epimastigote life cycle lysosome nonhuman pathogenesis priority journal Trypanosoma cruzi trypanosomiasis animal Chagas disease enzymology human isolation and purification lysosome metabolism parasitology pathogenicity physiology Animalia Protozoa Trypanosoma Trypanosoma cruzi Animals Catalysis Chagas Disease Humans Lysosomes Phospholipases A Phospholipids Trypanosoma cruzi |
| description |
We found that, as in African trypanosomes, endogenous phospholipase A1 (Plase A1) activity can catalyse extensive deacylation of phospholipids upon cell death in all life stages of Trypanosoma cruzi. A major lysosomal Plase A1 was purified and characterized. The enzyme products can explain the lesions surrounding degenerating T. cruzi cells in host tissues. Thus Plase A1 emerges as a target to block pathogenesis in trypanosomal infections. |
| title |
Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease |
| title_short |
Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease |
| title_full |
Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease |
| title_fullStr |
Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease |
| title_full_unstemmed |
Lysosomal phospholipase A1 in Trypanosoma cruzi: An enzyme with a possible role in the pathogenesis of Chagas' disease |
| title_sort |
lysosomal phospholipase a1 in trypanosoma cruzi: an enzyme with a possible role in the pathogenesis of chagas' disease |
| publishDate |
2001 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v355_n3_p765_Wainszelbaum http://hdl.handle.net/20.500.12110/paper_02646021_v355_n3_p765_Wainszelbaum |
| _version_ |
1768544955286945792 |