These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Inhibitory effect of phospholipase A(2) isolated from Crotalus durissus terrificus venom on macrophage function.
    Author: Sampaio SC, Rangel-Santos AC, Peres CM, Curi R, Cury Y.
    Journal: Toxicon; 2005 Apr; 45(5):671-6. PubMed ID: 15777963.
    Abstract:
    Recent work demonstrated that crotoxin, the main toxin of Crotalus durissus terrificus venom, inhibits macrophage spreading and phagocytic activities. The crotoxin molecule is composed of two subunits, an acidic non-toxic and non-enzymatic polypeptide named crotapotin and a weakly toxic basic phospholipase A(2) (PLA(2)). In the present work, the active subunit responsible for the inhibitory effect of crotoxin on macrophage function was investigated. Peritoneal macrophages harvested from naive rats were used. Crotapotin (2.12, 3.75, or 8.37nM/ml), added for 2h to the medium of peritoneal cell incubation, did not modify the spreading and phagocytic activities of these cells. On the other hand, the PLA(2) (1.43, 2.86, or 6.43nM/ml) subunit caused a significant reduction (30, 33, and 35%, respectively) of the spreading activity. The PLA(2) also inhibited the phagocytosis of opsonised zymosan, opsonised sheep erythrocytes, and Candida albicans, indicating that this inhibitory effect is not dependent on the type of receptor involved in the phagocytosis process. The inhibitory effect of PLA(2) was not due to loss of cell membrane integrity, since macrophage viability was higher than 95%. These findings indicate that the inhibitory effect of crotoxin on macrophage spreading and phagocytic activities is caused by the phospholipase A(2) subunit.
    [Abstract] [Full Text] [Related] [New Search]