What's new for 'Trypanosomatids' in PubMed

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Sent on Sunday, 2011 Feb 20
Search kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
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PubMed Results

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1.	Lab Chip. 2011 Feb 18. [Epub ahead of print] Separation of parasites from human blood using deterministic lateral displacement. Holm SH, Beech JP, Barrett MP, Tegenfeldt JO. Division of Solid State Physics, nmC@LU, Lund University, PO Box 118, S-221 00, Lund, Sweden. jonas.tegenfeldt@ftf.lth.se. Abstract We present the use of a simple microfluidic technique to separate living parasites from human blood. Parasitic trypanosomatids cause a range of human and animal diseases. African trypanosomes, responsible for human African trypanosomiasis (sleeping sickness), live free in the blood and other tissue fluids. Diagnosis relies on detection and due to their often low numbers against an overwhelming background of predominantly red blood cells it is crucial to separate the parasites from the blood. By modifying the method of deterministic lateral displacement, confining parasites and red blood cells in channels of optimized depth which accentuates morphological differences, we were able to achieve separation thus offering a potential route to diagnostics.
	PMID: 21331436 [PubMed - as supplied by publisher]
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2.	J Biol Chem. 2011 Feb 17. [Epub ahead of print] Endoplasmic reticulum stress-induced apoptosis in Leishmania through CA2+-dependent and caspase-independent mechani sm. Dolai S, Pal S, Yadav RK, Adak S. Indian Institute of Chemical Biology, India. Abstract Numerous reports have shown that mitochondrial dysfunctions play a major role in apoptosis of Leishmania parasites but the endoplasmic reticulum (ER) stress induced apoptosis in Leishmania remains largely unknown. In this study we investigate ER stress induced apoptotic pathway in L. major using tunicamycin (TM) as an ER stress inducer. ER stress activates the expression of ER-localized chaperone protein BIP/GRP78 (binding protein/identical to the 78 kDa glucose regulated protein) with concomitant generation of intracellular reactive oxygen species (ROS). Upon exposure to ER stress, the elevation of cytosolic Ca2+ level is observed due to release of Ca2+ from internal stores. Increase in cytosolic Ca2+ causes mitochondrial membrane potential depolarization and ATP loss as ablation of Ca2+ by blocking voltage-gated cation channels with verapamil preserves mitochondrial membrane potential and cellular ATP content. Furthermore ER stress induced ROS dependent release of cytochrome c (Cyt C) and endonuclease G (Endo G) from mitochondria to cytosol and subsequent translocation of Endo G to nucleus is observed. Inhibition of caspase like proteases with caspase inhibitor Z-VAD-FMK or metacaspase inhibitor antipain does not prevent nuclear DNA fragmentation and phosphatidylserine exposure. Conversely significant protection in TM induced DNA degradation and phosphatidylserine exposure was achieved by either pretreatment of antioxidants (N-acetyl-L-cysteine, GSH and L-cysteine), chemical chaperone (4-phenyl butyric acid) or addition of Ca2+ chelator (1,2-bis(2-aminophenoxy)ethane-N,N,N,N-tetraacetic acid-acetoxymethyl ester). Taken together these data strongly demonstrate that ER stress induced apoptosis in L. major is dependent on ROS and Ca2+ induced mitochondrial toxicity but independent of caspase like proteases. Free Article
	PMID: 21330370 [PubMed - as supplied by publisher]
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