NDLI: Specific Inhibition of the Plasmodial Surface Anion Channel by Dantrolene▿

Please wait, while we are loading the content...

Tcc1p, a Novel Protein Containing the Tetratricopeptide Repeat Motif, Interacts with Tup1p To Regulate Morphological Transition and Virulence in Candida albicans ▿ †

Galactose Starvation in a Bloodstream Form Trypanosoma brucei UDP-Glucose 4′-Epimerase Conditional Null Mutant

Expressed in the Yeast Saccharomyces cerevisiae, Human ERK5 Is a Client of the Hsp90 Chaperone That Complements Loss of the Slt2p (Mpk1p) Cell Integrity Stress-Activated Protein Kinase▿

Effect of Sequence-Directed Nucleosome Disruption on Cell-Type-Specific Repression by α2/Mcm1 in the Yeast Genome▿

Novel Mitogen-Activated Protein Kinase MpkC of Aspergillus fumigatus Is Required for Utilization of Polyalcohol Sugars▿

Year: 2006, Volume: 5, Issue: 10

Year: 2006, Volume: 5, Issue: 9

Year: 2006, Volume: 5, Issue: 8

Year: 2006, Volume: 5, Issue: 7

Year: 2006, Volume: 5, Issue: 6

Year: 2006, Volume: 5, Issue: 5

Year: 2006, Volume: 5, Issue: 4

Year: 2006, Volume: 5, Issue: 3

Year: 2006, Volume: 5, Issue: 2

Year: 2006, Volume: 5, Issue: 1

Year: 2005, Volume: 4

Year: 2004, Volume: 3

Year: 2003, Volume: 2

Year: 2002, Volume: 1

Specific Inhibition of the Plasmodial Surface Anion Channel by Dantrolene▿

Content Provider	PubMed Central
Author	Lisk, Godfrey Kang, Myungsa Cohn, Jamieson V. Desai, Sanjay A.
Copyright Year	2006
Abstract	The plasmodial surface anion channel (PSAC), induced on human erythrocytes by the malaria parasite Plasmodium falciparum, is an important target for antimalarial drug development because it may contribute to parasite nutrient acquisition. However, known antagonists of this channel are quite nonspecific, inhibiting many other channels and carriers. This lack of specificity not only complicates drug development but also raises doubts about the exact role of PSAC in the well-known parasite-induced permeability changes. We recently identified a family of new PSAC antagonists structurally related to dantrolene, an antagonist of muscle Ca++ release channels. Here, we explored the mechanism of dantrolene's actions on parasite-induced permeability changes. We found that dantrolene inhibits the increased permeabilities of sorbitol, two amino acids, an organic cation, and hypoxanthine, suggesting a common pathway shared by these diverse solutes. It also produced parallel reductions in PSAC single-channel and whole-cell Cl− currents. In contrast to its effect on parasite-induced permeabilities, dantrolene had no measurable effect on five other classes of anion channels, allaying concerns of poor specificity inherent to other known antagonists. Our studies indicate that dantrolene binds PSAC at an extracellular site distinct from the pore, where it inhibits the conformational changes required for channel gating. Its affinity for this site depends on ionic strength, implicating electrostatic interactions in dantrolene binding. In addition to the potential therapeutic applications of its derivatives, dantrolene's specificity and its defined mechanism of action on PSAC make it a useful tool for transport studies of infected erythrocytes.
Related Links	http://dx.doi.org/10.1128/ec.00212-06
Ending Page	1893
Page Count	12
Starting Page	1882
File Format	PDF
ISSN	15359778
e-ISSN	15359786
Journal	Eukaryotic Cell
Issue Number	11
Volume Number	5
Language	English
Publisher	American Society for Microbiology
Publisher Date	2006-11-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The Plasmodial Surface Anion Channel Is Functionally Conserved in Divergent Malaria Parasites

Complex inheritance of the plasmodial surface anion channel in a Plasmodium falciparum genetic cross

High Guanidinium Permeability Reveals Dehydration-Dependent Ion Selectivity in the Plasmodial Surface Anion Channel

Two Distinct Mechanisms of Transport through the Plasmodial Surface Anion Channel

Synergistic Malaria Parasite Killing by Two Types of Plasmodial Surface Anion Channel Inhibitors

Voltage-dependent inactivation of the plasmodial surface anion channel via a cleavable cytoplasmic component

Altered plasmodial surface anion channel activity and in vitro resistance to permeating antimalarial compounds

Plasmodial Surface Anion Channel-independent Phloridzin Resistance in Plasmodium falciparum

Inhibition of the mitochondrial inner membrane anion channel by dicyclohexylcarbodiimide. Evidence for a specific transport pathway.

Specific Inhibition of the Plasmodial Surface Anion Channel by Dantrolene▿

Similar Documents

The Plasmodial Surface Anion Channel Is Functionally Conserved in Divergent Malaria Parasites

Complex inheritance of the plasmodial surface anion channel in a Plasmodium falciparum genetic cross

High Guanidinium Permeability Reveals Dehydration-Dependent Ion Selectivity in the Plasmodial Surface Anion Channel

Two Distinct Mechanisms of Transport through the Plasmodial Surface Anion Channel

Synergistic Malaria Parasite Killing by Two Types of Plasmodial Surface Anion Channel Inhibitors

Voltage-dependent inactivation of the plasmodial surface anion channel via a cleavable cytoplasmic component

Altered plasmodial surface anion channel activity and in vitro resistance to permeating antimalarial compounds

Plasmodial Surface Anion Channel-independent Phloridzin Resistance in Plasmodium falciparum

Inhibition of the mitochondrial inner membrane anion channel by dicyclohexylcarbodiimide. Evidence for a specific transport pathway.

Specific Inhibition of the Plasmodial Surface Anion Channel by Dantrolene▿