دورية أكاديمية
Isolation and characterization of a novel member of the ACC ligand-gated chloride channel family, Hco-LCG-46, from the parasitic nematode Haemonchus contortus.
| العنوان: | Isolation and characterization of a novel member of the ACC ligand-gated chloride channel family, Hco-LCG-46, from the parasitic nematode Haemonchus contortus. |
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| المؤلفون: | Habibi SA; Applied Bioscience Graduate Program, Faculty of Science, Ontario Tech University, 2000 Simcoe Street North, Oshawa, ON, L1H 7K4, Canada., Blazie SM; Neurobiology Section, Division of Biological Sciences, University of California, San Diego, La Jolla, CA, 92093, United States., Jin Y; Neurobiology Section, Division of Biological Sciences, University of California, San Diego, La Jolla, CA, 92093, United States., Forrester SG; Applied Bioscience Graduate Program, Faculty of Science, Ontario Tech University, 2000 Simcoe Street North, Oshawa, ON, L1H 7K4, Canada. Electronic address: sean.forrester@uoit.ca. |
| المصدر: | Molecular and biochemical parasitology [Mol Biochem Parasitol] 2020 May; Vol. 237, pp. 111276. Date of Electronic Publication: 2020 Apr 06. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier/North-Holland Biomedical Press Country of Publication: Netherlands NLM ID: 8006324 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1872-9428 (Electronic) Linking ISSN: 01666851 NLM ISO Abbreviation: Mol Biochem Parasitol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam, Elsevier/North-Holland Biomedical Press. |
| مواضيع طبية MeSH: | Acetylcholine/*metabolism , Chloride Channels/*chemistry , Cysteine Loop Ligand-Gated Ion Channel Receptors/*chemistry , Haemonchus/*metabolism , Helminth Proteins/*chemistry, Acetylcholine/pharmacology ; Action Potentials/drug effects ; Action Potentials/physiology ; Aldicarb/pharmacology ; Amino Acid Sequence ; Animals ; Anthelmintics/pharmacology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Carbachol/metabolism ; Carbachol/pharmacology ; Chloride Channels/genetics ; Chloride Channels/isolation & purification ; Chloride Channels/metabolism ; Choline/analogs & derivatives ; Choline/metabolism ; Choline/pharmacology ; Cloning, Molecular ; Cysteine Loop Ligand-Gated Ion Channel Receptors/genetics ; Cysteine Loop Ligand-Gated Ion Channel Receptors/isolation & purification ; Cysteine Loop Ligand-Gated Ion Channel Receptors/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Haemonchus/genetics ; Helminth Proteins/genetics ; Helminth Proteins/isolation & purification ; Helminth Proteins/metabolism ; Models, Molecular ; Oocytes/cytology ; Oocytes/metabolism ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Xenopus laevis/genetics ; Xenopus laevis/metabolism |
| مستخلص: | The ACC-1 family of cys-loop receptors are ligand-gated chloride channels sensitive to acetylcholine (ACh), and are only present in invertebrates. Studies of this family of inhibitory receptors has provided insight into how they bind and respond to ACh in a manner vastly different from nicotinic acetylcholine receptors and appear to be present in tissues that are relevant to anthelmintic action. Here, we have identified two members of the ACC-1 family from the parasitic nematode Haemonchus contortus, Hco-LGC-46 and Hco-ACC-4. Hco-LGC-46 is an ACC subunit that has never been previously expressed and pharmacologically characterized. We found that Hco-LGC-46 when expressed in Xenopus laevis oocytes forms a functional homomeric channel that is responsive to the cholinergic agonists ACh and methylcholine. hco-lgc-46 expressed in a C. elegans lgc-46 null strain (ok2900) suppressed hypersensitivity to aldicarb in a manner similar to cel-lgc-46. It was also found that Hco-LGC-46 assembles with Hco-ACC-1 and produces a receptor that is over 5-fold more sensitive to ACh and responds to the cholinergic agonists methycholine and carbachol. In contrast, the co-expression of Hco-LGC-46 with Hco-ACC-4 resulted in non-functional channels in oocytes. Hco-ACC-4 also appears to form heteromeric channels with a previously characterized subunit, Hco-ACC-2. Co-expression of Hco-ACC-4 with Hco-ACC-2 resulted in a functional heteromeric channel with an EC (Copyright © 2020 Elsevier B.V. All rights reserved.) |
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| معلومات مُعتمدة: | R37 NS035546 United States NS NINDS NIH HHS |
| فهرسة مساهمة: | Keywords: Aldicarb sensitivity; Cys-loop receptor; Haemonchus contortus; Ion channels; Parasitic nematode |
| المشرفين على المادة: | 0 (Anthelmintics) 0 (Chloride Channels) 0 (Cysteine Loop Ligand-Gated Ion Channel Receptors) 0 (Helminth Proteins) 0 (Recombinant Proteins) 0 (methylcholine) 8V071SH05P (Aldicarb) 8Y164V895Y (Carbachol) N91BDP6H0X (Choline) N9YNS0M02X (Acetylcholine) |
| تواريخ الأحداث: | Date Created: 20200409 Date Completed: 20210204 Latest Revision: 20220822 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC9392465 |
| DOI: | 10.1016/j.molbiopara.2020.111276 |
| PMID: | 32268182 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1872-9428 |
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| DOI: | 10.1016/j.molbiopara.2020.111276 |