Molecular characterization of a novel intracellular ADP-ribosyl cyclase.
<h4>Background</h4>ADP-ribosyl cyclases are remarkable enzymes capable of catalyzing multiple reactions including the synthesis of the novel and potent intracellular calcium mobilizing messengers, cyclic ADP-ribose and NAADP. Not all ADP-ribosyl cyclases however have been characterized a...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2007-08-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0000797&type=printable |
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| author | Dev Churamani Michael J Boulware Timothy J Geach Andrew C R Martin Gary W Moy Yi-Hsien Su Victor D Vacquier Jonathan S Marchant Leslie Dale Sandip Patel |
| author_facet | Dev Churamani Michael J Boulware Timothy J Geach Andrew C R Martin Gary W Moy Yi-Hsien Su Victor D Vacquier Jonathan S Marchant Leslie Dale Sandip Patel |
| author_sort | Dev Churamani |
| collection | DOAJ |
| description | <h4>Background</h4>ADP-ribosyl cyclases are remarkable enzymes capable of catalyzing multiple reactions including the synthesis of the novel and potent intracellular calcium mobilizing messengers, cyclic ADP-ribose and NAADP. Not all ADP-ribosyl cyclases however have been characterized at the molecular level. Moreover, those that have are located predominately at the outer cell surface and thus away from their cytosolic substrates.<h4>Methodology/principal findings</h4>Here we report the molecular cloning of a novel expanded family of ADP-ribosyl cyclases from the sea urchin, an extensively used model organism for the study of inositol trisphosphate-independent calcium mobilization. We provide evidence that one of the isoforms (SpARC1) is a soluble protein that is targeted exclusively to the endoplasmic reticulum lumen when heterologously expressed. Catalytic activity of the recombinant protein was readily demonstrable in crude cell homogenates, even under conditions where luminal continuity was maintained.<h4>Conclusions/significance</h4>Our data reveal a new intracellular location for ADP-ribosyl cyclases and suggest that production of calcium mobilizing messengers may be compartmentalized. |
| format | Article |
| id | doaj-art-b297d46cbfef4af6bcff27eb22419e8f |
| institution | Kabale University |
| issn | 1932-6203 |
| language | English |
| publishDate | 2007-08-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-b297d46cbfef4af6bcff27eb22419e8f2025-08-20T03:55:22ZengPublic Library of Science (PLoS)PLoS ONE1932-62032007-08-0128e79710.1371/journal.pone.0000797Molecular characterization of a novel intracellular ADP-ribosyl cyclase.Dev ChuramaniMichael J BoulwareTimothy J GeachAndrew C R MartinGary W MoyYi-Hsien SuVictor D VacquierJonathan S MarchantLeslie DaleSandip Patel<h4>Background</h4>ADP-ribosyl cyclases are remarkable enzymes capable of catalyzing multiple reactions including the synthesis of the novel and potent intracellular calcium mobilizing messengers, cyclic ADP-ribose and NAADP. Not all ADP-ribosyl cyclases however have been characterized at the molecular level. Moreover, those that have are located predominately at the outer cell surface and thus away from their cytosolic substrates.<h4>Methodology/principal findings</h4>Here we report the molecular cloning of a novel expanded family of ADP-ribosyl cyclases from the sea urchin, an extensively used model organism for the study of inositol trisphosphate-independent calcium mobilization. We provide evidence that one of the isoforms (SpARC1) is a soluble protein that is targeted exclusively to the endoplasmic reticulum lumen when heterologously expressed. Catalytic activity of the recombinant protein was readily demonstrable in crude cell homogenates, even under conditions where luminal continuity was maintained.<h4>Conclusions/significance</h4>Our data reveal a new intracellular location for ADP-ribosyl cyclases and suggest that production of calcium mobilizing messengers may be compartmentalized.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0000797&type=printable |
| spellingShingle | Dev Churamani Michael J Boulware Timothy J Geach Andrew C R Martin Gary W Moy Yi-Hsien Su Victor D Vacquier Jonathan S Marchant Leslie Dale Sandip Patel Molecular characterization of a novel intracellular ADP-ribosyl cyclase. PLoS ONE |
| title | Molecular characterization of a novel intracellular ADP-ribosyl cyclase. |
| title_full | Molecular characterization of a novel intracellular ADP-ribosyl cyclase. |
| title_fullStr | Molecular characterization of a novel intracellular ADP-ribosyl cyclase. |
| title_full_unstemmed | Molecular characterization of a novel intracellular ADP-ribosyl cyclase. |
| title_short | Molecular characterization of a novel intracellular ADP-ribosyl cyclase. |
| title_sort | molecular characterization of a novel intracellular adp ribosyl cyclase |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0000797&type=printable |
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