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- Publisher Website: 10.1016/0012-1606(88)90242-4
- Scopus: eid_2-s2.0-0023866262
- PMID: 2449375
- WOS: WOS:A1988M442600011
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Article: Internal GTP stimulates the speract receptor mediated voltage changes in sea urchin spermatozoa membrane vesicles
Title | Internal GTP stimulates the speract receptor mediated voltage changes in sea urchin spermatozoa membrane vesicles |
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Authors | |
Issue Date | 1988 |
Publisher | Academic Press. The Journal's web site is located at http://www.elsevier.com/locate/ydbio |
Citation | Developmental Biology, 1988, v. 126 n. 1, p. 91-97 How to Cite? |
Abstract | A voltage-sensitive Na+/H+ exchanger in the flagellar membrane is responsible for regulating the intracellular pH of the sea urchin spermatozoa. A previous study has shown that the egg peptide speract can modulate this Na+/H+ exchanger through its hyperpolarizing effect on the membrane potential. The effect of GTP on this speract receptor mediated process is investigated in this study. Plasma membrane vesicles with an outwardly directed K+ gradient were prepared from the isolated flagella by osmotic lysis. Vesicular membrane potential was monitored by a cationic probe, diS-C3-(5), and an anionic probe, diS-BA-C2-(3). Results show that the presence of internal GTP greatly stimulated the speract induced membrane hyperpolarization in this vesicle system. The analog GTPγS was not only active but could, by itself, induce partial hyperpolarization which was further enhanced by speract addition. Internal GDP was partially active in supporting the speract effect, whereas GDPβS, cGMP, GMP, and ATP were all inactive. The ionic selectivity of the speract effect was investigated by increasing the external concentration of various cations. K+ and Rb+ abolished the hyperpolarization while Cs+ had no effect. These results indicate that internal GTP is involved in the coupling between the speract receptor and the membrane hyperpolarization, which is most likely due to the activation of K+ selective channels. |
Persistent Identifier | http://hdl.handle.net/10722/171521 |
ISSN | 2023 Impact Factor: 2.5 2023 SCImago Journal Rankings: 1.147 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Lee, HC | en_US |
dc.date.accessioned | 2012-10-30T06:15:31Z | - |
dc.date.available | 2012-10-30T06:15:31Z | - |
dc.date.issued | 1988 | en_US |
dc.identifier.citation | Developmental Biology, 1988, v. 126 n. 1, p. 91-97 | en_US |
dc.identifier.issn | 0012-1606 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171521 | - |
dc.description.abstract | A voltage-sensitive Na+/H+ exchanger in the flagellar membrane is responsible for regulating the intracellular pH of the sea urchin spermatozoa. A previous study has shown that the egg peptide speract can modulate this Na+/H+ exchanger through its hyperpolarizing effect on the membrane potential. The effect of GTP on this speract receptor mediated process is investigated in this study. Plasma membrane vesicles with an outwardly directed K+ gradient were prepared from the isolated flagella by osmotic lysis. Vesicular membrane potential was monitored by a cationic probe, diS-C3-(5), and an anionic probe, diS-BA-C2-(3). Results show that the presence of internal GTP greatly stimulated the speract induced membrane hyperpolarization in this vesicle system. The analog GTPγS was not only active but could, by itself, induce partial hyperpolarization which was further enhanced by speract addition. Internal GDP was partially active in supporting the speract effect, whereas GDPβS, cGMP, GMP, and ATP were all inactive. The ionic selectivity of the speract effect was investigated by increasing the external concentration of various cations. K+ and Rb+ abolished the hyperpolarization while Cs+ had no effect. These results indicate that internal GTP is involved in the coupling between the speract receptor and the membrane hyperpolarization, which is most likely due to the activation of K+ selective channels. | en_US |
dc.language | eng | en_US |
dc.publisher | Academic Press. The Journal's web site is located at http://www.elsevier.com/locate/ydbio | en_US |
dc.relation.ispartof | Developmental Biology | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Cell Membrane - Physiology | en_US |
dc.subject.mesh | Flagella - Physiology | en_US |
dc.subject.mesh | Guanosine Triphosphate - Metabolism | en_US |
dc.subject.mesh | Ion Channels - Metabolism | en_US |
dc.subject.mesh | Male | en_US |
dc.subject.mesh | Membrane Potentials - Drug Effects | en_US |
dc.subject.mesh | Oligopeptides - Pharmacology | en_US |
dc.subject.mesh | Potassium - Metabolism | en_US |
dc.subject.mesh | Receptors, Cell Surface - Physiology | en_US |
dc.subject.mesh | Rubidium - Metabolism | en_US |
dc.subject.mesh | Sea Urchins | en_US |
dc.subject.mesh | Spermatozoa - Physiology - Ultrastructure | en_US |
dc.subject.mesh | Valinomycin - Pharmacology | en_US |
dc.title | Internal GTP stimulates the speract receptor mediated voltage changes in sea urchin spermatozoa membrane vesicles | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lee, HC:leehc@hku.hk | en_US |
dc.identifier.authority | Lee, HC=rp00545 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/0012-1606(88)90242-4 | - |
dc.identifier.pmid | 2449375 | - |
dc.identifier.scopus | eid_2-s2.0-0023866262 | en_US |
dc.identifier.volume | 126 | en_US |
dc.identifier.issue | 1 | en_US |
dc.identifier.spage | 91 | en_US |
dc.identifier.epage | 97 | en_US |
dc.identifier.isi | WOS:A1988M442600011 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Lee, HC=26642959100 | en_US |
dc.identifier.issnl | 0012-1606 | - |