FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2079069988> ?p ?o ?g. }

• W2079069988 endingPage "15638" @default.
• W2079069988 startingPage "15634" @default.
• W2079069988 abstract "We investigated both conformational changes in the junctional foot protein (JFP) and Ca2+ release from sarcoplasmic reticulum (SR) in parallel after stimulation of triadic vesicles by the JFP-specific ligand, polylysine. To monitor protein conformational change, the JFP was labeled in a site-directed fashion with the fluorescent conformational probe methylcoumarin acetate (MCA) (Kang, J. J., Tarcsafalvi, A., Carlos, A. D., Fujimoto, E., Shahrokh, Z., Thevenin, B. J.-M., Shohet, S. B., and Ikemoto, N.(1992) Biochemistry 31, 3288-3293). The induction of SR Ca2+ release by polylysine produced a rapid increase in the fluorescence intensity of the JFP-bound MCA. The polylysine concentration dependence of the fluorescence change was essentially the same as that of Ca2+ release, suggesting that the two events are tightly coupled. However, the rate constant of MCA fluorescence change was much larger than that of Ca2+ release; i.e. the conformational change preceded Ca2+ release. Prevention of protein conformational change by lysine (0.2 M) inhibited Ca2+ release from SR. Inhibition of Ca2+ release by Mg2+ (5 mM), however, had little effect on the conformational change. These results suggest that binding of polylysine to the JFP produces conformational changes in the protein, which in turn activates the Ca2+ channel, leading to Ca2+ release from the SR. We investigated both conformational changes in the junctional foot protein (JFP) and Ca2+ release from sarcoplasmic reticulum (SR) in parallel after stimulation of triadic vesicles by the JFP-specific ligand, polylysine. To monitor protein conformational change, the JFP was labeled in a site-directed fashion with the fluorescent conformational probe methylcoumarin acetate (MCA) (Kang, J. J., Tarcsafalvi, A., Carlos, A. D., Fujimoto, E., Shahrokh, Z., Thevenin, B. J.-M., Shohet, S. B., and Ikemoto, N.(1992) Biochemistry 31, 3288-3293). The induction of SR Ca2+ release by polylysine produced a rapid increase in the fluorescence intensity of the JFP-bound MCA. The polylysine concentration dependence of the fluorescence change was essentially the same as that of Ca2+ release, suggesting that the two events are tightly coupled. However, the rate constant of MCA fluorescence change was much larger than that of Ca2+ release; i.e. the conformational change preceded Ca2+ release. Prevention of protein conformational change by lysine (0.2 M) inhibited Ca2+ release from SR. Inhibition of Ca2+ release by Mg2+ (5 mM), however, had little effect on the conformational change. These results suggest that binding of polylysine to the JFP produces conformational changes in the protein, which in turn activates the Ca2+ channel, leading to Ca2+ release from the SR." @default.
• W2079069988 created "2016-06-24" @default.
• W2079069988 creator A5005124124 @default.
• W2079069988 creator A5005937607 @default.
• W2079069988 creator A5044941017 @default.
• W2079069988 date "1995-06-01" @default.
• W2079069988 modified "2023-10-02" @default.
• W2079069988 title "A Conformational Change in the Junctional Foot Protein Is Involved in the Regulation of Ca2+ Release from Sarcoplasmic Reticulum" @default.
• W2079069988 cites W1042593676 @default.
• W2079069988 cites W113046133 @default.
• W2079069988 cites W125040153 @default.
• W2079069988 cites W1505568511 @default.
• W2079069988 cites W1563253655 @default.
• W2079069988 cites W1740533879 @default.
• W2079069988 cites W1952906612 @default.
• W2079069988 cites W1967950304 @default.
• W2079069988 cites W1973150566 @default.
• W2079069988 cites W1986598978 @default.
• W2079069988 cites W2024929666 @default.
• W2079069988 cites W2025671875 @default.
• W2079069988 cites W2039547987 @default.
• W2079069988 cites W2040059550 @default.
• W2079069988 cites W2040292909 @default.
• W2079069988 cites W2056212703 @default.
• W2079069988 cites W2060055554 @default.
• W2079069988 cites W206588626 @default.
• W2079069988 cites W2067254948 @default.
• W2079069988 cites W2074361372 @default.
• W2079069988 cites W2083310303 @default.
• W2079069988 cites W2101011826 @default.
• W2079069988 cites W2124339566 @default.
• W2079069988 cites W2128113643 @default.
• W2079069988 cites W2131310568 @default.
• W2079069988 cites W2138450406 @default.
• W2079069988 cites W2147265362 @default.
• W2079069988 cites W2161957047 @default.
• W2079069988 cites W4235579029 @default.
• W2079069988 cites W4376453111 @default.
• W2079069988 doi "https://doi.org/10.1074/jbc.270.26.15634" @default.
• W2079069988 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7797562" @default.
• W2079069988 hasPublicationYear "1995" @default.
• W2079069988 type Work @default.
• W2079069988 sameAs 2079069988 @default.
• W2079069988 citedByCount "38" @default.
• W2079069988 countsByYear W20790699882012 @default.
• W2079069988 countsByYear W20790699882013 @default.
• W2079069988 countsByYear W20790699882017 @default.
• W2079069988 countsByYear W20790699882019 @default.
• W2079069988 crossrefType "journal-article" @default.
• W2079069988 hasAuthorship W2079069988A5005124124 @default.
• W2079069988 hasAuthorship W2079069988A5005937607 @default.
• W2079069988 hasAuthorship W2079069988A5044941017 @default.
• W2079069988 hasBestOaLocation W20790699881 @default.
• W2079069988 hasConcept C12554922 @default.
• W2079069988 hasConcept C130316041 @default.
• W2079069988 hasConcept C158617107 @default.
• W2079069988 hasConcept C185592680 @default.
• W2079069988 hasConcept C2777339483 @default.
• W2079069988 hasConcept C2780075363 @default.
• W2079069988 hasConcept C41625074 @default.
• W2079069988 hasConcept C55493867 @default.
• W2079069988 hasConcept C86803240 @default.
• W2079069988 hasConceptScore W2079069988C12554922 @default.
• W2079069988 hasConceptScore W2079069988C130316041 @default.
• W2079069988 hasConceptScore W2079069988C158617107 @default.
• W2079069988 hasConceptScore W2079069988C185592680 @default.
• W2079069988 hasConceptScore W2079069988C2777339483 @default.
• W2079069988 hasConceptScore W2079069988C2780075363 @default.
• W2079069988 hasConceptScore W2079069988C41625074 @default.
• W2079069988 hasConceptScore W2079069988C55493867 @default.
• W2079069988 hasConceptScore W2079069988C86803240 @default.
• W2079069988 hasIssue "26" @default.
• W2079069988 hasLocation W20790699881 @default.
• W2079069988 hasOpenAccess W2079069988 @default.
• W2079069988 hasPrimaryLocation W20790699881 @default.
• W2079069988 hasRelatedWork W1641805382 @default.
• W2079069988 hasRelatedWork W1965544384 @default.
• W2079069988 hasRelatedWork W2031369310 @default.
• W2079069988 hasRelatedWork W2054509900 @default.
• W2079069988 hasRelatedWork W2059028563 @default.
• W2079069988 hasRelatedWork W2081205442 @default.
• W2079069988 hasRelatedWork W2428083287 @default.
• W2079069988 hasRelatedWork W2470630500 @default.
• W2079069988 hasRelatedWork W2513634880 @default.
• W2079069988 hasRelatedWork W2078792694 @default.
• W2079069988 hasVolume "270" @default.
• W2079069988 isParatext "false" @default.
• W2079069988 isRetracted "false" @default.
• W2079069988 magId "2079069988" @default.
• W2079069988 workType "article" @default.