The role of ganglioside GM3 in the modulation of conformation and activity of sarcoplasmic reticulum CA2+-ATPase

F. Y. Yang; L. H. Wang; X. Y. Yang; Z. C. Tsui; Y. P. Tu

doi:10.1016/S0301-4622(97)00025-2

The role of ganglioside GM₃ in the modulation of conformation and activity of sarcoplasmic reticulum CA²⁺-ATPase

F. Y. Yang, L. H. Wang, X. Y. Yang, Z. C. Tsui, Y. P. Tu

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Rabbit sarcoplasmic reticulum does contain trace amounts of gangliosides, and the main species is GM₃. Incorporation of GM₃ into the SR vesicles or addition of it to the soybean phospholipid used for reconstitution of proteoliposomes obviously increased ATP hydrolysis, as well as, Ca²⁺ uptake activity of sarcoplasmic reticulum Ca²⁺-ATPase. Conformation changes of Ca²⁺-ATPase induced by GM₃ were also observed by circular dichroism, intrinsic fluorescence and fluorescence quenching measurements.

Original language	English (US)
Pages (from-to)	137-146
Number of pages	10
Journal	Biophysical Chemistry
Volume	68
Issue number	1-3
DOIs	https://doi.org/10.1016/S0301-4622(97)00025-2
State	Published - Oct 1997
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Organic Chemistry

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10.1016/S0301-4622(97)00025-2

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title = "The role of ganglioside GM3 in the modulation of conformation and activity of sarcoplasmic reticulum CA2+-ATPase",

abstract = "Rabbit sarcoplasmic reticulum does contain trace amounts of gangliosides, and the main species is GM3. Incorporation of GM3 into the SR vesicles or addition of it to the soybean phospholipid used for reconstitution of proteoliposomes obviously increased ATP hydrolysis, as well as, Ca2+ uptake activity of sarcoplasmic reticulum Ca2+-ATPase. Conformation changes of Ca2+-ATPase induced by GM3 were also observed by circular dichroism, intrinsic fluorescence and fluorescence quenching measurements.",

author = "Yang, {F. Y.} and Wang, {L. H.} and Yang, {X. Y.} and Tsui, {Z. C.} and Tu, {Y. P.}",

note = "Funding Information: This project was supported by the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences and National Natural Science Foundation of China. Copyright: Copyright 2004 Elsevier Science B.V., Amsterdam. All rights reserved.",

year = "1997",

month = oct,

doi = "10.1016/S0301-4622(97)00025-2",

language = "English (US)",

volume = "68",

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journal = "Biophysical Chemistry",

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T1 - The role of ganglioside GM3 in the modulation of conformation and activity of sarcoplasmic reticulum CA2+-ATPase

AU - Yang, F. Y.

AU - Wang, L. H.

AU - Yang, X. Y.

AU - Tsui, Z. C.

AU - Tu, Y. P.

N1 - Funding Information: This project was supported by the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences and National Natural Science Foundation of China. Copyright: Copyright 2004 Elsevier Science B.V., Amsterdam. All rights reserved.

PY - 1997/10

Y1 - 1997/10

N2 - Rabbit sarcoplasmic reticulum does contain trace amounts of gangliosides, and the main species is GM3. Incorporation of GM3 into the SR vesicles or addition of it to the soybean phospholipid used for reconstitution of proteoliposomes obviously increased ATP hydrolysis, as well as, Ca2+ uptake activity of sarcoplasmic reticulum Ca2+-ATPase. Conformation changes of Ca2+-ATPase induced by GM3 were also observed by circular dichroism, intrinsic fluorescence and fluorescence quenching measurements.

AB - Rabbit sarcoplasmic reticulum does contain trace amounts of gangliosides, and the main species is GM3. Incorporation of GM3 into the SR vesicles or addition of it to the soybean phospholipid used for reconstitution of proteoliposomes obviously increased ATP hydrolysis, as well as, Ca2+ uptake activity of sarcoplasmic reticulum Ca2+-ATPase. Conformation changes of Ca2+-ATPase induced by GM3 were also observed by circular dichroism, intrinsic fluorescence and fluorescence quenching measurements.

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The role of ganglioside GM₃ in the modulation of conformation and activity of sarcoplasmic reticulum CA²⁺-ATPase

Abstract

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