Quenching of fluorescence in membrane protein by hypocrellin B

Yue, Jiachang; Pang, Suzhen

doi:10.1007/bf02882048

Cited by 4 publications

(4 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1,6‐diphenyl‐1,3,5‐hexatriene (DPH), merocyanine‐540 (MC‐540) and 2‐(4′‐maleimidylanilino)naphthalene‐6‐sulfonic acid, sodium salt (MIANS) were purchased from Molecular Probes. Hypocrellin B (HB) was prepared by Prof. Jiachang Yue of the Institute of Biophysics, Academia Sinica according to the method described in [15]. β‐Nicotinamide adenine dinucleotide (NADH), reduced disodium salt, was obtained from Boehringer.…”

Section: Methodsmentioning

confidence: 99%

The characterization of plasma membrane Ca²⁺‐ATPase in rich sphingomyelin–cholesterol domains

2005

View full text Add to dashboard Cite

According to the raft hypothesis, sphingolipid-cholesterol (CHOL) microdomains are involved in numerous cellular functions. Here, we have prepared liposomes to simulate the lipid composition of rafts/caveolae using phosphatidylchone, sphingomyelin (SPM)-CHOL in vitro. Experiments of both 1,6-diphenyl-1,3,5-hexatriene and merocyanine-540 fluorescence showed that a phase transition from l d to l o can be observed clearly. In particular, we investigated the behavior of a membrane protein, plasma membrane Ca 2+ -ATPase (PMCA), in lipid rafts (l o phase). Three complementary approaches to characterize the physical appearance of PMCA were employed in the present study. Tryptophan intrinsic fluorescence increase, fluorescence quenching by both acrylamid and hypocrellin B decrease, and MIANS fluorescence decrease, indicate that the conformation of PMCA embedded in lipid l o phase is more compact than in lipid l d phase. Also, our results showed that PMCA activity decreased with the increase of SPM-CHOL content, in other words, with the increase of l o phase. This suggests that the specific domains containing high SPM-CHOL concentration are not a favorable place for PMCA activity. Finally, a possible explanation about PMCA molecules concentrated in caveolae/ rafts was discussed.

show abstract

Section: Methodsmentioning

confidence: 99%

The characterization of plasma membrane Ca²⁺‐ATPase in rich sphingomyelin–cholesterol domains

2005

View full text Add to dashboard Cite

show abstract

“…GM3 (c18:0‐d18:1) was purchased from Biorain (Japan). Hypocrellin B (HB) was prepared by Prof. Jiachang Yue of the Institute of Biophysics, Academia Sinica according to the method described in [6]. Other reagents were commercially available in China and were of AR grade.…”

Section: Methodsmentioning

confidence: 99%

Antagonistic effect of ganglioside GM1 and GM3 on the activity and conformation of sarcoplasmic reticulum Ca²⁺‐ATPase

Wang¹,

Tsui²,

Yang³

1999

FEBS Letters

View full text Add to dashboard Cite

It was found that rabbit skeletal muscle sarcoplasmic reticulum (SR) contained two main gangliosides:, and that the most abundant ganglioside GM3 could positively modulate the SR Ca 2+ -ATPase activity. In this paper, the effect of GM1 on Ca 2+ -ATPase was further investigated and compared with that of GM3. The study demonstrates that GM1 has an opposite effect with respect to GM3 on the activity of SR Ca 2+ -ATPase. Using assays, including intrinsic and time-resolved fluorescence and fluorescence quenching, the conformational changes of SR Ca 2+ -ATPase induced by GM1 and GM3 were compared. Obtained results indicate that GM1 could make the Ca 2+ -ATPase molecules less compact in the hydrophilic domain but more compact in the hydrophobic domain, while GM3 makes the enzyme more compact in both the hydrophilic and hydrophobic domain. Homogeneous GM1 and GM3 with the same ceramide moiety had similar effects on SR Ca 2+ -ATPase activities compared to their natural counterparts, suggesting that the carbohydrate chain may be the key moiety of the ganglioside molecule to be responsible for the difference of the effect on enzyme activity.z 1999 Federation of European Biochemical Societies.

show abstract

“…Asolectin was the product of Fluka. Hypocrellin B (HB) was a generous gift from Dr. Yue [21]. All other reagents were of the highest purity available.…”

Section: Methodsmentioning

confidence: 99%

Membrane association and conformational change of palmitoylated G_oα

2001

View full text Add to dashboard Cite

show abstract

Quenching of fluorescence in membrane protein by hypocrellin B

Cited by 4 publications

References 7 publications

The characterization of plasma membrane Ca²⁺‐ATPase in rich sphingomyelin–cholesterol domains

The characterization of plasma membrane Ca²⁺‐ATPase in rich sphingomyelin–cholesterol domains

Antagonistic effect of ganglioside GM1 and GM3 on the activity and conformation of sarcoplasmic reticulum Ca²⁺‐ATPase

Membrane association and conformational change of palmitoylated G_oα

Contact Info

Product

Resources

About

Quenching of fluorescence in membrane protein by hypocrellin B

Cited by 4 publications

References 7 publications

The characterization of plasma membrane Ca2+‐ATPase in rich sphingomyelin–cholesterol domains

The characterization of plasma membrane Ca2+‐ATPase in rich sphingomyelin–cholesterol domains

Antagonistic effect of ganglioside GM1 and GM3 on the activity and conformation of sarcoplasmic reticulum Ca2+‐ATPase

Membrane association and conformational change of palmitoylated Goα

Contact Info

Product

Resources

About

The characterization of plasma membrane Ca²⁺‐ATPase in rich sphingomyelin–cholesterol domains

The characterization of plasma membrane Ca²⁺‐ATPase in rich sphingomyelin–cholesterol domains

Antagonistic effect of ganglioside GM1 and GM3 on the activity and conformation of sarcoplasmic reticulum Ca²⁺‐ATPase

Membrane association and conformational change of palmitoylated G_oα