ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase. / Procida, K; Caspersen, C; Kromann, H; Christensen, S B; Treiman, M.

In: FEBS Letters, Vol. 439, No. 1-2, 1998, p. 127-32.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Procida, K, Caspersen, C, Kromann, H, Christensen, SB & Treiman, M 1998, 'ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase', FEBS Letters, vol. 439, no. 1-2, pp. 127-32.

APA

Procida, K., Caspersen, C., Kromann, H., Christensen, S. B., & Treiman, M. (1998). ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase. FEBS Letters, 439(1-2), 127-32.

Vancouver

Procida K, Caspersen C, Kromann H, Christensen SB, Treiman M. ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase. FEBS Letters. 1998;439(1-2):127-32.

Author

Procida, K ; Caspersen, C ; Kromann, H ; Christensen, S B ; Treiman, M. / ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase. In: FEBS Letters. 1998 ; Vol. 439, No. 1-2. pp. 127-32.

Bibtex

@article{6429dbb0e93b11ddbf70000ea68e967b,
title = "ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase",
abstract = "Thapsigargin is a highly potent and selective inhibitor of sarco-endoplasmic reticulum (SERCA) family of Ca2+-ATPases and a useful tool in research concerning the function of intracellular Ca2+ stores. We describe here a novel fluorescent derivative (8-O-(4-aminocinnamoyl)-8-O-debutanoylthapsigargin, termed ACTA) of this compound, acting as a Ca2+-ATPase inhibitor with a potency approaching that of thapsigargin. Binding of ACTA to the skeletal muscle sarcoplasmic reticulum vesicles results in a strong fluorescence enhancement, approximately 66% of which depends on ACTA association with Ca2+-ATPase. This specific component of ACTA fluorescence is sensitive to the E1-E2 conformational equilibrium of the pump. The combined properties of high potency and binding-dependent fluorescence suggest ACTA to be a useful probe for a range of studies involving the SERCA class of ATPases.",
author = "K Procida and C Caspersen and H Kromann and Christensen, {S B} and M Treiman",
note = "Keywords: Calcium; Calcium-Transporting ATPases; Enzyme Inhibitors; Fluorescent Dyes; Muscle, Skeletal; Protein Conformation; Thapsigargin",
year = "1998",
language = "English",
volume = "439",
pages = "127--32",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-2",

}

RIS

TY - JOUR

T1 - ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase

AU - Procida, K

AU - Caspersen, C

AU - Kromann, H

AU - Christensen, S B

AU - Treiman, M

N1 - Keywords: Calcium; Calcium-Transporting ATPases; Enzyme Inhibitors; Fluorescent Dyes; Muscle, Skeletal; Protein Conformation; Thapsigargin

PY - 1998

Y1 - 1998

N2 - Thapsigargin is a highly potent and selective inhibitor of sarco-endoplasmic reticulum (SERCA) family of Ca2+-ATPases and a useful tool in research concerning the function of intracellular Ca2+ stores. We describe here a novel fluorescent derivative (8-O-(4-aminocinnamoyl)-8-O-debutanoylthapsigargin, termed ACTA) of this compound, acting as a Ca2+-ATPase inhibitor with a potency approaching that of thapsigargin. Binding of ACTA to the skeletal muscle sarcoplasmic reticulum vesicles results in a strong fluorescence enhancement, approximately 66% of which depends on ACTA association with Ca2+-ATPase. This specific component of ACTA fluorescence is sensitive to the E1-E2 conformational equilibrium of the pump. The combined properties of high potency and binding-dependent fluorescence suggest ACTA to be a useful probe for a range of studies involving the SERCA class of ATPases.

AB - Thapsigargin is a highly potent and selective inhibitor of sarco-endoplasmic reticulum (SERCA) family of Ca2+-ATPases and a useful tool in research concerning the function of intracellular Ca2+ stores. We describe here a novel fluorescent derivative (8-O-(4-aminocinnamoyl)-8-O-debutanoylthapsigargin, termed ACTA) of this compound, acting as a Ca2+-ATPase inhibitor with a potency approaching that of thapsigargin. Binding of ACTA to the skeletal muscle sarcoplasmic reticulum vesicles results in a strong fluorescence enhancement, approximately 66% of which depends on ACTA association with Ca2+-ATPase. This specific component of ACTA fluorescence is sensitive to the E1-E2 conformational equilibrium of the pump. The combined properties of high potency and binding-dependent fluorescence suggest ACTA to be a useful probe for a range of studies involving the SERCA class of ATPases.

M3 - Journal article

C2 - 9849892

VL - 439

SP - 127

EP - 132

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1-2

ER -

ID: 9910536