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Heparin-derived oligosaccharides interact with the phospholamban cytoplasmic domain and stimulate SERCA function

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Heparin-derived oligosaccharides interact with the phospholamban cytoplasmic domain and stimulate SERCA function. / Hughes, Eleri; Edwards, Rachel; Middleton, David A.
In: Biochemical and Biophysical Research Communications, Vol. 401, No. 3, 22.10.2010, p. 370-5.

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Hughes E, Edwards R, Middleton DA. Heparin-derived oligosaccharides interact with the phospholamban cytoplasmic domain and stimulate SERCA function. Biochemical and Biophysical Research Communications. 2010 Oct 22;401(3):370-5. doi: 10.1016/j.bbrc.2010.09.056

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Hughes, Eleri ; Edwards, Rachel ; Middleton, David A. / Heparin-derived oligosaccharides interact with the phospholamban cytoplasmic domain and stimulate SERCA function. In: Biochemical and Biophysical Research Communications. 2010 ; Vol. 401, No. 3. pp. 370-5.

Bibtex

@article{ba2d9d5ffaa44979a0916b2fd6089e61,
title = "Heparin-derived oligosaccharides interact with the phospholamban cytoplasmic domain and stimulate SERCA function",
abstract = "The association between the cardiac transmembrane proteins phospholamban and sarcoplasmic reticulum Ca(2+) ATPase (SERCA2a) regulates the active transport of Ca(2+) into the sarcoplasmic reticulum (SR) lumen and controls the contraction and relaxation of the heart. Heart failure (HF) and cardiac hypertrophy have been linked to defects in Ca(2+) uptake by the cardiac SR and stimulation of calcium transport by modulation of the PLB-SERCA interaction is a potential therapy. This work is part of an effort to identify compounds that destabilise the PLB-SERCA interaction in well-defined membrane environments. It is shown that heparin-derived oligosaccharides (HDOs) interact with the cytoplasmic domain of PLB and consequently stimulate SERCA activity. These results indicate that the cytoplasmic domain of PLB is functionally important and could be a valid target for compounds with drug-like properties.",
keywords = "Animals, Calcium-Binding Proteins, Cytoplasm, Heparin, Oligosaccharides, Protein Structure, Tertiary, Rabbits, Sarcoplasmic Reticulum Calcium-Transporting ATPases",
author = "Eleri Hughes and Rachel Edwards and Middleton, {David A}",
note = "Copyright {\textcopyright} 2010 Elsevier Inc. All rights reserved.",
year = "2010",
month = oct,
day = "22",
doi = "10.1016/j.bbrc.2010.09.056",
language = "English",
volume = "401",
pages = "370--5",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

RIS

TY - JOUR

T1 - Heparin-derived oligosaccharides interact with the phospholamban cytoplasmic domain and stimulate SERCA function

AU - Hughes, Eleri

AU - Edwards, Rachel

AU - Middleton, David A

N1 - Copyright © 2010 Elsevier Inc. All rights reserved.

PY - 2010/10/22

Y1 - 2010/10/22

N2 - The association between the cardiac transmembrane proteins phospholamban and sarcoplasmic reticulum Ca(2+) ATPase (SERCA2a) regulates the active transport of Ca(2+) into the sarcoplasmic reticulum (SR) lumen and controls the contraction and relaxation of the heart. Heart failure (HF) and cardiac hypertrophy have been linked to defects in Ca(2+) uptake by the cardiac SR and stimulation of calcium transport by modulation of the PLB-SERCA interaction is a potential therapy. This work is part of an effort to identify compounds that destabilise the PLB-SERCA interaction in well-defined membrane environments. It is shown that heparin-derived oligosaccharides (HDOs) interact with the cytoplasmic domain of PLB and consequently stimulate SERCA activity. These results indicate that the cytoplasmic domain of PLB is functionally important and could be a valid target for compounds with drug-like properties.

AB - The association between the cardiac transmembrane proteins phospholamban and sarcoplasmic reticulum Ca(2+) ATPase (SERCA2a) regulates the active transport of Ca(2+) into the sarcoplasmic reticulum (SR) lumen and controls the contraction and relaxation of the heart. Heart failure (HF) and cardiac hypertrophy have been linked to defects in Ca(2+) uptake by the cardiac SR and stimulation of calcium transport by modulation of the PLB-SERCA interaction is a potential therapy. This work is part of an effort to identify compounds that destabilise the PLB-SERCA interaction in well-defined membrane environments. It is shown that heparin-derived oligosaccharides (HDOs) interact with the cytoplasmic domain of PLB and consequently stimulate SERCA activity. These results indicate that the cytoplasmic domain of PLB is functionally important and could be a valid target for compounds with drug-like properties.

KW - Animals

KW - Calcium-Binding Proteins

KW - Cytoplasm

KW - Heparin

KW - Oligosaccharides

KW - Protein Structure, Tertiary

KW - Rabbits

KW - Sarcoplasmic Reticulum Calcium-Transporting ATPases

U2 - 10.1016/j.bbrc.2010.09.056

DO - 10.1016/j.bbrc.2010.09.056

M3 - Journal article

C2 - 20851101

VL - 401

SP - 370

EP - 375

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -