Modulation of sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase activity and oxidative modification during the development of adjuvant arthritis

Miriam K. Strosova, Janka Karlovska, Petronela Zizkova, Magdalena Kwolek-Mirek, Silvester Ponist, Corinne M. Spickett, Lubica Horakova

Research output: Contribution to journalArticle

Abstract

Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA. SR Ca(2+)-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site. The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca(2+) level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.
LanguageEnglish
Pages40-47
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume511
Issue number1-2
Early online date22 Apr 2011
DOIs
Publication statusPublished - Jul 2011

Fingerprint

Sarcoplasmic Reticulum Calcium-Transporting ATPases
Experimental Arthritis
Sarcoplasmic Reticulum
Endoplasmic Reticulum
Cysteine
Adenosine Triphosphatases
Fluidity
Modulation
Membrane Fluidity
Binding Sites
Fluorescence
Calsequestrin
Calcium
Nitration
Phosphatidic Acids
Fluorescein-5-isothiocyanate
Tyrosine
Muscle
Muscle Development
Rats

Keywords

  • animals
  • experimental arthritis
  • carrier proteins
  • membrane fluidity
  • skeletal muscle
  • oxidative stress
  • phosphatidic acids
  • protein carbonylation
  • protein conformation
  • post-translational protein processing
  • rats
  • inbred Lew rats
  • sarcoplasmic reticulum
  • sarcoplasmic reticulum calcium-transporting ATPases
  • sulfhydryl compounds
  • SERCA
  • free radicals
  • calsequestrin
  • nitrotyrosine
  • adjuvant arthritis

Cite this

Strosova, Miriam K. ; Karlovska, Janka ; Zizkova, Petronela ; Kwolek-Mirek, Magdalena ; Ponist, Silvester ; Spickett, Corinne M. ; Horakova, Lubica. / Modulation of sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase activity and oxidative modification during the development of adjuvant arthritis. In: Archives of Biochemistry and Biophysics. 2011 ; Vol. 511, No. 1-2. pp. 40-47.
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abstract = "Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA. SR Ca(2+)-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site. The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca(2+) level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.",
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Modulation of sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase activity and oxidative modification during the development of adjuvant arthritis. / Strosova, Miriam K.; Karlovska, Janka; Zizkova, Petronela; Kwolek-Mirek, Magdalena; Ponist, Silvester; Spickett, Corinne M.; Horakova, Lubica.

In: Archives of Biochemistry and Biophysics, Vol. 511, No. 1-2, 07.2011, p. 40-47.

Research output: Contribution to journalArticle

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T1 - Modulation of sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase activity and oxidative modification during the development of adjuvant arthritis

AU - Strosova, Miriam K.

AU - Karlovska, Janka

AU - Zizkova, Petronela

AU - Kwolek-Mirek, Magdalena

AU - Ponist, Silvester

AU - Spickett, Corinne M.

AU - Horakova, Lubica

N1 - Copyright © 2011 Elsevier Inc. All rights reserved.

PY - 2011/7

Y1 - 2011/7

N2 - Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA. SR Ca(2+)-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site. The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca(2+) level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.

AB - Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA. SR Ca(2+)-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site. The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca(2+) level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.

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KW - rats

KW - inbred Lew rats

KW - sarcoplasmic reticulum

KW - sarcoplasmic reticulum calcium-transporting ATPases

KW - sulfhydryl compounds

KW - SERCA

KW - free radicals

KW - calsequestrin

KW - nitrotyrosine

KW - adjuvant arthritis

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U2 - 10.1016/j.abb.2011.04.011

DO - 10.1016/j.abb.2011.04.011

M3 - Article

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EP - 47

JO - Archives of Biochemistry and Biophysics

T2 - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

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